Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O31611
|
YJBM_BACSU
|
MDDKQWERFLVPYRQAVEELKVKLKGIRTLYEYEDDHSPIEFVTGRVKPVASILEKARRKSIPLHEIETMQDIAGLRIMCQFVDDIQIVKEMLFARKDFTVVDQRDYIAEHKESGYRSYHLVVLYPLQTVSGEKHVLVEIQIRTLAMNFWATIEHSLNYKYSGNIPEKVKLRLQRASEAASRLDEEMSEIRGEVQEAQAAFSRKKKGSEQQ
|
2.7.6.5
| null |
guanosine tetraphosphate biosynthetic process [GO:0015970]; phosphorylation [GO:0016310]
| null |
ATP binding [GO:0005524]; GTP binding [GO:0005525]; GTP diphosphokinase activity [GO:0008728]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]
|
PF04607;
|
3.30.460.10;1.10.287.860;
|
RelA/SpoT family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate; Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5; Evidence={ECO:0000269|PubMed:26460002}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22089; Evidence={ECO:0000305|PubMed:26460002}; CATALYTIC ACTIVITY: Reaction=ATP + GDP = AMP + guanosine 3',5'-bis(diphosphate); Xref=Rhea:RHEA:28098, ChEBI:CHEBI:30616, ChEBI:CHEBI:58189, ChEBI:CHEBI:77828, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:26460002}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28099; Evidence={ECO:0000305|PubMed:26460002};
| null |
PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step 1/2.
| null | null |
FUNCTION: Functions as a (p)ppGpp synthase; GDP can be used instead of GTP, resulting in an increase of (p)ppGpp synthesis (PubMed:18067544). The enzyme binds ATP, then GDP or GTP and catalysis is highly cooperative (PubMed:26460002). In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. Probably has a minor role in the stringent response (PubMed:18067544). {ECO:0000269|PubMed:18067544, ECO:0000269|PubMed:26460002}.
|
Bacillus subtilis (strain 168)
|
O31612
|
NADK1_BACSU
|
MKFAVSSKGDQVSDTLKSKIQAYLLDFDMELDENEPEIVISVGGDGTLLYAFHRYSDRLDKTAFVGVHTGHLGFYADWVPHEIEKLVLAIAKTPYHTVEYPLLEVIVTYHENEREERYLALNECTIKSIEGSLVADVEIKGQLFETFRGDGLCLSTPSGSTAYNKALGGAIIHPSIRAIQLAEMASINNRVFRTVGSPLLLPSHHDCMIKPRNEVDFQVTIDHLTLLHKDVKSIRCQVASEKVRFARFRPFPFWKRVQDSFIGKGE
|
2.7.1.23
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:12897004}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:12897004}; Note=Divalent metal ions. Both Ca(2+) and Mn(2+) ions are more effective activators than zinc, cobalt, copper and magnesium ions at low concentrations. {ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:12897004};
|
NAD metabolic process [GO:0019674]; NADP biosynthetic process [GO:0006741]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; NAD+ kinase activity [GO:0003951]
|
PF01513;PF20143;
| null |
NAD kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}.
|
CATALYTIC ACTIVITY: Reaction=ATP + NAD(+) = ADP + H(+) + NADP(+); Xref=Rhea:RHEA:18629, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57540, ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; EC=2.7.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:12897004};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.73 mM for NAD (at pH 7.8 and 25 degrees Celsius) {ECO:0000269|PubMed:12897004}; Vmax=3.82 umol/min/mg enzyme (at pH 7.8 and 25 degrees Celsius) {ECO:0000269|PubMed:12897004}; Note=kcat is 8 sec(-1) for kinase activity with NAD (at pH 7.8 and 25 degrees Celsius).;
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. {ECO:0000269|PubMed:12897004};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. Half of the activity is lost after treatment at 40 degrees Celsius for 15 minutes. {ECO:0000269|PubMed:12897004};
|
FUNCTION: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates (GTP, UTP) as well as inorganic polyphosphate (poly(P)) as a source of phosphorus. {ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:12897004}.
|
Bacillus subtilis (strain 168)
|
O31616
|
GLYOX_BACSU
|
MKRHYEAVVIGGGIIGSAIAYYLAKENKNTALFESGTMGGRTTSAAAGMLGAHAECEERDAFFDFAMHSQRLYKGLGEELYALSGVDIRQHNGGMFKLAFSEEDVLQLRQMDDLDSVSWYSKEEVLEKEPYASGDIFGASFIQDDVHVEPYFVCKAYVKAAKMLGAEIFEHTPVLHVERDGEALFIKTPSGDVWANHVVVASGVWSGMFFKQLGLNNAFLPVKGECLSVWNDDIPLTKTLYHDHCYIVPRKSGRLVVGATMKPGDWSETPDLGGLESVMKKAKTMLPAIQNMKVDRFWAGLRPGTKDGKPYIGRHPEDSRILFAAGHFRNGILLAPATGALISDLIMNKEVNQDWLHAFRIDRKEAVQI
|
1.4.3.19
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:11744710}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11744710};
|
amino acid metabolic process [GO:0006520]; response to herbicide [GO:0009635]; thiamine biosynthetic process [GO:0009228]; thiamine diphosphate biosynthetic process [GO:0009229]
|
cytoplasm [GO:0005737]
|
FAD binding [GO:0071949]; glycine oxidase activity [GO:0043799]; oxidoreductase activity [GO:0016491]
|
PF01266;
|
3.30.9.10;3.50.50.60;
|
DAO family, ThiO subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=glycine + H2O + O2 = glyoxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:11532, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305; EC=1.4.3.19; Evidence={ECO:0000269|PubMed:11744710, ECO:0000269|PubMed:19864430, ECO:0000269|PubMed:9827558}; CATALYTIC ACTIVITY: Reaction=H2O + N-ethylglycine + O2 = ethylamine + glyoxylate + H2O2; Xref=Rhea:RHEA:12472, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:36655, ChEBI:CHEBI:57440, ChEBI:CHEBI:566789; EC=1.4.3.19; Evidence={ECO:0000269|PubMed:11744710, ECO:0000269|PubMed:19864430, ECO:0000269|PubMed:9827558}; CATALYTIC ACTIVITY: Reaction=H2O + O2 + sarcosine = glyoxylate + H2O2 + methylamine; Xref=Rhea:RHEA:15165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:36655, ChEBI:CHEBI:57433, ChEBI:CHEBI:59338; EC=1.4.3.19; Evidence={ECO:0000269|PubMed:11744710, ECO:0000269|PubMed:19864430, ECO:0000269|PubMed:9827558}; CATALYTIC ACTIVITY: Reaction=D-alanine + H2O + O2 = H2O2 + NH4(+) + pyruvate; Xref=Rhea:RHEA:22688, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57416; EC=1.4.3.19; Evidence={ECO:0000269|PubMed:11744710, ECO:0000269|PubMed:19864430, ECO:0000269|PubMed:9827558}; CATALYTIC ACTIVITY: Reaction=glyphosate + H2O + O2 = aminomethylphosphonate + glyoxylate + H(+) + H2O2; Xref=Rhea:RHEA:52740, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:36655, ChEBI:CHEBI:133673, ChEBI:CHEBI:133674; Evidence={ECO:0000269|PubMed:19864430};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.22 mM for sarcosine (at pH 8.0) {ECO:0000269|PubMed:9827558}; KM=0.66 mM for N-ethylglycine (at pH 8.0) {ECO:0000269|PubMed:9827558}; KM=0.99 mM for glycine (at pH 8.0) {ECO:0000269|PubMed:9827558}; KM=46 mM for D-proline (at pH 8.0) {ECO:0000269|PubMed:9827558}; KM=81 mM for D-alanine (at pH 8.0) {ECO:0000269|PubMed:9827558}; KM=0.7 mM for glycine (at pH 8.5 and 37 degrees Celsius) {ECO:0000269|PubMed:19864430}; KM=87 mM for glyphosate (at pH 8.5 and 37 degrees Celsius) {ECO:0000269|PubMed:19864430}; Note=kcat is 1.3 sec(-1) with glycine as substrate. kcat is 1.6 sec(-1) with sarcosine as substrate. kcat is 1.4 sec(-1) with N-ethylglycine as substrate. kcat is 1.3 sec(-1) with D-proline as substrate. kcat is 1.1 sec(-1) with D-alanine as substrate (at pH 8.0) (PubMed:9827558). kcat is 0.60 sec(-1) with glycine as substrate. kcat is 0.91 sec(-1) with glyphosate as substrate (at pH 8.5 and 37 degrees Celsius) (PubMed:19864430). {ECO:0000269|PubMed:19864430, ECO:0000269|PubMed:9827558};
|
PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. {ECO:0000269|PubMed:12627963}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:9827558};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:9827558};
|
FUNCTION: Catalyzes the FAD-dependent oxidative deamination of various amines and D-amino acids to yield the corresponding alpha-keto acids, ammonia/amine, and hydrogen peroxide. Oxidizes sarcosine (N-methylglycine), N-ethylglycine and glycine (PubMed:11744710, PubMed:19864430, PubMed:9827558). Can also oxidize the herbicide glyphosate (N-phosphonomethylglycine) (PubMed:19864430). Displays lower activities on D-alanine, D-valine, D-proline and D-methionine (PubMed:11744710, PubMed:9827558). Does not act on L-amino acids and other D-amino acids (PubMed:9827558). Is essential for thiamine biosynthesis since the oxidation of glycine catalyzed by ThiO generates the glycine imine intermediate (dehydroglycine) required for the biosynthesis of the thiazole ring of thiamine pyrophosphate (PubMed:12627963). {ECO:0000269|PubMed:11744710, ECO:0000269|PubMed:12627963, ECO:0000269|PubMed:19864430, ECO:0000269|PubMed:9827558}.
|
Bacillus subtilis (strain 168)
|
O31644
|
MANR_BACSU
|
MEYINTRQKEILYLLLSEPDDYLVVQDFADRVQCSEKTIRNDLKVIEDYLNEHSHAQLIRKPGLGVYLHIEEQERTWLSQQLHTEHFSSRQRSDKERMLHIAYDLLMNPKPVSAKDIAARHFVNRSSIKKDLYAVEEWLKRFDLTLVSRQRLGLKVEGNERNKRKALARISDLIHNTAFTSQFIKSKFLHYEVDFVTKEIKSLQKKHSLYFTDETFESLLLHTLLMVRRIKMKQPISLSPKEMAAVKKKKEYQWTFACLQRLEPVFAIRFPEEEAVYLTLHILGGKVRYPLQTEENLENAVLPKVVGHLINRVSELKMMDFHKDQDLINGLNIHLNTVLQRLSYDLSVANPMLNDIKKMYPYLFHLIIDVLEDINQTFDLHIPEEEAAYLTLHFQAAIERMQGSSETHKKAVIVCHMGIGMSQLLRTKIERKYHQIAVMACIAKADLKDYIKKHEDIDLVISTIALENITVPHIVVSPLLEPGEEKKLSAFIRQLGESHRQKQKTFQMLNNTTPFLVFLQQEAEHRYKLIEQLATALFEKGYVDKDYAVHAVMREKMSATNIGSGIAIPHANAKFIKQSAIAIATLKEPLEWGNEKVSLVFMLAVKHEDQTMTKQLFSELSYLSEQPAFVQKLTKETNVMTFLSHLDY
|
2.7.1.191
| null |
phosphoenolpyruvate-dependent sugar phosphotransferase system [GO:0009401]; phosphorylation [GO:0016310]; regulation of DNA-templated transcription [GO:0006355]
| null |
DNA binding [GO:0003677]; kinase activity [GO:0016301]; protein-N(PI)-phosphohistidine-sugar phosphotransferase activity [GO:0008982]
|
PF08279;PF05043;PF00874;PF00359;
|
3.40.50.2300;1.10.1790.10;1.10.10.10;
|
Transcriptional antiterminator BglG family
| null | null |
CATALYTIC ACTIVITY: Reaction=D-mannose(out) + N(pros)-phospho-L-histidyl-[protein] = D-mannose 6-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:49232, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:4208, ChEBI:CHEBI:29979, ChEBI:CHEBI:58735, ChEBI:CHEBI:64837; EC=2.7.1.191;
| null | null | null | null |
FUNCTION: Positively regulates the expression of the mannose operon that consists of three genes, manP, manA, and yjdF, which are responsible for the transport and utilization of mannose. Also activates its own expression. {ECO:0000269|PubMed:20139185, ECO:0000269|PubMed:23551403}.
|
Bacillus subtilis (strain 168)
|
O31645
|
PTN3B_BACSU
|
MKLLAITSCPNGIAHTYMAAENLQKAADRLGVSIKVETQGGIGVENKLTEEEIREADAIIIAADRSVNKDRFIGKKLLSVGVQDGIRKPEELIQKALNGDIPVYRSATKSESGNHQEKKQNPIYRHLMNGVSFMVPFIVVGGLLIAVALTLGGEKTPKGLVIPDDSFWKTIEQIGSASFSFMIPILAGYIAYSIADKPGLVPGMIGGYIAATGSFYDSASGAGFLGGIIAGFLAGYAALWIKKLKVPKAIQPIMPIIIIPVFASLIVGLAFVFLIGAPVAQIFASLTVWLAGMKGSSSILLALILGAMISFDMGGPVNKVAFLFGSAMIGEGNYEIMGPIAVAICIPPIGLGIATFLGKRKFEASQREMGKAAFTMGLFGITEGAIPFAAQDPLRVIPSIMAGSMTGSVIAMIGNVGDRVAHGGPIVAVLGAVDHVLMFFIAVIAGSLVTALFVNVLKKDITASPVLSETAPTSAPSEAAAANEIKQPIQSQKAEMSEFKKLTDIISPELIEPNLSGETSDDIIDELIQKLSRRGALLSESGFKQAILNREQQGTTAIGMNIAIPHGKSEAVREPSVAFGIKRSGVDWNSLDGSEAKLIFMIAVPKESGGNQHLKILQMLSRKLMDDNYRERLLSVQTTEEAYKLLEEIE
|
2.7.1.191
| null |
phosphoenolpyruvate-dependent sugar phosphotransferase system [GO:0009401]; phosphorylation [GO:0016310]
|
plasma membrane [GO:0005886]
|
carbohydrate:proton symporter activity [GO:0005351]; kinase activity [GO:0016301]; protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity [GO:0022877]; protein-phosphocysteine-sugar phosphotransferase activity [GO:0090563]
|
PF00359;PF02378;PF02302;
|
3.40.50.2300;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00427}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00427}.
|
CATALYTIC ACTIVITY: Reaction=D-mannose(out) + N(pros)-phospho-L-histidyl-[protein] = D-mannose 6-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:49232, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:4208, ChEBI:CHEBI:29979, ChEBI:CHEBI:58735, ChEBI:CHEBI:64837; EC=2.7.1.191;
| null | null | null | null |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in mannose transport.
|
Bacillus subtilis (strain 168)
|
O31662
|
MTNA_BACSU
|
MTHSFAVPRSVEWKETAITILNQQKLPDETEYLELTTKEDVFDAIVTLKVRGAPAIGITAAFGLALAAKDIETDNVTEFRRRLEDIKQYLNSSRPTAINLSWALERLSHSVENAISVNEAKTNLVHEAIQIQVEDEETCRLIGQNALQLFKKGDRIMTICNAGSIATSRYGTALAPFYLAKQKDLGLHIYACETRPVLQGSRLTAWELMQGGIDVTLITDSMAAHTMKEKQISAVIVGADRIAKNGDTANKIGTYGLAILANAFDIPFFVAAPLSTFDTKVKCGADIPIEERDPEEVRQISGVRTAPSNVPVFNPAFDITPHDLISGIITEKGIMTGNYEEEIEQLFKGEKVH
|
5.3.1.23
| null |
L-methionine salvage from methylthioadenosine [GO:0019509]; L-methionine salvage from S-adenosylmethionine [GO:0019284]
| null |
S-methyl-5-thioribose-1-phosphate isomerase activity [GO:0046523]
|
PF01008;
|
1.20.120.420;
|
EIF-2B alpha/beta/delta subunits family, MtnA subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate; Xref=Rhea:RHEA:19989, ChEBI:CHEBI:58533, ChEBI:CHEBI:58548; EC=5.3.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01678};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=138 uM for methylthioribose-1-phosphate (at pH 8.5 and 35 degrees Celsius) {ECO:0000269|PubMed:17690466}; Vmax=20.4 umol/min/mg enzyme (at pH 8.5 and 35 degrees Celsius) {ECO:0000269|PubMed:17690466};
|
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 1/6. {ECO:0000255|HAMAP-Rule:MF_01678}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.1. {ECO:0000269|PubMed:17690466};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:17690466};
|
FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). {ECO:0000255|HAMAP-Rule:MF_01678, ECO:0000269|PubMed:14551435}.
|
Bacillus subtilis (strain 168)
|
O31677
|
QUEE_BACSU
|
MAKGIPVLEIFGPTIQGEGMVIGQKTMFVRTAGCDYSCSWCDSAFTWDGSAKKDIRWMTAEEIFAELKDIGGDAFSHVTISGGNPALLKQLDAFIELLKENNIRAALETQGTVYQDWFTLIDDLTISPKPPSSKMVTNFQKLDHILTSLQENDRQHAVSLKVVIFNDEDLEFAKTVHKRYPGIPFYLQVGNDDVHTTDDQSLIAHLLGKYEALVDKVAVDAELNLVRVLPQLHTLLWGNKRGV
|
4.3.99.3
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:23194065, ECO:0000305|PubMed:19354300}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000269|PubMed:23194065, ECO:0000305|PubMed:19354300}; COFACTOR: Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789; Evidence={ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:19354300, ECO:0000269|PubMed:23194065}; Note=Binds 1 S-adenosyl-L-methionine per subunit. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:19354300, ECO:0000269|PubMed:23194065}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:23194065};
|
queuosine biosynthetic process [GO:0008616]
| null |
4 iron, 4 sulfur cluster binding [GO:0051539]; carbon-nitrogen lyase activity [GO:0016840]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]; S-adenosyl-L-methionine binding [GO:1904047]
|
PF13353;PF04055;
|
3.20.20.70;
|
Radical SAM superfamily, 7-carboxy-7-deazaguanine synthase family
| null | null |
CATALYTIC ACTIVITY: Reaction=6-carboxy-5,6,7,8-tetrahydropterin + H(+) = 7-carboxy-7-deazaguanine + NH4(+); Xref=Rhea:RHEA:27974, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:61032, ChEBI:CHEBI:61036; EC=4.3.99.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:19354300, ECO:0000269|PubMed:23194065};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for 6-carboxy-5,6,7,8-tetrahydropterin {ECO:0000269|PubMed:23194065}; Note=kcat is 5.4 min(-1). {ECO:0000269|PubMed:23194065};
|
PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:19354300}.
| null | null |
FUNCTION: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000269|PubMed:14660578, ECO:0000269|PubMed:19354300, ECO:0000269|PubMed:23194065}.
|
Bacillus subtilis (strain 168)
|
O31678
|
QUEF_BACSU
|
MTTRKESELEGVTLLGNQGTNYLFEYAPDVLESFPNKHVNRDYFVKFNCPEFTSLCPKTGQPDFATIYISYIPDEKMVESKSLKLYLFSFRNHGDFHEDCMNIIMNDLIELMDPRYIEVWGKFTPRGGISIDPYTNYGKPGTKYEKMAEYRMMNHDLYPETIDNR
|
1.7.1.13
|
COFACTOR: Note=Does not require a metal cofactor.;
|
queuosine biosynthetic process [GO:0008616]
|
cytoplasm [GO:0005737]
|
metal ion binding [GO:0046872]; preQ1 synthase activity [GO:0033739]
|
PF14489;
|
3.30.1130.10;
|
GTP cyclohydrolase I family, QueF type 1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH; Xref=Rhea:RHEA:13409, ChEBI:CHEBI:15378, ChEBI:CHEBI:45075, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58703; EC=1.7.1.13; Evidence={ECO:0000269|PubMed:17929836};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.237 uM for 7-cyano-7-deazaguanine (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:17929836}; KM=19.2 uM for NADPH (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:17929836}; Note=kcat is 0.66 min(-1) (at pH 7.5 and 30 degrees Celsius).;
|
PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:17929836};
| null |
FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1), a late step in the queuosine pathway. {ECO:0000269|PubMed:15767583, ECO:0000269|PubMed:17929836}.
|
Bacillus subtilis (strain 168)
|
O31691
|
GLCT_BACSU
|
MNGSFTVKKVLNNNVLIASHHKYSEVVLIGKGIGFGKKQDDVIEDKGYDKMFILKDEKEQKQFKKLLDYVDEKLVDISNDVIYHISNRTNHSLNEHIHIALTDHIAFAIKRQQQGFDMKNPFLMETQSLYPEEYQIAKEVIDMINEKAGLCLPEGEIGFIALHIHSALTNRPLSEVNQHSQLMAQLVEVIEDSFQMKVNKESVNYLRLIRHIRFTIERIKKEEPTKEPEKLMLLLKNEYPLCYNTAWKLIKILQQTLKKPVHEAEAVYLTLHLYRLTNKIS
| null | null |
positive regulation of DNA-templated transcription [GO:0045893]
| null |
RNA binding [GO:0003723]
|
PF03123;PF00874;
|
1.20.58.1950;1.20.890.100;2.30.24.10;1.10.1790.10;
|
Transcriptional antiterminator BglG family, GlcT subfamily
|
PTM: Phosphorylated by HPr (PtsH) and EII-Glc (PtsG). HPr phosphorylates the PRD 2 domain which has a slight stimulatory effect on GlcT activity, while EII-Glc phosphorylates the PRD 1 domain which inactivates GlcT. The phosphorylation is dependent on the presence or absence of glucose which acts as an inducer of the ptsGHI operon expression. In the presence of glucose the phosphoryl group is transferred from phosphorylated HPr to the sugar via EII-Glc. Under these conditions GlcT is not phosphorylated and binds to the RAT sequence, thus allowing transcription of the ptsGHI operon. In the absence of glucose, phosphorylated EII-Glc accumulates in the cell and phosphorylates the PRD 1 domain of GlcT, leading to its inactivation; this phosphorylation may prevent dimerization of GlcT. {ECO:0000269|PubMed:14527945, ECO:0000269|PubMed:9765562}.
| null | null | null | null | null | null |
FUNCTION: Mediates the positive regulation of the glucose PTS operon (ptsGHI) by functioning as an antiterminator factor of transcription via its interaction with the RNA-antiterminator (RAT) sequence located upstream of the ptsG gene. The RNA-binding domain of GlcT directly binds to the RNA antiterminator (RAT) sequence and prevents transcriptional termination. GlcT binding requires two identical and nearly symmetrical triple base pairings in the RAT sequence. {ECO:0000269|PubMed:11902727, ECO:0000269|PubMed:9765562}.
|
Bacillus subtilis (strain 168)
|
O31718
|
RPOY_BACSU
|
MIYKVFYQEKADEVPVREKTDSLYIEGVSERDVRTKLKEKKFNIEFITPVDGAFLEYEQQSENFKVLEL
|
2.7.7.6
| null |
DNA-templated transcription [GO:0006351]
|
cytoplasm [GO:0005737]; DNA-directed RNA polymerase complex [GO:0000428]; nucleoid [GO:0009295]
|
DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]
|
PF07288;
|
3.10.20.730;
|
RNA polymerase subunit epsilon family
| null |
SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:25092033}. Note=Colocalizes with RNAP. {ECO:0000269|PubMed:25092033}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01553};
| null | null | null | null |
FUNCTION: A non-essential component of RNA polymerase (RNAP) (PubMed:18289874, PubMed:21710567, PubMed:25092033, PubMed:6802805). Has a similar structure to bacteriophage T7 protein Gp2 (AC P03704), which is known to bind to RNAP in the DNA binding-cleft. Unlike Gp2 however, this protein does not inhibit transcription initiation (PubMed:25092033). In vitro reconstitution experiments show this subunit is dispensible (PubMed:18289874). {ECO:0000269|PubMed:18289874, ECO:0000269|PubMed:21710567, ECO:0000269|PubMed:25092033, ECO:0000269|PubMed:6802805}.
|
Bacillus subtilis (strain 168)
|
O31749
|
PYRH_BACSU
|
MEKPKYKRIVLKLSGEALAGEQGNGINPTVIQSIAKQVKEIAELEVEVAVVVGGGNLWRGKTGSDLGMDRATADYMGMLATVMNSLALQDSLETLGIQSRVQTSIEMRQVAEPYIRRKAIRHLEKKRVVIFAAGTGNPYFSTDTTAALRAAEIEADVILMAKNNVDGVYNADPRKDESAVKYESLSYLDVLKDGLEVMDSTASSLCMDNDIPLIVFSIMEEGNIKRAVIGESIGTIVRGK
|
2.7.4.22
| null |
'de novo' CTP biosynthetic process [GO:0044210]; phosphorylation [GO:0016310]; UDP biosynthetic process [GO:0006225]
|
cytosol [GO:0005829]
|
ATP binding [GO:0005524]; UMP kinase activity [GO:0033862]
|
PF00696;
|
3.40.1160.10;
|
UMP kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15018105}. Note=Is predominantly localized near the bacterial membranes.
|
CATALYTIC ACTIVITY: Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400, ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223, ChEBI:CHEBI:456216; EC=2.7.4.22;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.9 mM for ATP {ECO:0000269|PubMed:12869195, ECO:0000269|PubMed:17210578}; KM=8 uM for UMP (in the absence of GTP) {ECO:0000269|PubMed:12869195, ECO:0000269|PubMed:17210578}; KM=30 uM for UMP (in the presence of GTP) {ECO:0000269|PubMed:12869195, ECO:0000269|PubMed:17210578}; KM=120 uM for 5-fluoro-UMP {ECO:0000269|PubMed:12869195, ECO:0000269|PubMed:17210578}; KM=140 uM for 6-aza-UMP {ECO:0000269|PubMed:12869195, ECO:0000269|PubMed:17210578}; Vmax=25 umol/min/mg enzyme with UMP as substrate {ECO:0000269|PubMed:12869195, ECO:0000269|PubMed:17210578}; Vmax=24 umol/min/mg enzyme with 5-fluoro-UMP as substrate {ECO:0000269|PubMed:12869195, ECO:0000269|PubMed:17210578}; Vmax=0.6 umol/min/mg enzyme with 6-aza-UMP as substrate {ECO:0000269|PubMed:12869195, ECO:0000269|PubMed:17210578}; Note=In the absence of GTP, the activity is less than 10% of its maximum activity. Is unstable in the absence of UTP. Positive cooperativity is observed with ATP as variable substrate, but it is strongly reduced in the presence of GTP. GTP enhances the affinity for ATP whereas UTP decreases it.;
|
PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
| null | null |
FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP, with ATP or dATP as the most efficient phosphate donors. Is also able to phosphorylate 5-fluoro-UMP and 6-aza-UMP. {ECO:0000269|PubMed:12869195, ECO:0000269|PubMed:15018105}.
|
Bacillus subtilis (strain 168)
|
O31760
|
RNJ2_BACSU
|
MKKKNTENVRIIALGGVGEIGKNLYVIEIDSDIFVVDAGLMHPENEMLGIDVVIPDISYLIERADRVKAIFLTHGHDENIGGVFYLLNKLSVPVYGTKLTLALLREKLKQYGHNRKTDLREIHSKSVITFESTKVSFFRTIHSIPDSVGVSFKTSLGSIVCTGDFKFDQTPALNQTCDIGEIAKIGNSGVLALLSDSANAERPGYTPSEAAVSGEISDALYNSQNRVIIAVFASNINRIQQVIHAAAQNGRKIAVAGKNLQSVLQLARKLGYIEADDELFISVQDVKKYPKREVAIITAGSQGEPLAALTRMANKAHKQLNIEEGDTVVIASTPIPGQELIYSKTVDLLARAGAQVIFAQKRVHVSGHGSQEELKLMINLLKPKYLIPVNGEYRMQKAHSKIAEETGMKRSDIFLIEKGDVVEFRGQNVKIGDKVPYGNILIDGLGVGDIGNIVLRDRRLLSQDGILIVVITLDKQKKHLVSGPEIITRGFVYVRESEGLIVQATELVRSIVTEATETSNVEWSTLKQAMRDALNQFLYEKTKRKPMIIPIIMEV
|
3.1.-.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250, ECO:0000269|PubMed:15831787, ECO:0000269|PubMed:21893285}; Note=Binds 1 zinc ion per subunit. The inability to bind a second zinc ion may explain its very poor exonuclease activity (PubMed:21893285). {ECO:0000250, ECO:0000269|PubMed:15831787, ECO:0000269|PubMed:21893285};
|
mRNA processing [GO:0006397]; rRNA processing [GO:0006364]
|
cytoplasm [GO:0005737]
|
5'-3' RNA exonuclease activity [GO:0004534]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521]; zinc ion binding [GO:0008270]
|
PF00753;PF07521;PF17770;
|
3.10.20.580;3.40.50.10710;3.60.15.10;
|
Metallo-beta-lactamase superfamily, RNA-metabolizing metallo-beta-lactamase-like family, Bacterial RNase J subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491, ECO:0000269|PubMed:15831787}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.96 uM for exonuclease on 30 nt RNA hybridized to 17 nt quenching DNA, J2 alone {ECO:0000269|PubMed:20025672}; KM=0.22 uM for exonuclease on 30 nt RNA hybridized to 17 nt quenching DNA, J1/J2 complex {ECO:0000269|PubMed:20025672}; Note=kcat is 0.58 sec(-1) for J1, 0.13 sec(-1) for J1/J2 and <0.005 sec(-1) for J2.;
| null | null | null |
FUNCTION: Endonucleolytically cleaves the 5'-leader sequence of certain mRNAs. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2 complex is highly processive on substrates longer than 5 nucleotides, on shorter substrates is distributive. Plays a role in mRNA maturation and stability. Appears to have a limited effect on 16S rRNA maturation, despite its similarity to RNase J1. This subunit alone has very poor 5'-3' exonuclease activity. {ECO:0000269|PubMed:15831787, ECO:0000269|PubMed:17229210, ECO:0000269|PubMed:18445592, ECO:0000269|PubMed:18713320, ECO:0000269|PubMed:20025672, ECO:0000269|PubMed:21893286}.
|
Bacillus subtilis (strain 168)
|
O31774
|
RNY_BACSU
|
MTPIMMVLISILLILLGLVVGYFVRKTIAEAKIAGARGAAEQILEDAKRDAEALKKEALLEAKDEIHKLRIDAEQEVRERRNELQKQENRLLQKEENLDRKHEGIDKREAMLEKKDHSLNERQQHIEEMESKVDEMIRMQQSELERISSLTRDEAKQIILERVENELSHDIAIMTKETENRAKEEADKKAKNILSLALQRCAADHVAETTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIRRETARIALDKLVQDGRIHPARIEEMVEKSRREVDDYIREMGEQTTFEVGVHGLHPDLIKILGRLKFRTSYGQNVLKHSMEVAFLAGLMASELGEDAKLAKRAGLLHDIGKAIDHEVEGSHVEIGVELATKYKEHPVVINSIASHHGDEEPTSIIAVLVAAADALSAARPGARSETLENYIRRLEKLEEISESYEGVEKSFAIQAGREVRIMVKPDSINDLEAHRLARDIRKRIEDELDYPGHIKVTVIRETRAVEYAK
|
3.1.-.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19779461}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19779461}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19779461}; Note=Magnesium. Can also use manganese or zinc. {ECO:0000269|PubMed:19779461};
|
mRNA catabolic process [GO:0006402]; mRNA processing [GO:0006397]
|
plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521]
|
PF01966;PF00013;PF12072;
|
1.10.3210.10;3.30.1370.10;
|
RNase Y family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20572937}; Single-pass membrane protein {ECO:0000269|PubMed:20572937}. Note=Dispersed along membrane with a few foci at septation sites and cell poles; in the absence of dynA fewer foci are seen, in the absence of minJ no foci are seen. {ECO:0000269|PubMed:23060960}.
| null | null | null | null | null |
FUNCTION: Endoribonuclease that initiates mRNA decay. Initiates the decay of all SAM-dependent riboswitches, such as yitJ riboswitch. Involved in processing of the gapA operon mRNA, it cleaves between cggR and gapA (PubMed:19193632). Is also the decay-initiating endonuclease for rpsO mRNA. Involved in degradation of type I toxin-antitoxin system bsrG/SR4 RNAs and a minor role in degradation of type I toxin-antitoxin system bsrE/SR5 degradation (PubMed:22229825, PubMed:26940229). {ECO:0000269|PubMed:19193632, ECO:0000269|PubMed:19779461, ECO:0000269|PubMed:20418391, ECO:0000269|PubMed:22229825, ECO:0000269|PubMed:22412379, ECO:0000269|PubMed:23504012, ECO:0000269|PubMed:26940229}.
|
Bacillus subtilis (strain 168)
|
O31775
|
YMDB_BACSU
|
MRILFIGDVVGSPGRDMVKEYVPKLKTKYKPHFTIINGENAAHGKGLTEKIYHSLIQSGADAITMGNHTWDKKEIFDFIDDVPNLVRPANFPEGTPGKGITYVKANGKELAVINLQGRTFLPPLDDPFLKADELIAEAAKRTPYIFIDFHAEATSEKLALGWYTDGRASAVVGTHTHVQTADNRILPKGTAYITDVGMTGPYDGILGMDRETIIKRFKTNLPVRFTVAEGKTTLSGVVIDIDDQTKKAVKIERILINDDHMFFE
|
3.1.4.16
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:24163345}; Note=Corresponds to iron 2 in the structure. {ECO:0000305|PubMed:24163345}; COFACTOR: Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000269|PubMed:24163345}; Note=Corresponds to iron 1 in the structure. {ECO:0000305|PubMed:24163345};
| null |
cytoplasm [GO:0005737]
|
2',3'-cyclic-nucleotide 2'-phosphodiesterase activity [GO:0008663]; 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity [GO:0004113]; metal ion binding [GO:0046872]
|
PF13277;
|
3.60.21.10;
|
YmdB-like family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26906740}. Note=Localizes to the cytoplasm, cell periphery and nanotubes. {ECO:0000269|PubMed:26906740}.
|
CATALYTIC ACTIVITY: Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 3'-phosphate + H(+); Xref=Rhea:RHEA:19621, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:66949, ChEBI:CHEBI:66954; EC=3.1.4.16; Evidence={ECO:0000269|PubMed:24163345};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for 2',3'-cAMP {ECO:0000269|PubMed:24163345}; KM=0.29 mM for 2',3'-cGMP {ECO:0000269|PubMed:24163345}; KM=1.3 mM for 3',5'-cAMP {ECO:0000269|PubMed:24163345}; KM=0.85 mM for 3',5'-cGMP {ECO:0000269|PubMed:24163345}; KM=0.94 mM for bis-pNPP {ECO:0000269|PubMed:24163345}; Vmax=0.83 umol/min/mg enzyme with 2',3'-cAMP as substrate {ECO:0000269|PubMed:24163345}; Vmax=1.02 umol/min/mg enzyme with 2',3'-cGMP as substrate {ECO:0000269|PubMed:24163345}; Vmax=0.45 umol/min/mg enzyme with 3',5'-cAMP as substrate {ECO:0000269|PubMed:24163345}; Vmax=0.37 umol/min/mg enzyme with 3',5'-cGMP as substrate {ECO:0000269|PubMed:24163345}; Vmax=105 umol/min/mg enzyme with bis-pNPP as substrate {ECO:0000269|PubMed:24163345}; Note=kcat is 15.0 min(-1) with 2',3'-cAMP as substrate. kcat is 22.1 min(-1) with 2',3'-cGMP as substrate. kcat is 9.2 min(-1) with 3',5'-cAMP as substrate. kcat is 7.7 min(-1) with 3',5'-cGMP as substrate. {ECO:0000269|PubMed:24163345};
| null | null | null |
FUNCTION: Plays a central, regulatory role in the late adaptive responses and affects the levels of many genes (PubMed:24163345). May act via regulation of cAMP levels (PubMed:26904951). Decreases the expression of motility genes and induces genes involved in biofilm formation, by controlling the expression of SlrR (PubMed:21856853). Required for formation of intercellular nanotubes that bridge neighboring cells to allow molecular exchange (PubMed:26906740). Plays a key role in directing the early stages of colony development (PubMed:26904951). In vitro, has a metal-dependent phosphodiesterase activity against 2',3'-cAMP and 2',3'-cGMP. Has also 3',5'-cyclic-nucleotide phosphodiesterase activity, but cannot use cyclic di-AMP or cyclic di-GMP, and does not have phosphatase activity (PubMed:24163345). {ECO:0000269|PubMed:21856853, ECO:0000269|PubMed:24163345, ECO:0000269|PubMed:26904951, ECO:0000269|PubMed:26906740, ECO:0000305|PubMed:26904951}.
|
Bacillus subtilis (strain 168)
|
O31851
|
YOJM_BACSU
|
MHRLLLLMMLTALGVAGCGQKKPPDPPNRVPEKKVVETSAFGHHVQLVNREGKAVGFIEIKESDDEGLDIHISANSLRPGASLGFHIYEKGSCVRPDFESAGGPFNPLNKEHGFNNPMGHHAGDLPNLEVGADGKVDVIMNAPDTSLKKGSKLNILDEDGSAFIIHEQADDYLTNPSGNSGARIVCGALLGNNEKQ
| null |
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per homodimer. The zinc ion is bound between 2 subunits and mediates dimerization.;
|
removal of superoxide radicals [GO:0019430]
|
extracellular space [GO:0005615]; periplasmic space [GO:0042597]; plasma membrane [GO:0005886]
|
copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; ion binding [GO:0043167]; superoxide dismutase activity [GO:0004784]; zinc ion binding [GO:0008270]
|
PF13627;PF00080;
|
2.60.40.200;
|
Cu-Zn superoxide dismutase family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
| null | null | null | null | null | null |
Bacillus subtilis (strain 168)
|
O31854
|
CDAS_BACSU
|
MKAMRYEQISENAFKGKIQVYLEQILGDASLILKTLHEKDQCLLCELDDLGHVFQDMQGIASSFYLQSYIEEFTPAFIELAKAIKALSEHKHGALIVIERADPVERFIQKGTSLHAEISSSLIESIFFPGNPLHDGALLVRENKLVSAANVLPLTTKEVDIHLGTRHRAALGMSGYTDALVLVVSEETGKMSFAKDGVLYPLISPRT
|
2.7.7.85
| null |
cAMP biosynthetic process [GO:0006171]
| null |
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; diadenylate cyclase activity [GO:0106408]
|
PF10372;PF02457;
|
3.40.1700.10;1.10.287.770;
|
Adenylate cyclase family, DacB/CdaS subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=2 ATP = 3',3'-c-di-AMP + 2 diphosphate; Xref=Rhea:RHEA:35655, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:71500; EC=2.7.7.85; Evidence={ECO:0000255|HAMAP-Rule:MF_00838};
| null | null | null | null |
FUNCTION: One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di-AMP synthesis (PubMed:23192352, PubMed:24939848). Overexpression of the hyperactive mutant (L44F) in the absence of c-di-AMP phosphodiesterase GdpP leads to growth defects in log phase (long curly cell filaments) that disappear upon sporulation; spore formation is normal, showing sporulation is insensitive to the excess c-di-AMP (PubMed:23192352). In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess. {ECO:0000269|PubMed:23192352, ECO:0000269|PubMed:24939848, ECO:0000305, ECO:0000305|PubMed:22211522}.
|
Bacillus subtilis (strain 168)
|
O32001
|
YOKF_BACSU
|
MKKVLLGFAAFTLSLSLAACSSNDSEKVSTEKETPQASTDVEKKTEQKESTKEKTADKSKEKDKKELVDVTLDRAVDGDTIKVTYNGNVDTVRYLLIDTPETKKPNSCVQPYGEDASKRNKELVNSGKLQLEFDKGDRRDKYGRLLAYVYVDGKSVQETLLKEGLARVAYVYEPNTKYIDQFKKDEQEAKSEKLSIWSKNGYVTDRGFNGCVKEKTTAVKKATTSKPAATQPTTPKASSETSTTTEKEASSETTGGTETFKNCTELRKKYPNGVPSSHPAYQSKMDRDHDNYACER
|
3.1.-.-
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:11584000}; Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:11584000}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11584000}; Note=Binds 1 Ca(2+) ion per subunit. Can also use Co(2+) or Mn(2+). {ECO:0000269|PubMed:11584000};
| null |
plasma membrane [GO:0005886]
|
endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; nuclease activity [GO:0004518]; nucleic acid binding [GO:0003676]
|
PF05901;PF00565;
|
2.40.50.90;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:11584000};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-45 degrees Celsius. {ECO:0000269|PubMed:11584000};
|
FUNCTION: Catalyzes the hydrolysis of supercoiled double and single strand DNA and RNA. Involved in chromosomal DNA degradation and cell death caused by thermal stress. {ECO:0000269|PubMed:11584000}.
|
Bacillus subtilis (strain 168)
|
O32076
|
FLOT_BACSU
|
MTMPIIMIIGVVFFLLIALIAVFITKYRTAGPDEALIVTGSYLGNKNVHVDEGGNRIKIVRGGGTFVLPVFQQAEPLSLLSSKLDVSTPEVYTEQGVPVMADGTAIIKIGGSIGEIATAAEQFLGKSKDDREQEAREVLEGHLRSILGSMTVEEIYKNREKFSQEVQRVASQDLAKMGLVIVSFTIKDVRDKNGYLESLGKPRIAQVKRDADIATAEADKETRIKRAEADKDAKKSELERATEIAEAEKINQLKMAEFRREQDTAKANADQAYDLETARARQQVTEQEMQVKIIERQKQIELEEKEILRRERQYDSEVKKKADADRYSVEQSAAAEKAKQLAEADAKKYSIEAMAKAEAEKVRIDGLAKAEAEKAKGETEAEVIRLKGLAEAEAKEKIAAAFEQYGQAAIFDMIVKMLPEYAKQAAAPLSNIDKITVVDTGGSGESSGANKVTSYATNLMSSLQESLKASSGIDVKEMLENFSGKGNVKQSINELTNEIKEAKTIQKSE
| null | null |
protein localization to plasma membrane [GO:0072659]; regulation of cell shape [GO:0008360]
|
plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]
| null |
PF01145;PF15975;
|
3.30.479.30;
|
Band 7/mec-2 family, Flotillin subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19383680, ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:25909364, ECO:0000305|PubMed:25635948}. Membrane raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23249255, ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:27362352, ECO:0000305|PubMed:19383680}. Note=Tethered to the membrane by a hairpin loop that inserts into the cell membrane (PubMed:25635948). A few foci are seen on the cell membrane during exponential growth, more are seen as cells enter stationary phase. Restricted to the mother cell during sporulation. Foci form a spiral track on the cell membrane and move in the cell. Associated with high bouyancy, cardiolipin- and phosphatidylglycerol-rich membrane fractions, association is not obligatory (PubMed:19383680). Present in detergent-resistant membrane (DRM) fractions, approximately 6 dynamic foci per cell; colocalizes with KinC and sometimes with FloA in DRMs. Foci are lost when cells are treated with squalene synthase inhibitor zaragozic acid (PubMed:20713508). Found in discrete, highly mobile foci, often colocalizes with NfeD2 but rarely with FloA (PubMed:22753055). Forms discrete foci on the cell membrane, about 20% of foci are at the septal site. At the septa colocalizes with FloA and FtsH (PubMed:22882210, PubMed:23249255). Colocalizes with FtsX, OppA, SdhA and SecY in DRMs (PubMed:23651456). Careful analysis gives an average of 13 FloA and 6 FloT foci per cell; FloA foci are smaller that FloT foci (PubMed:25909364). Another study shows FloA and FloT foci are similar in size, forming membrane assemblies of 85-110 nm. FloA are more mobile than FloT foci and they do not overlap. This study found no evidence of colocalization of FloA with FloT, and nearly complete colocalization of FloT with NfeD2 (PubMed:27362352). {ECO:0000269|PubMed:19383680, ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23249255, ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:25635948, ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:27362352}.
| null | null | null | null | null |
FUNCTION: Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. FloA and FloT function is partially redundant; double deletions have marked synthetic phenotypes (PubMed:20713508, PubMed:22753055, PubMed:25909364, PubMed:27362352). Flotillins are thought to be important factors in membrane fluidity, especially during periods of rapid growth in rich media (Probable). Whether specific proteins are associated with FMMs is controversial; in one study FloT rafts have been shown to include proteins involved in adaptation to stationary phase, while FloA-FloT rafts include proteins involved in differentiation including sporulation, biofilm formation and DNA uptake competence. Another (more finely resolved) study only showed association of NfeD2 with FloT rafts of all the proteins examined (PubMed:25909364, PubMed:27362352). Aids homooligomerization of KinC and KinD but not KinB, may prevent incorrect hetero-association of the above kinases (PubMed:26297017). Simultaneous overexpression of both FloA and FloT leads to defects in cell division and differentiation, in part caused by stabilization of FtsH and its subsequent increased ability to degrade proteins. Cells make more biofilm, are about half as long, have less EzrA and more frequent Z-rings (PubMed:24222488). Involved in spatial organization of membranes, perhaps recruiting proteins (e.g. NfeD2) to specific membrane regions (Probable) (PubMed:23651456). Plays a role in phosphorylation of master regulator Spo0A, an early sporulation event (PubMed:19383680). Plays a non-redundant role with dynamin-like protein A (dynA) in membrane dynamics and cell shape (PubMed:23249255). {ECO:0000269|PubMed:19383680, ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22753055, ECO:0000269|PubMed:23249255, ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:24222488, ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:26297017, ECO:0000269|PubMed:27362352, ECO:0000305|PubMed:22753055, ECO:0000305|PubMed:32662773}.
|
Bacillus subtilis (strain 168)
|
O32129
|
LIPA_BACSU
|
MAKKDEHLRKPEWLKIKLNTNENYTGLKKLMRENNLHTVCEEAKCPNIHECWAVRRTATFMILGSVCTRACRFCAVKTGLPTELDLQEPERVADSVALMNLKHAVITAVARDDQKDGGAGIFAETVRAIRRKSPFTTIEVLPSDMGGNYDNLKTLMDTRPDILNHNIETVRRLTPRVRARATYDRSLEFLRRAKEMQPDIPTKSSIMIGLGETKEEIIEVMDDLLANNVDIMAIGQYLQPTKKHLKVQKYYHPDEFAELKEIAMQKGFSHCEAGPLVRSSYHADEQVNEASKKRQAQA
|
2.8.1.8
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_00206}; Note=Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000255|HAMAP-Rule:MF_00206};
|
lipoate biosynthetic process [GO:0009107]; protein lipoylation [GO:0009249]
|
cytoplasm [GO:0005737]
|
4 iron, 4 sulfur cluster binding [GO:0051539]; lipoate synthase activity [GO:0016992]; metal ion binding [GO:0046872]
|
PF16881;PF04055;
|
3.20.20.70;
|
Radical SAM superfamily, Lipoyl synthase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00206}.
|
CATALYTIC ACTIVITY: Reaction=[[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16585, Rhea:RHEA-COMP:9928, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:14568, Rhea:RHEA-COMP:14569, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:29034, ChEBI:CHEBI:29919, ChEBI:CHEBI:33722, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:78809, ChEBI:CHEBI:83100; EC=2.8.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00206};
| null |
PATHWAY: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]. {ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:19820084}.
| null | null |
FUNCTION: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. {ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:19820084}.
|
Bacillus subtilis (strain 168)
|
O32141
|
PUCL_BACSU
|
MFTMDDLNQMDTQTLTDTLGSIFEHSSWIAERSAALRPFSSLSDLHRKMTGIVKAADRETQLDLIKKHPRLGTKKTMSDDSVREQQNAGLGKLEQQEYEEFLMLNEHYYDRFGFPFILAVKGKTKQDIHQALLARLESERETEFQQALIEIYRIARFRLADIITEKGETQMKRTMSYGKGNVFAYRTYLKPLTGVKQIPESSFAGRDNTVVGVDVTCEIGGEAFLPSFTDGDNTLVVATDSMKNFIQRHLASYEGTTTEGFLHYVAHRFLDTYSHMDTITLTGEDIPFEAMPAYEEKELSTSRLVFRRSRNERSRSVLKAERSGNTITITEQYSEIMDLQLVKVSGNSFVGFIRDEYTTLPEDGNRPLFVYLNISWQYENTNDSYASDPARYVAAEQVRDLASTVFHELETPSIQNLIYHIGCRILARFPQLTDVSFQSQNHTWDTVVEEIPGSKGKVYTEPRPPYGFQHFTVTREDAEKEKQKAAEKCRSLKA
|
1.7.3.3; 4.1.1.97
| null |
allantoin metabolic process [GO:0000255]; purine nucleobase metabolic process [GO:0006144]; urate catabolic process [GO:0019628]
|
peroxisome [GO:0005777]
|
2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activity [GO:0051997]; urate oxidase activity [GO:0004846]
|
PF09349;PF01014;
|
1.10.3330.10;3.10.270.10;
|
OHCU decarboxylase family; Uricase family
| null | null |
CATALYTIC ACTIVITY: Reaction=5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+) = (S)-allantoin + CO2; Xref=Rhea:RHEA:26301, ChEBI:CHEBI:15378, ChEBI:CHEBI:15678, ChEBI:CHEBI:16526, ChEBI:CHEBI:58639; EC=4.1.1.97; CATALYTIC ACTIVITY: Reaction=H2O + O2 + urate = 5-hydroxyisourate + H2O2; Xref=Rhea:RHEA:21368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072; EC=1.7.3.3;
| null |
PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.; PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from urate: step 3/3.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:20168977};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. Retains 90% of its activity after 72 hours of incubation at 20 degrees Celsius or -4 degrees Celsius, but loses 50% of its activity after 12 hours of incubation at 37 degrees Celsius. {ECO:0000269|PubMed:20168977};
|
FUNCTION: Catalyzes two steps in the degradation of uric acid, i.e. the oxidation of uric acid to 5-hydroxyisourate (HIU) and the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin. {ECO:0000269|PubMed:11344136, ECO:0000269|PubMed:17567580, ECO:0000269|PubMed:20168977}.
|
Bacillus subtilis (strain 168)
|
O32142
|
HIUH_BACSU
|
MGKLTTHILDLTCGKPAANVKIGLKRLGESIMKEVYTNNDGRVDVPLLAGEELMSGEYVMEFHAGDYFASKNMNAADQPFLTIVTVRFQLADPDAHYHIPLLLSPFGYQVYRGS
|
3.5.2.17
| null |
purine nucleobase metabolic process [GO:0006144]; urate catabolic process [GO:0019628]
| null |
hydroxyisourate hydrolase activity [GO:0033971]; identical protein binding [GO:0042802]
|
PF00576;
|
2.60.40.180;
|
Transthyretin family, 5-hydroxyisourate hydrolase subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+); Xref=Rhea:RHEA:23736, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18072, ChEBI:CHEBI:58639; EC=3.5.2.17; Evidence={ECO:0000269|PubMed:16098976};
| null |
PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from urate: step 2/3.
| null | null |
FUNCTION: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
|
Bacillus subtilis (strain 168)
|
O32148
|
PUCG_BACSU
|
MSGRRELCTPLRTIMTPGPVEVDPRVLRVMSTPVVGQFDPAFTGIMNETMEMLRELFQTKNRWAYPIDGTSRAGIEAVLASVIEPEDDVLIPIYGRFGYLLTEIAERYGANVHMLECEWGTVFDPEDIIREIKKVKPKIVAMVHGETSTGRIHPLKAIGEACRTEDALFIVDAVATIGGCEVKVDEWKIDAAIGGTQKCLSVPSGMAPITYNERVADVIAARKKVERGIATQADRAALSGNRPITSNYFDLSQLEDYWSERRLNHHTEATTMLYALREGVRLVLEEGLETRFERHRHHEAALAAGIKAMGLRLFGDDSCKMPVVTCVEIPGGIDGESVRDMLLAQFGIEIASSFGPLAGKIWRIGTMGYSCRKENVLFVLAGLEAVLLRHNAGIEAGKALQAALDVYENAGRQAAV
|
2.6.1.112
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:20852637};
|
allantoin catabolic process [GO:0000256]; glycine biosynthetic process, by transamination of glyoxylate [GO:0019265]; purine nucleobase metabolic process [GO:0006144]
|
peroxisome [GO:0005777]
|
alanine-glyoxylate transaminase activity [GO:0008453]; serine-pyruvate transaminase activity [GO:0004760]
|
PF00266;
|
3.90.1150.10;3.40.640.10;
|
Class-V pyridoxal-phosphate-dependent aminotransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=(S)-2-ureidoglycine + glyoxylate = glycine + N-carbamoyl-2-oxoglycine; Xref=Rhea:RHEA:33867, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:57824, ChEBI:CHEBI:59947; EC=2.6.1.112; Evidence={ECO:0000269|PubMed:20852637};
| null |
PATHWAY: Nitrogen metabolism; (S)-allantoin degradation. {ECO:0000305|PubMed:11344136, ECO:0000305|PubMed:20852637}.
| null | null |
FUNCTION: Catalyzes the transamination between an unstable intermediate ((S)-ureidoglycine) and the end product of purine catabolism (glyoxylate) to yield oxalurate and glycine. Glyoxylate is the preferred substrate, but other amino-group acceptors can be used. {ECO:0000269|PubMed:20852637}.
|
Bacillus subtilis (strain 168)
|
O32163
|
SUFU_BACSU
|
MSFNANLDTLYRQVIMDHYKNPRNKGVLNDSIVVDMNNPTCGDRIRLTMKLDGDIVEDAKFEGEGCSISMASASMMTQAIKGKDIETALSMSKIFSDMMQGKEYDDSIDLGDIEALQGVSKFPARIKCATLSWKALEKGVAKEEGGN
|
2.-.-.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:24321018}; Note=Bind 1 Zn(2+) per monomer. {ECO:0000269|PubMed:24321018};
|
intracellular iron ion homeostasis [GO:0006879]; iron-sulfur cluster assembly [GO:0016226]
|
cytoplasm [GO:0005737]
|
2 iron, 2 sulfur cluster binding [GO:0051537]; ferrous iron binding [GO:0008198]; transferase activity [GO:0016740]
|
PF01592;
|
3.90.1010.10;
|
NifU family
| null | null | null | null | null | null | null |
FUNCTION: Part of the SUF-like system that mediates the biosynthesis of iron-sulfur (Fe-S) clusters. Acts as a sulfurtransferase and thus transfers sulfur from SufS to SufB (PubMed:29292548). Mechanistically, the transfer from SufS to SufU is triggered by zinc-ligand swapping that provides a free thiol from SufU to accept sulfur from SufS (PubMed:29235855). {ECO:0000269|PubMed:20097860, ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21236255, ECO:0000269|PubMed:21744456, ECO:0000269|PubMed:24321018, ECO:0000269|PubMed:27382962, ECO:0000269|PubMed:29235855, ECO:0000269|PubMed:29292548}.
|
Bacillus subtilis (strain 168)
|
O32164
|
SUFS_BACSU
|
MNITDIREQFPILHQQVNGHDLVYLDSAATSQKPRAVIETLDKYYNQYNSNVHRGVHTLGTRATDGYEGAREKVRKFINAKSMAEIIFTKGTTTSLNMVALSYARANLKPGDEVVITYMEHHANIIPWQQAVKATGATLKYIPLQEDGTISLEDVRETVTSNTKIVAVSHVSNVLGTVNPIKEMAKIAHDNGAVIVVDGAQSTPHMKIDVQDLDCDFFALSSHKMCGPTGVGVLYGKKALLENMEPAEFGGEMIDFVGLYESTWKELPWKFEAGTPIIAGAIGLGAAIDFLEEIGLDEISRHEHKLAAYALERFRQLDGVTVYGPEERAGLVTFNLDDVHPHDVATVLDAEGIAVRAGHHCAQPLMKWLDVTATARASFYLYNTEEEIDKLVEALQKTKEYFTNVF
|
2.8.1.7
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250};
|
cysteine metabolic process [GO:0006534]
| null |
cysteine desulfurase activity [GO:0031071]; pyridoxal phosphate binding [GO:0030170]
|
PF00266;
|
3.90.1150.10;3.40.640.10;
|
Class-V pyridoxal-phosphate-dependent aminotransferase family, Csd subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972, ChEBI:CHEBI:64428; EC=2.8.1.7; Evidence={ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:27382962};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=86 uM for L-cysteine {ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21236255}; KM=30 uM for SufU {ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21236255}; Vmax=1157 nmol/min/mg enzyme in the presence of SufU {ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21236255}; Note=In the presence of dithiothreitol, which regenerates the second reaction product SufU.S.;
| null | null | null |
FUNCTION: Type II cysteine desulfurase that acts as the initial step in the SUF-like Fe-S cluster assembly pathway. Catalyzes the removal of elemental sulfur atoms from L-cysteine by using the cofactor pyridoxal 5'-phosphate (PLP), resulting in the production of L-alanine and persulfide (PubMed:31587510). Activity is stimulated by SufU, which acts as a sulfurtransferase that receives sulfur from SufS via a zinc-ligand swapping mechanism and transfers it to SufB (PubMed:27382962, PubMed:29235855). {ECO:0000269|PubMed:20097860, ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21744456, ECO:0000269|PubMed:27382962, ECO:0000269|PubMed:29235855, ECO:0000269|PubMed:31587510}.
|
Bacillus subtilis (strain 168)
|
O32219
|
CADA_BACSU
|
MRLVKQEYVLDGLDCSNCARKIENGVKGIKGINGCAVNFAASTLTVSADGKEEQWVTNKVEKKVKSIDPHVTVRQKHIKKSADDGYRNRMVNMLIRMAAAVILGAAAYLVQSGTIEFFLFLGAYLIIGGDIIIRAVKNIIRGQVFDEHFLMALATIGAFLIQQYPEGVAVMLFYQIGELFQGAAVSRSRKSISALMDIRPDYANLKTKNGIEQVSSEDVQTGDIIVVNPGESIPLDGKVVQGSAMVDTSALTGESVPRKAAEGQDVMSGFINQNGVLHIEVTKGYQESAVSKILDLVQNASSRKARTENFITKFAKYYTPAVVIIAVLLAFVPPLVLSGAALSDWVYRALIFLVISCPCALVVSIPLGFFGGIGAASKAGVLVKGSNYLEALNQVKYAVFDKTGTLTKGSFEVTEIKPAEGFTKDRLLEAAAYAELHSQHPIAESVRKAYGKMLSSDEIESYEEISGHGIFAKVNGTEILAGNKKLMEREQIEDVPDENAGTIVHVAVDQRYAGAIIIADEIKEDAAQAVADLKSLGIKQTAMLTGDSKQTGEAVGKQLGIGEVYAELLPQDKVAQVEALEAKLLPSEKLIFVGDGINDTPVLARADIGVAMGGLGSDAAVEAADIVLMTDQPSKIAEAIRIAKRTRRIVWQNIGFALGVKAIFLILGAFGIATMWEAVFSDVGVTLLAVANAMRVMRLKNK
|
7.2.2.12; 7.2.2.21
| null |
cobalt ion transport [GO:0006824]; copper ion transport [GO:0006825]; metal ion transport [GO:0030001]; response to cadmium ion [GO:0046686]; transmembrane transport [GO:0055085]; zinc ion transport [GO:0006829]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cadmium ion transmembrane transporter activity [GO:0015086]; metal ion binding [GO:0046872]; P-type cadmium transporter activity [GO:0008551]; P-type zinc transporter activity [GO:0016463]
|
PF00122;PF00403;PF00702;
|
3.30.70.100;3.40.1110.10;2.70.150.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IB subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out); Xref=Rhea:RHEA:20621, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.12; Evidence={ECO:0000269|PubMed:11934502, ECO:0000269|PubMed:12779235}; CATALYTIC ACTIVITY: Reaction=ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:12132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48775, ChEBI:CHEBI:456216; EC=7.2.2.21; Evidence={ECO:0000269|PubMed:11934502, ECO:0000269|PubMed:12779235};
| null | null | null | null |
FUNCTION: Couples the hydrolysis of ATP with the transport of cadmium, zinc and cobalt out of the cell. Does not seem to transport copper. {ECO:0000269|PubMed:12779235}.
|
Bacillus subtilis (strain 168)
|
O32220
|
COPA_BACSU
|
MSEQKEIAMQVSGMTCAACAARIEKGLKRMPGVTDANVNLATETSNVIYDPAETGTAAIQEKIEKLGYHVVTEKAEFDIEGMTCAACANRIEKRLNKIEGVANAPVNFALETVTVEYNPKEASVSDLKEAVDKLGYKLKLKGEQDSEAAAKKKEERKQTARLIFSAVLSFPLLWAMVSHFTFTSFIWVPDIFLNPWMQFALATPVQFLIGWPFYVGAYKALRNKSANMDVLVALGTTAAYAYSLYLTFQSIGSHGHTDGLYYETSAILLTLILLGKLFETKAKGRSSDAIKKLMKLQAKTATVVRDGQEQIIPIDEVLVNDIVYVKPGERIPVDGEVVEGRSAVDESMITGESLPVDKNPGDSVTGSTVNANGFLKIKAVNVGKDTALSHIIKIVEEAQGSKAPIQRLADQISGIFVPIVLGIAVLTFLIWYLWAAPGDFAEAISKFIAVLVIACPCALGLATPTSIMAGSGRAAEFGILFKGGEHLEKTHRLDTIVLDKTGTVTNGKPRLTDAIPFGRFEEKDLLQFAAAAETGSEHPLGEAIIAGVKDKGLEIPKLTRFEAKVGAGILAEAGGKSILVGTRKLMESEQVEHGALLAQMEELEAEGKTVMLVSIDGEAAGLVAVADTIKDTSRKAVARLKELGLDVIMMTGDNRRTAEAIAKEAGIANIIAEVLPEQKAAEIARLQKEGRQTAMVGDGINDAPALATADIGMAIGTGTDIAMETADITLIRGDLNSIADAIRMSRLTMKNIKQNLFWALGYNSLGIPIAALGFLAPWIAGAAMAFSSVSVVLNALRLQKVK
|
7.2.2.8
| null |
copper ion export [GO:0060003]; copper ion homeostasis [GO:0055070]; copper ion import [GO:0015677]; intracellular copper ion homeostasis [GO:0006878]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; P-type divalent copper transporter activity [GO:0043682]; P-type monovalent copper transporter activity [GO:0140581]
|
PF00122;PF00403;PF00702;
|
3.30.70.100;3.40.1110.10;2.70.150.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IB subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552, ChEBI:CHEBI:456216; EC=7.2.2.8;
| null | null | null | null |
FUNCTION: Involved in copper export. {ECO:0000269|PubMed:12644235}.
|
Bacillus subtilis (strain 168)
|
O32224
|
AZOR2_BACSU
|
MAKVLYITAHPHDEATSYSMATGKAFIESYKEANPNDEVVHIDLYKENIPHIDADVFSGWGKLQSGTGFEELSESEKAKVGRLGELSDQFASADKYVFVTPLWNFSFPPVMKAYLDSVAVAGKSFKYTEQGPVGLLTDKKAIHIQARGGYYSEGPAAEMEMGHRYIGIMMNFFGVPSFDGIFVEGHNAEPDKAQQIKEDAIARAKEAGKTF
|
1.6.5.-; 1.7.1.17
|
COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:17284825}; Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:17284825};
|
aromatic compound catabolic process [GO:0019439]; response to toxic substance [GO:0009636]
| null |
electron transfer activity [GO:0009055]; FMN binding [GO:0010181]; oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor [GO:0016652]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655]
|
PF02525;
|
3.40.50.360;
|
Azoreductase type 1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+); Xref=Rhea:RHEA:65952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225; Evidence={ECO:0000255|HAMAP-Rule:MF_01216}; CATALYTIC ACTIVITY: Reaction=anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH; Xref=Rhea:RHEA:55872, ChEBI:CHEBI:15378, ChEBI:CHEBI:15783, ChEBI:CHEBI:16567, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:71579; EC=1.7.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:17284825}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55874; Evidence={ECO:0000269|PubMed:17284825};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 uM for 2,6-dichloroondophenol (DCIP) (at pH 7.5 and at 25 degrees Celsius) {ECO:0000269|PubMed:17284825}; KM=190 uM for NADH (at pH 7.5 and at 25 degrees Celsius) {ECO:0000269|PubMed:17284825};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:17284825};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Activity increases linearly up to 40 degrees Celsius. Stable up to 55 degrees Celsius after incubation for 30 minutes at pH 7.5. During incubation at 25 degrees Celsius for 16h, the enzyme is stable between pH 5.5 and 9.0, where 80% activity is observed. {ECO:0000269|PubMed:17284825};
|
FUNCTION: Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones (Probable). Contributes to resistance to 2-methylhydroquinone (2-MHQ) and catechol (PubMed:17725564, PubMed:18208493). Exhibits NADH-dependent 2,6-dichloroindophenol (DCIP) oxidoreductase activity (PubMed:17284825). {ECO:0000269|PubMed:17284825, ECO:0000269|PubMed:17725564, ECO:0000269|PubMed:18208493, ECO:0000305|PubMed:18208493}.; FUNCTION: Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines (PubMed:17284825). Can reduce methyl red (PubMed:17284825). {ECO:0000269|PubMed:17284825}.
|
Bacillus subtilis (strain 168)
|
O32472
|
PHAJ_AERCA
|
MSAQSLEVGQKARLSKRFGAAEVAAFAALSEDFNPLHLDPAFAATTAFERPIVHGMLLASLFSGLLGQQLPGKGSIYLGQSLSFKLPVFVGDEVTAEVEVTALREDKPIATLTTRIFTQGGALAVTGEAVVKLP
|
4.2.1.119
| null |
fatty acid biosynthetic process [GO:0006633]
|
fatty acid synthase complex [GO:0005835]
|
(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity [GO:0019171]; fatty acid synthase activity [GO:0004312]
|
PF01575;
|
3.10.129.10;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:26526, ChEBI:CHEBI:15377, ChEBI:CHEBI:57319, ChEBI:CHEBI:58856; EC=4.2.1.119; Evidence={ECO:0000269|PubMed:9457873};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=29 uM for crotonyl-CoA {ECO:0000269|PubMed:9457873}; KM=36 uM for 2-pentenoyl-CoA {ECO:0000269|PubMed:9457873}; KM=34 uM for 2-hexenoyl-CoA {ECO:0000269|PubMed:9457873}; KM=50 uM for 2-octenoyl-CoA {ECO:0000269|PubMed:9457873}; Vmax=6200 umol/min/mg enzyme with crotonyl-CoA as substrate {ECO:0000269|PubMed:9457873}; Vmax=2800 umol/min/mg enzyme with 2-pentenoyl-CoA as substrate {ECO:0000269|PubMed:9457873}; Vmax=1800 umol/min/mg enzyme with 2-hexenoyl-CoA as substrate {ECO:0000269|PubMed:9457873}; Vmax=2.5 umol/min/mg enzyme with 2-octenoyl-CoA as substrate {ECO:0000269|PubMed:9457873};
| null | null | null |
FUNCTION: Catalyzes the hydration of trans-2-enoyl-CoA with a chain-length of 4-6 carbon atoms, forming the corresponding (3R)-3-hydroxyacyl-CoA. {ECO:0000269|PubMed:9244271, ECO:0000269|PubMed:9457873}.
|
Aeromonas caviae (Aeromonas punctata)
|
O32504
|
PPRA_DEIRA
|
MLPLAFLICSGHNKGSMARAKAKDQTDGIYAAFDTLMSTAGVDSQIAALAASEADAGTLDAALTQSLQEAQGRWGLGLHHLRHEARLTDDGDIEILTDGRPSARVSEGFGALAQAYAPMQALDERGLSQWAALGEGYRAPGDLPLAQLKVLIEHARDFETDWSAGRGETFQRVWRKGDTLFVEVARPASAEAALSDAAWDVIASIKDRAFQRELMRRSEKDGMLGALLGARHAGAKANLAQLPEAHFTVQAFVQTLSGAAARNAEEYRAALKTAAAALEEYQGVTTRQLSEVLRHGLRES
| null | null |
cellular response to desiccation [GO:0071465]; cellular response to gamma radiation [GO:0071480]; DNA repair [GO:0006281]; positive regulation of DNA ligation [GO:0051106]
| null |
damaged DNA binding [GO:0003684]; double-stranded DNA binding [GO:0003690]
| null | null | null |
PTM: Phosphorylated by RqkA in vitro. Phosphorylated primarily at Thr-88, and to a little extent at Ser-128 and Thr-160. {ECO:0000269|PubMed:23994692}.
| null | null | null | null | null | null |
FUNCTION: dsDNA-binding protein that contributes to the ionizing radiation resistance of D.radiodurans. Plays a role in DNA repair and genome reconstitution, and is necessary for recovery from severe genomic fragmentation as a result of exposure to severe levels of ionizing radiation. In vitro, binds to double-stranded DNA carrying strand breaks and stimulates the DNA end-joining reaction catalyzed by DNA ligases. Thus, PprA plays a critical role in a non-homologous end-joining (NHEJ) pathway for the repair of radiation-induced DNA double-strands breaks. Cannot bind to dsDNA without strand breaks or single-stranded DNA. {ECO:0000269|PubMed:15454524, ECO:0000269|PubMed:15458422}.
|
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
|
O32583
|
THIS_ECOLI
|
MQILFNDQAMQCAAGQTVHELLEQLDQRQAGAALAINQQIVPREQWAQHIVQDGDQILLFQVIAGG
| null | null |
thiamine biosynthetic process [GO:0009228]; thiamine diphosphate biosynthetic process [GO:0009229]; thiazole biosynthetic process [GO:0052837]
|
adenylyltransferase complex [GO:1902503]; sulfurtransferase complex [GO:1990228]
|
nucleotide binding [GO:0000166]; sulfur carrier activity [GO:0097163]
|
PF02597;
|
3.10.20.30;
|
Sulfur carrier protein ThiS family
|
PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) by ThiF, then thiocarboxylated (-COSH) by ThiI. {ECO:0000269|PubMed:9632726}.
| null | null | null |
PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
| null | null |
FUNCTION: Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate. {ECO:0000269|PubMed:9632726}.
|
Escherichia coli (strain K12)
|
O32765
|
LDH_LACHE
|
MAREEKPRKVILVGDGAVGSTFAFSMVQQGIAEELGIIDIAKEHVEGDAIDLADATPWTSPKNIYAADYPDCKDADLVVITAGAPQKPGETRLDLVNKNLKILSSIVEPVVESGFEGIFLVVANPVDILTHATWRMSGFPKDRVIGSGTSLDTGRLQKVIGKMENVDPSSVNAYMLGEHGDTEFPAWSYNNVAGVKVADWVKAHNMPESKLEDIHQEVKDMAYDIINKKGATFYGIGTASAMIAKAILNDEHRVLPLSVPMDGEYGLHDLHIGTPAVVGRKGLEQVIEMPLSDKEQELMTASADQLKKVMDKAFKETGVKVRQ
|
1.1.1.27
| null |
glycolytic process [GO:0006096]; lactate metabolic process [GO:0006089]
|
cytoplasm [GO:0005737]
|
L-lactate dehydrogenase activity [GO:0004459]
|
PF02866;PF00056;
|
3.90.110.10;3.40.50.720;
|
LDH/MDH superfamily, LDH family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00488}.
|
CATALYTIC ACTIVITY: Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate; Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27; Evidence={ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:9212432};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for pyruvate {ECO:0000269|PubMed:9212432}; Note=kcat is 643 sec(-1) for pyruvate as substrate. {ECO:0000269|PubMed:9212432};
|
PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00488}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:9212432};
| null |
FUNCTION: Catalyzes the conversion of lactate to pyruvate. {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:9212432}.
|
Lactobacillus helveticus (Lactobacillus suntoryeus)
|
O33125
|
DBH_MYCLE
|
MNKAELIDVLTQKLGSDRRQATAAVENVVDTIVRAVHKGDSVTITGFGVFEQRRRAARVARNPRTGETVKVKPTSVPAFRPGAQFKAVVAGAQRLPLEGPAVKRGVATSAAKKAAIKKAPVKKALAKKAATKAPAKKAVKAPAKKITTAVKVPAKKATKVVKKVAAKAPVRKATTRALAKKAAVKKAPAKKVTAAKRGRK
|
1.16.3.1
| null |
chromosome condensation [GO:0030261]
|
cell surface [GO:0009986]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleoid [GO:0009295]
|
DNA binding [GO:0003677]; ferric iron binding [GO:0008199]; ferroxidase activity [GO:0004322]; structural constituent of chromatin [GO:0030527]
|
PF00216;
|
4.10.520.10;
|
Bacterial histone-like protein family, Long actinobacterial subfamily
|
PTM: May also be methylated and possibly phosphorylated in vivo. {ECO:0000250|UniProtKB:A5U6Z7, ECO:0000250|UniProtKB:P9WMK7}.
|
SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000250|UniProtKB:Q9ZHC5}. Secreted, cell wall {ECO:0000269|PubMed:10449784}. Cell surface {ECO:0000269|PubMed:10449784}.
|
CATALYTIC ACTIVITY: Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; Evidence={ECO:0000269|PubMed:21698192}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11149; Evidence={ECO:0000269|PubMed:21698192};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.129 mM for Fe(2+) {ECO:0000269|PubMed:21698192};
| null | null | null |
FUNCTION: A nucleoid-associated protein (NAP) that plays a role in local chromosome architecture and chromosome compactation. Required for biofilm formation, stress survival and possibly in cell wall assembly, probably influences transcription (By similarity). RNase E and HupB jointly contribute to cellular adaptation to changing growth conditions and survival during antibiotic treatment and in the host (By similarity). {ECO:0000250|UniProtKB:P9WMK7, ECO:0000250|UniProtKB:Q9ZHC5}.; FUNCTION: Binds Fe(3+) but not Fe(2+). Has ferroxidase activity, converts Fe(2+) into Fe(3+) and in the presence of H(2)O(2) prevents the generation of hydroxyl radicals (the Fenton reaction). Protects DNA from damage in the presence of FeSO(4) and H(2)O(2). May function in iron storage. {ECO:0000269|PubMed:21698192}.; FUNCTION: May be involved in entry into human Schwann cells. {ECO:0000305|PubMed:10449784}.
|
Mycobacterium leprae (strain TN)
|
O33194
|
G3PP_MYCTU
|
MKSIAQEHDCLLIDLDGTVFCGRQPTGGAVQSLSQVRSRKLFVTNNASRSADEVAAHLCELGFTATGEDVVTSAQSAAHLLAGQLAPGARVLIVGTEALANEVAAVGLRPVRRFEDRPDAVVQGLSMTTGWSDLAEAALAIRAGALWVAANVDPTLPTERGLLPGNGSMVAALRTATGMDPRVAGKPAPALMTEAVARGDFRAALVVGDRLDTDIEGANAAGLPSLMVLTGVNSAWDAVYAEPVRRPTYIGHDLRSLHQDSKLLAVAPQPGWQIDVGGGAVTVCANGDVDDLEFIDDGLSIVRAVASAVWEARAADLHQRPLRIEAGDERARAALQRWSLMRSDHPVTSVGTQ
| null |
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23801751}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:23801751}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:23801751}; Note=Although Co(2+) and Mn(2+) support eight- and fourfold higher catalytic efficiency than Mg(2+), respectively, Mg(2+) is likely the physiologically relevant catalytic divalent metal ion. {ECO:0000269|PubMed:23801751};
|
glycerol metabolic process [GO:0006071]; glycerophospholipid catabolic process [GO:0046475]
| null |
cobalt ion binding [GO:0050897]; glycerol-1-phosphatase activity [GO:0000121]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; phosphatase activity [GO:0016791]; protein homodimerization activity [GO:0042803]
|
PF18407;PF13344;PF13242;
|
3.30.300.290;3.40.50.1000;
|
HAD-like hydrolase superfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + sn-glycerol 1-phosphate = glycerol + phosphate; Xref=Rhea:RHEA:46084, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754, ChEBI:CHEBI:43474, ChEBI:CHEBI:57685; Evidence={ECO:0000269|PubMed:23801751}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46085; Evidence={ECO:0000269|PubMed:23801751};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.89 mM for D,L-glycerol 3-phosphate {ECO:0000269|PubMed:23801751}; KM=1.3 mM for D-ribulose 5-phosphate {ECO:0000269|PubMed:23801751}; KM=2.01 mM for glycerol 2-phosphate {ECO:0000269|PubMed:23801751}; KM=19.3 mM for p-nitrophenyl 3-phosphate {ECO:0000269|PubMed:23801751}; KM=1.1 mM for L-glycerol 3-phosphate {ECO:0000269|PubMed:23801751}; Note=kcat is 0.77 sec(-1) with D,L-glycerol 3-phosphate as substrate. kcat is 0.18 sec(-1) with D-ribulose 5-phosphate as substrate. kcat is 0.18 sec(-1) with glycerol 2-phosphate as substrate. kcat is 1.00 sec(-1) with p-nitrophenyl 3-phosphate as substrate. kcat is 0.02 sec(-1) with L-glycerol 3-phosphate as substrate. {ECO:0000269|PubMed:23801751};
|
PATHWAY: Glycerolipid metabolism. {ECO:0000269|PubMed:23801751}.
| null | null |
FUNCTION: Dephosphorylates D-glycerol 3-phosphate (sn-glycerol 1-phosphate). Is the final enzyme involved in the recycling/catabolism of glycerophospholipid polar heads. To a lesser extent, is also able to act on glycerol 2-phosphate and D-ribulose 5-phosphate, but cannot use D-glyceraldehyde 3-phosphate, dihydroxyacetone-phosphate, UMP or GMP as substrates. {ECO:0000269|PubMed:23801751}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O33283
|
EPHG_MYCTU
|
MAELTETSPETPETTEAIRAVEAFLNALQNEDFDTVDAALGDDLVYENVGFSRIRGGRRTATLLRRMQGRVGFEVKIHRIGADGAAVLTERTDALIIGPLRVQFWVCGVFEVDDGRITLWRDYFDVYDMFKGLLRGLVALVVPSLKATL
|
3.3.2.10; 3.3.2.11
| null |
epoxide metabolic process [GO:0097176]
|
plasma membrane [GO:0005886]
|
cholesterol-5,6-oxide hydrolase activity [GO:0033963]; epoxide hydrolase activity [GO:0004301]
|
PF07858;
|
3.10.450.50;
|
Limonene-1,2-epoxide hydrolase family
| null | null |
CATALYTIC ACTIVITY: Reaction=an epoxide + H2O = an ethanediol; Xref=Rhea:RHEA:19037, ChEBI:CHEBI:15377, ChEBI:CHEBI:32955, ChEBI:CHEBI:140594; EC=3.3.2.10; Evidence={ECO:0000269|PubMed:16051262}; CATALYTIC ACTIVITY: Reaction=5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O = 5alpha-cholestane-3beta,5,6beta-triol; Xref=Rhea:RHEA:11964, ChEBI:CHEBI:15377, ChEBI:CHEBI:28082, ChEBI:CHEBI:49305; EC=3.3.2.11; Evidence={ECO:0000269|PubMed:16051262}; CATALYTIC ACTIVITY: Reaction=5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O = 5alpha-cholestane-3beta,5,6beta-triol; Xref=Rhea:RHEA:15113, ChEBI:CHEBI:15377, ChEBI:CHEBI:28082, ChEBI:CHEBI:28164; EC=3.3.2.11; Evidence={ECO:0000269|PubMed:16051262};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=45 uM for cis-9,10-epoxystearate {ECO:0000269|PubMed:16051262}; KM=60 uM for cholesterol 5,6-oxide {ECO:0000269|PubMed:16051262}; Vmax=30 nmol/min/mg enzyme with cis-9,10-epoxystearate as substrate {ECO:0000269|PubMed:16051262}; Vmax=1.1 nmol/min/mg enzyme with cholesterol 5,6-oxide as substrate {ECO:0000269|PubMed:16051262};
| null | null | null |
FUNCTION: Epoxide hydrolase capable of hydrolyzing long or bulky lipophilic epoxides such as 9,10-epoxystearic acid and cholesterol 5,6-oxide in vitro. The physiological substrates have yet to be identified, but could be fatty acid or steroid derivatives. {ECO:0000269|PubMed:16051262}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O33289
|
ARGA_MYCTU
|
MTERPRDCRPVVRRARTSDVPAIKQLVDTYAGKILLEKNLVTLYEAVQEFWVAEHPDLYGKVVGCGALHVLWSDLGEIRTVAVDPAMTGHGIGHAIVDRLLQVARDLQLQRVFVLTFETEFFARHGFTEIEGTPVTAEVFDEMCRSYDIGVAEFLDLSYVKPNILGNSRMLLVL
|
2.3.1.1
| null |
arginine biosynthetic process via ornithine [GO:0042450]; protein homotetramerization [GO:0051289]
|
cytoplasm [GO:0005737]
|
acetyl-CoA:L-glutamate N-acetyltransferase activity [GO:0004042]; methione N-acyltransferase activity [GO:0103045]; N-acetyltransferase activity [GO:0008080]; protein homodimerization activity [GO:0042803]
|
PF00583;
|
3.40.630.30;
|
Acetyltransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate; Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1; Evidence={ECO:0000269|PubMed:15838030};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=150 mM for acetyl-CoA {ECO:0000269|PubMed:15838030}; KM=280 mM for glutamine {ECO:0000269|PubMed:15838030};
|
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
| null | null |
FUNCTION: Catalyzes the conversion of L-glutamate to alpha-N-acetyl-L-glutamate. L-glutamine is a significantly better substrate compared to L-glutamate. {ECO:0000269|PubMed:15838030}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O33336
|
PPTT_MYCTU
|
MTVGTLVASVLPATVFEDLAYAELYSDPPGLTPLPEEAPLIARSVAKRRNEFITVRHCARIALDQLGVPPAPILKGDKGEPCWPDGMVGSLTHCAGYRGAVVGRRDAVRSVGIDAEPHDVLPNGVLDAISLPAERADMPRTMPAALHWDRILFCAKEATYKAWFPLTKRWLGFEDAHITFETDSTGWTGRFVSRILIDGSTLSGPPLTTLRGRWSVERGLVLTAIVL
|
2.7.8.7
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25785780};
|
enterobactin biosynthetic process [GO:0009239]; siderophore biosynthetic process [GO:0019290]; siderophore metabolic process [GO:0009237]
|
enterobactin synthetase complex [GO:0009366]; plasma membrane [GO:0005886]
|
holo-[acyl-carrier-protein] synthase activity [GO:0008897]; magnesium ion binding [GO:0000287]
|
PF17837;PF01648;
| null |
P-Pant transferase superfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7; Evidence={ECO:0000269|PubMed:16709676, ECO:0000269|PubMed:25785780, ECO:0000269|PubMed:28203522, ECO:0000269|PubMed:9831524};
| null | null | null | null |
FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein (PubMed:16709676, PubMed:25785780, PubMed:28203522, PubMed:9831524). Involved in post-translational modification of various type-I polyketide synthases required for the formation of both mycolic acids and lipid virulence factors (PubMed:16709676). Acts on Pks13, Mas, PpsA, PpsB, PpsC and PpsD (PubMed:16709676, PubMed:28203522). Also acts on AcpM, the meromycolate extension acyl carrier protein (PubMed:25785780). In addition, is involved in the activation of the acyl carrier protein MbtL and the nonribosomal peptides synthases MbtB and MbtE, which are involved in the biosynthesis of the siderophore mycobactin (PubMed:28203522, PubMed:9831524). {ECO:0000269|PubMed:16709676, ECO:0000269|PubMed:25785780, ECO:0000269|PubMed:28203522, ECO:0000269|PubMed:9831524}.; FUNCTION: Required for the replication and survival of Mycobacterium during the acute and chronic phases of infection in mice. {ECO:0000269|PubMed:23308068}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O33348
|
RELG_MYCTU
|
MPYTVRFTTTARRDLHKLPPRILAAVVEFAFGDLSREPLRVGKPLRRELAGTFSARRGTYRLLYRIDDEHTTVVILRVDHRADIYRR
|
3.1.-.-
| null |
negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of growth [GO:0045926]; RNA catabolic process [GO:0006401]
| null |
DNA binding [GO:0003677]; endonuclease activity [GO:0004519]
|
PF05016;
|
3.30.2310.20;
|
RelE toxin family
| null | null | null | null | null | null | null |
FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Has RNase activity and preferentially cleaves at the 3'-end of purine ribonucleotides (By similarity). Overexpression in M.tuberculosis or M.smegmatis inhibits colony formation in a bacteriostatic rather than bacteriocidal fashion. Its toxic effect is neutralized by coexpression with cognate antitoxin RelB2 (shown only for M.smegmatis). Overexpression also increases the number of gentamicin-tolerant and levofloxacin-tolerant persister cells. {ECO:0000250, ECO:0000269|PubMed:19114484, ECO:0000269|PubMed:20011113, ECO:0000269|PubMed:20061486, ECO:0000269|PubMed:20498855}.; FUNCTION: In combination with cognate antitoxin RelF represses its own promoter. Has been seen to bind DNA in complex with antitoxin RelF but not alone.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O33363
|
GDSL_MYCTU
|
MSRPGTYVIGLTLLVGLVVGNPGCPRSYRPLTLDYRLNPVAVIGDSYTTGTDEGGLGSKSWTARTWQMLAARGVRIAADVAAEGRAGYGVPGDHGNVFEDLTARAVQPDDALVVFFGSRNDQGMDPEDPEMLAEKVRDTFDLARHRAPSASLLVIAPPWPTADVPGPMLRIRDVLGAQARAAGAVFVDPIADHWFVDRPELIGADGVHPNDAGHEYLADKIAPLISMELVG
|
3.1.1.-
| null |
lipid catabolic process [GO:0016042]
|
extracellular region [GO:0005576]
|
carboxylic ester hydrolase activity [GO:0052689]
|
PF13472;
|
3.40.50.1110;
|
'GDSL' lipolytic enzyme family
| null |
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:31125644}. Secreted, extracellular space {ECO:0000269|PubMed:31125644}.
|
CATALYTIC ACTIVITY: Reaction=a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:59388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35748; Evidence={ECO:0000269|PubMed:31125644}; CATALYTIC ACTIVITY: Reaction=decanoate ester + H2O = an aliphatic alcohol + decanoate + H(+); Xref=Rhea:RHEA:47360, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:87658; Evidence={ECO:0000269|PubMed:31125644}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000269|PubMed:31125644}; CATALYTIC ACTIVITY: Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659; Evidence={ECO:0000269|PubMed:31125644}; CATALYTIC ACTIVITY: Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) + tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:31125644};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=400 uM for pNP-decanoate {ECO:0000269|PubMed:31125644}; Note=kcat is 14440 min(-1) with pNP-decanoate as substrate. {ECO:0000269|PubMed:31125644};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 (with pNP-decanoate as substrate). {ECO:0000269|PubMed:31125644};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius (with pNP-decanoate as substrate). {ECO:0000269|PubMed:31125644};
|
FUNCTION: GDSL lipase that catalyzes the hydrolysis of p-nitrophenyl (pNP) esters. pNP-decanoate (C10) is the preferred substrate. It can also use pNP-octanoate (C8), pNP-dodecanoate (C12) and pNP-tetradecanoate (C14). Has lower activity with pNP-butyrate (C4), pNP-palmitate (C16) and pNP-stearate (C18) (PubMed:31125644). Does not show phospholipase A1 activity (PubMed:31125644). Might help bacteria to utilize available lipids for its growth as well as provide resistance to various intracellular stresses by cell wall modulation resulting in enhanced intracellular survival (PubMed:31125644). {ECO:0000269|PubMed:31125644}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O33407
|
ESTA_PSEAE
|
MIRMALKPLVAACLLASLSTAPQAAPSPYSTLVVFGDSLSDAGQFPDPAGPAGSTSRFTNRVGPTYQNGSGEIFGPTAPMLLGNQLGIAPGDLAASTSPVNAQQGIADGNNWAVGGYRTDQIYDSITAANGSLIERDNTLLRSRDGYLVDRARQGLGADPNALYYITGGGNDFLQGRILNDVQAQQAAGRLVDSVQALQQAGARYIVVWLLPDLGLTPATFGGPLQPFASQLSGTFNAELTAQLSQAGANVIPLNIPLLLKEGMANPASFGLAADQNLIGTCFSGNGCTMNPTYGINGSTPDPSKLLFNDSVHPTITGQRLIADYTYSLLSAPWELTLLPEMAHGTLRAYQDELRSQWQADWENWQNVGQWRGFVGGGGQRLDFDSQDSAASGDGNGYNLTLGGSYRIDEAWRAGVAAGFYRQKLEAGAKDSDYRMNSYMASAFVQYQENRWWADAALTGGYLDYDDLKRKFALGGGERSEKGDTNGHLWAFSARLGYDIAQQADSPWHLSPFVSADYARVEVDGYSEKGASATALDYDDQKRSSKRLGAGLQGKYAFGSDTQLFAEYAHEREYEDDTQDLTMSLNSLPGNRFTLEGYTPQDHLNRVSLGFSQKLAPELSLRGGYNWRKGEDDTQQSVSLALSLDF
|
3.1.1.1
| null |
bacterial-type flagellum-dependent cell motility [GO:0071973]; bacterial-type flagellum-dependent swarming motility [GO:0071978]; cell motility [GO:0048870]; glycolipid biosynthetic process [GO:0009247]; lipid biosynthetic process [GO:0008610]; single-species biofilm formation [GO:0044010]
|
cell outer membrane [GO:0009279]; extracellular region [GO:0005576]
|
carboxylesterase activity [GO:0106435]; carboxylic ester hydrolase activity [GO:0052689]; lipase activity [GO:0016298]
|
PF03797;PF00657;
|
2.40.128.130;3.40.50.1110;
|
'GDSL' lipolytic enzyme family
| null |
SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:10559163, ECO:0000269|PubMed:17631636}; Multi-pass membrane protein {ECO:0000269|PubMed:10559163, ECO:0000269|PubMed:17631636}.
|
CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000269|PubMed:10559163, ECO:0000269|PubMed:20931591};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:20931591}; Vmax=220 umol/min/mg enzyme with p-nitrophenyl butyrate as substrate {ECO:0000269|PubMed:20931591};
| null | null | null |
FUNCTION: Esterase whose enzymatic activity is required for rhamnolipid production, all kinds of cell motility (swimming, swarming, and twitching), and biofilm formation; the exact role of EstA in these processes is unclear. In vitro, has pronounced esterase activities towards p-nitrophenyl esters of short acyl chain length (C4-C6) and Tween detergents. Also shows relatively high activity towards beta-naphthyl butyrate, whereas its activities towards triacylglycerols and acyls-CoA are negligible. {ECO:0000269|PubMed:17631636, ECO:0000269|PubMed:20931591}.
|
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
|
O33434
|
SOXA_PARPN
|
MPRFTKTKGTLAATALGLALAGAAFADPVEDGLVIETDSGPVEIVTKTAPPAFLADTFDTIYSGWHFRDDSTRDLERDDFDNPAMVFVDRGLDKWNAAMGVNGESCASCHQGPESMAGLRAVMPRVDEHTGKLMIMEDYVNACVTERMGLEKWGVTSDNMKDMLSLISLQSRGMAVNVKIDGPAAPYWEHGKEIYYTRYGQLEMSCANCHEDNAGNMIRADHLSQGQINGFPTYRLKDSGMVTAQHRFVGCVRDTRAETFKAGSDDFKALELYVASRGNGLSVEGVSVRH
|
2.8.5.2
|
COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:10940005, ECO:0000269|PubMed:16297640, ECO:0000269|PubMed:17547421}; Note=Binds 2 heme c groups covalently per subunit. {ECO:0000269|PubMed:10940005, ECO:0000269|PubMed:16297640, ECO:0000269|PubMed:17547421}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16297640}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:16297640};
|
sulfur oxidation [GO:0019417]
|
cytochrome complex [GO:0070069]; periplasmic space [GO:0042597]
|
electron transfer activity [GO:0009055]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor [GO:0016669]; protein heterodimerization activity [GO:0046982]; sulfurtransferase activity [GO:0016783]; thiosulfate sulfurtransferase activity [GO:0004792]; zinc ion binding [GO:0008270]
|
PF21342;
|
1.10.760.10;
|
SoxA family
|
PTM: Cysteine persulfide at Cys-251. {ECO:0000269|PubMed:16297640}.
|
SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10940005, ECO:0000305|PubMed:17547421}.
|
CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:56720, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14328, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14691, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:29950, ChEBI:CHEBI:33542, ChEBI:CHEBI:139321; EC=2.8.5.2; Evidence={ECO:0000269|PubMed:10940005}; CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + S-sulfanyl-L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-(2-sulfodisulfanyl)-L-cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:51224, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14689, Rhea:RHEA-COMP:14690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:33542, ChEBI:CHEBI:61963, ChEBI:CHEBI:140664; EC=2.8.5.2; Evidence={ECO:0000269|PubMed:10940005};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.034 uM for thiosulfate using purified SoxAX complex (at pH 7.5) {ECO:0000269|PubMed:10940005, ECO:0000269|PubMed:17547421};
| null | null | null |
FUNCTION: C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation. {ECO:0000269|PubMed:10940005, ECO:0000269|PubMed:16297640, ECO:0000269|PubMed:17547421}.
|
Paracoccus pantotrophus (Thiosphaera pantotropha)
|
O33469
|
PAAK_PSEPU
|
MNMYHDADRALLDPMETASVDALRQHQLERLRWSLKHAYDNVPLYRQRFAECGAHPDDLTCLEDLAKFPFTGKNDLRDNYPYGMFAVPQEEVVRLHASSGTTGKPTVVGYTQNDINTWANVVARSIRAAGGRKGDKVHVSYGYGLFTGGLGAHYGAERLGCTVIPMSGGQTEKQVQLIRDFQPDIIMVTPSYMLNLADEIERQGIDPHDLKLRLGIFGAEPWTDELRRSIEQRLGINALDIYGLSEIMGPGVAMECIETKDGPTIWEDHFYPEIIDPVTGEVLPDGQLGELVFTSLSKEALPMVRYRTRDLTRLLPGTARPMRRIGKITGRSDDMLIIRGVNVFPTQIEEQVLKIKQLSEMYEIHLYRNGNLDSVEVHVELRAECQHLDEGQRKLVIGELSKQIKTYIGISTQVHLQACGTLKRSEGKACHVYDKRLAS
|
6.2.1.30
| null |
phenylacetate catabolic process [GO:0010124]
| null |
ATP binding [GO:0005524]; phenylacetate-CoA ligase activity [GO:0047475]
|
PF00501;PF14535;
|
3.30.300.30;3.40.50.12780;
|
Phenylacetyl-CoA ligase family
| null | null |
CATALYTIC ACTIVITY: Reaction=2-phenylacetate + ATP + CoA = AMP + diphosphate + phenylacetyl-CoA; Xref=Rhea:RHEA:20956, ChEBI:CHEBI:18401, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57390, ChEBI:CHEBI:456215; EC=6.2.1.30; Evidence={ECO:0000269|PubMed:2324116}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20957; Evidence={ECO:0000269|PubMed:2324116};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.7 mM for ATP (at 30 degrees Celsius and pH 8.2) {ECO:0000269|PubMed:2324116}; KM=1 mM for CoA (at 30 degrees Celsius and pH 8.2) {ECO:0000269|PubMed:2324116}; KM=16.5 mM for PA (at 30 degrees Celsius and pH 8.2) {ECO:0000269|PubMed:2324116};
|
PATHWAY: Aromatic compound metabolism; phenylacetate degradation. {ECO:0000305|PubMed:8969218, ECO:0000305|PubMed:9600981}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.2. {ECO:0000269|PubMed:2324116};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. The enzyme is heat stable. {ECO:0000269|PubMed:2324116};
|
FUNCTION: Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA) (PubMed:2324116). Involved in the phenylalanine metabolism (PubMed:2324116, PubMed:8969218, PubMed:9600981). Can also use CTP and UTP as substrate (PubMed:2324116). {ECO:0000269|PubMed:2324116, ECO:0000269|PubMed:8969218, ECO:0000269|PubMed:9600981}.
|
Pseudomonas putida (Arthrobacter siderocapsulatus)
|
O33599
|
LYTM_STAA8
|
MKKLTAAAIATMGFATFTMAHQADAAETTNTQQAHTQMSTQSQDVSYGTYYTIDSNGDYHHTPDGNWNQAMFDNKEYSYTFVDAQGHTHYFYNCYPKNANANGSGQTYVNPATAGDNNDYTASQSQQHINQYGYQSNVGPDASYYSHSNNNQAYNSHDGNGKVNYPNGTSNQNGGSASKATASGHAKDASWLTSRKQLQPYGQYHGGGAHYGVDYAMPENSPVYSLTDGTVVQAGWSNYGGGNQVTIKEANSNNYQWYMHNNRLTVSAGDKVKAGDQIAYSGSTGNSTAPHVHFQRMSGGIGNQYAVDPTSYLQSR
|
3.4.24.75
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:14687573}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:14687573};
|
cell wall organization [GO:0071555]; peptide catabolic process [GO:0043171]; proteolysis [GO:0006508]; septum digestion after cytokinesis [GO:0000920]
|
cell division site [GO:0032153]; cell outer membrane [GO:0009279]; extracellular region [GO:0005576]
|
cobalt ion binding [GO:0050897]; manganese ion binding [GO:0030145]; metalloendopeptidase activity [GO:0004222]; nickel cation binding [GO:0016151]; zinc ion binding [GO:0008270]
|
PF01551;
|
2.40.50.290;2.70.70.10;
|
Peptidase M23B family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10220159, ECO:0000269|PubMed:20472795}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans.; EC=3.4.24.75;
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-8. {ECO:0000269|PubMed:10220159};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable at 100 degrees Celsius for 15 minutes, but loses activity at the same temperature within 30 minutes. {ECO:0000269|PubMed:10220159};
|
FUNCTION: Peptidoglycan hydrolase (autolysin) specifically acting on polyglycine interpeptide bridges of the cell wall peptidoglycan. {ECO:0000269|PubMed:10220159, ECO:0000269|PubMed:8095258}.
|
Staphylococcus aureus (strain NCTC 8325 / PS 47)
|
O33830
|
AGLA_THEMA
|
MPSVKIGIIGAGSAVFSLRLVSDLCKTPGLSGSTVTLMDIDEERLDAILTIAKKYVEEVGADLKFEKTMNLDDVIIDADFVINTAMVGGHTYLEKVRQIGEKYGYYRGIDAQEFNMVSDYYTFSNYNQLKYFVDIARKIEKLSPKAWYLQAANPIFEGTTLVTRTVPIKAVGFCHGHYGVMEIVEKLGLEEEKVDWQVAGVNHGIWLNRFRYNGGNAYPLLDKWIEEKSKDWKPENPFNDQLSPAAIDMYRFYGVMPIGDTVRNSSWRYHRDLETKKKWYGEPWGGADSEIGWKWYQDTLGKVTEITKKVAKFIKENPSVRLSDLGSVLGKDLSEKQFVLEVEKILDPERKSGEQHIPFIDALLNDNKARFVVNIPNKGIIHGIDDDVVVEVPALVDKNGIHPEKIEPPLPDRVVKYYLRPRIMRMEMALEAFLTGDIRIIKELLYRDPRTKSDEQVEKVIEEILALPENEEMRKHYLKR
|
3.2.1.20
|
COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|PubMed:10972187}; Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:10972187}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:10972187}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:10972187}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:10972187}; Note=Binds 1 Mn(2+) ion per subunit. Can also use Co(2+) and Ni(2+) ions, albeit less efficiently than manganese ion. {ECO:0000269|PubMed:10972187};
| null | null |
maltose alpha-glucosidase activity [GO:0032450]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]
|
PF02056;PF11975;
|
3.90.1820.10;
|
Glycosyl hydrolase 4 family
| null | null |
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 mM for p-nitrophenyl-alpha-D-glucopyranoside {ECO:0000269|PubMed:10972187, ECO:0000269|PubMed:12062450}; KM=0.53 mM for p-nitrophenyl-alpha-D-galactopyranoside {ECO:0000269|PubMed:10972187, ECO:0000269|PubMed:12062450}; Vmax=9.94 umol/min/mg enzyme with p-nitrophenyl-alpha-D-glucopyranoside as substrate {ECO:0000269|PubMed:10972187, ECO:0000269|PubMed:12062450}; Vmax=11.42 umol/min/mg enzyme with p-nitrophenyl-alpha-D-galactopyranoside as substrate {ECO:0000269|PubMed:10972187, ECO:0000269|PubMed:12062450};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. Active from pH 6.5 to 9. {ECO:0000269|PubMed:10972187};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 90 degrees Celsius. Active from 60 to 105 degrees Celsius. Highly thermostable. {ECO:0000269|PubMed:10972187};
|
FUNCTION: Alpha-glycosidase with a very broad specificity. Hydrolyzes maltose and other small maltooligosaccharides but is inactive against the polymeric substrate starch. AglA is not specific with respect to the configuration at the C-4 position of its substrates because glycosidic derivatives of D-galactose are also hydrolyzed. Does not cleave beta-glycosidic bonds.
|
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
|
O33832
|
BSUHB_THEMA
|
MDRLDFSIKLLRKVGHLLMIHWGRVDNVEKKTGFKDIVTEIDREAQRMIVDEIRKFFPDENIMAEEGIFEKGDRLWIIDPIDGTINFVHGLPNFSISLAYVENGEVKLGVVHAPALNETLYAEEGSGAFFNGERIRVSENASLEECVGSTGSYVDFTGKFIERMEKRTRRIRILGSAALNAAYVGAGRVDFFVTWRINPWDIAAGLIIVKEAGGMVTDFSGKEANAFSKNFIFSNGLIHDEVVKVVNEVVEEIGGK
|
3.1.3.11; 3.1.3.25
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10508089};
|
inositol metabolic process [GO:0006020]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; signal transduction [GO:0007165]
| null |
fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; inositol monophosphate 1-phosphatase activity [GO:0008934]; inositol monophosphate 3-phosphatase activity [GO:0052832]; inositol monophosphate 4-phosphatase activity [GO:0052833]; metal ion binding [GO:0046872]
|
PF00459;
|
3.40.190.80;3.30.540.10;
|
Inositol monophosphatase superfamily, FBPase class 4 family
| null | null |
CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:11062561}; CATALYTIC ACTIVITY: Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate; Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268, ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25; Evidence={ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.145 mM for DL-inositol-1-phosphate (at 95 degrees Celsius) {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561}; KM=0.126 mM for D-inositol-1-phosphate (at 95 degrees Celsius) {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561}; KM=0.46 mM for inositol-2-phosphate (at 95 degrees Celsius) {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561}; Vmax=443 umol/min/mg enzyme with D-inositol-1-phosphate as substrate (at 95 degrees Celsius) {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561}; Vmax=23 umol/min/mg enzyme with L-inositol-1-phosphate as substrate (at 95 degrees Celsius) {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561}; Vmax=5.8 umol/min/mg enzyme with inositol-2-phosphate as substrate (at 95 degrees Celsius) {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561}; Note=kcat is 207 sec(-1) for IMPase activity (at 95 degrees Celsius) and 268 sec(-1) for FBPase activity (at 95 degrees Celsius). {ECO:0000269|PubMed:11062561};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. No loss of IMPase activity after incubation at 85 degrees Celsius for 30 minutes. Heating at 100 degrees Celsius for 10 minutes results in a loss of about 20 to 25% of the activity, and 30 minutes at this temperature inactivate about 70% of the activity. {ECO:0000269|PubMed:10508089};
|
FUNCTION: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P) but displaying a 20-fold higher rate of hydrolysis of D-I-1-P than of the L isomer, 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, 5'-AMP and NAD(+). May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate. {ECO:0000269|PubMed:10508089, ECO:0000269|PubMed:11062561}.
|
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
|
O33855
|
MIG_MYCAV
|
MSDTTTAFTVPAVAKAVAAAIPDRELIIQGDRRYTYRQVIERSNRLAAYLHSQGLGCHTEREALAGHEVGQDLLGLYAYNGNEFVEALLGAFAARVAPFNVNFRYVKSELHYLLADSEATALIYHAAFAPRVAEILPELPRLRVLIQIADESGNELLDGAVDYEDALASVSAQPPPVRHCPDDLYVLYTGGTTGMPKGVLWRQHDIFMTSFGGRNLMTGEPSSSIDEIVQRAASGPGTKLMILPPLIHGAAQWSVMTAITTGQTVVFPTVVDHLDAEDVVRTIEREKVMVVTVVGDAMARPLVAAIEKGIADVSSLAVVANGGALLTPFVKQRLIEVLPNAVVVDGVGSSETGAQMHHMSTPGAVATGTFNAGPDTFVAAEDLSAILPPGHEGMGWLAQRGYVPLGYKGDAAKTAKTFPVIDGVRYAVPGDRARHHADGHIELLGRDSVCINSGGEKIFVEEVETAIASHPAVADVVVAGRPSERWGQEVVAVVALSDGAAVDAGELIAHASNSLARYKLPKAIVFRPVIERSPSGKADYRWAREQAVNG
|
6.2.1.2
| null |
fatty acid metabolic process [GO:0006631]
|
extracellular region [GO:0005576]
|
ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]; medium-chain fatty acid-CoA ligase activity [GO:0031956]
|
PF00501;PF13193;
|
3.30.300.30;3.40.50.12780;
|
ATP-dependent AMP-binding enzyme family
| null |
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:9353032}.
|
CATALYTIC ACTIVITY: Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2; Evidence={ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341; Evidence={ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA; Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741; Evidence={ECO:0000269|PubMed:11690636}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + heptanoate = AMP + diphosphate + heptanoyl-CoA; Xref=Rhea:RHEA:44088, ChEBI:CHEBI:30616, ChEBI:CHEBI:32362, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:78811, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44089; Evidence={ECO:0000269|PubMed:11690636}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA; Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632; Evidence={ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + decanoate = AMP + decanoyl-CoA + diphosphate; Xref=Rhea:RHEA:33627, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628; Evidence={ECO:0000269|PubMed:11690636}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA; Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624; Evidence={ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + tetradecanoate = AMP + diphosphate + tetradecanoyl-CoA; Xref=Rhea:RHEA:33619, ChEBI:CHEBI:30616, ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620; Evidence={ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616, ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608; Evidence={ECO:0000269|PubMed:11690636}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoate + ATP + CoA = (9Z,12Z,15Z)-octadecatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44936, ChEBI:CHEBI:30616, ChEBI:CHEBI:32387, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:74034, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44937; Evidence={ECO:0000269|PubMed:11690636}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:11690636}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714; Evidence={ECO:0000269|PubMed:11690636};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=285 uM for octanoic acid {ECO:0000269|PubMed:11690636}; KM=1775 uM for decanoic acid {ECO:0000269|PubMed:11690636}; KM=20 uM for dodecanoic acid {ECO:0000269|PubMed:11690636}; KM=36 uM for ATP {ECO:0000269|PubMed:11690636}; KM=45 uM for CoA {ECO:0000269|PubMed:11690636}; Vmax=183 nmol/min/mg enzyme with octanoic acid as substrate {ECO:0000269|PubMed:11690636}; Vmax=510 nmol/min/mg enzyme with decanoic acid as substrate {ECO:0000269|PubMed:11690636}; Vmax=163 nmol/min/mg enzyme with dodecanoic acid as substrate {ECO:0000269|PubMed:11690636};
|
PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000269|PubMed:11690636}.
| null | null |
FUNCTION: Catalyzes the activation of medium-chain fatty acids as acyl-coenzyme A (acyl-CoA) (PubMed:11690636, PubMed:19477415). Shows maximal activity with saturated fatty acids of medium-chain length between C6 and C12. Has lower activity with tridecanoic acid (C13), tetradecanoic acid (C14) and with unsaturated fatty acids like oleic acid (C18:1), linolenic acid (C18:3) and arachidonic acid (C20:4). Shows weak activity with some aromatic carbon acids (PubMed:11690636). Involved in the metabolism of fatty acid during mycobacterial survival in macrophages (PubMed:11690636). {ECO:0000269|PubMed:11690636, ECO:0000269|PubMed:19477415}.
|
Mycobacterium avium
|
O34002
|
PRPC_ABDS2
|
MTEPTIHKGLAGVTADVTAISKVNSDTNSLLYRGYPVQELAAKCSFEQVAYLLWNSELPNDSELKAFVNFERSHRKLDENVKGAIDLLSTACHPMDVARTAVSVLGANHARAQDSSPEANLEKAMSLLATFPSVVAYDQRRRRGEELIEPREDLDYSANFLWMTFGEEAAPEVVEAFNVSMILYAEHSFNASTFTARVITSTLADLHSAVTGAIGALKGPLHGGANEAVMHTFEEIGIRKDESLDEAATRSKAWMVDALAQKKKVMGFGHRVYKNGDSRVPTMKSALDAMIKHYDRPEMLGLYNGLEAAMEEAKQIKPNLDYPAGPTYNLMGFDTEMFTPLFIAARITGWTAHIMEQVADNALIRPLSEYNGPEQRQVP
|
2.3.3.16; 2.3.3.5
| null |
carbohydrate metabolic process [GO:0005975]; propionate metabolic process, methylcitrate cycle [GO:0019679]; tricarboxylic acid cycle [GO:0006099]
|
cytosol [GO:0005829]
|
2-methylcitrate synthase activity [GO:0050440]; citrate (Si)-synthase activity [GO:0004108]; citrate synthase activity [GO:0036440]
|
PF00285;
|
1.10.580.10;1.10.230.10;
|
Citrate synthase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + oxaloacetate + propanoyl-CoA = (2S,3S)-2-methylcitrate + CoA + H(+); Xref=Rhea:RHEA:23780, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:58853; EC=2.3.3.5; Evidence={ECO:0000269|PubMed:9579066}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+); Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.16; Evidence={ECO:0000269|PubMed:9310359, ECO:0000269|PubMed:9579066};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3 uM for oxaloacetate (with propionyl-CoA at pH 8 and 23 degrees Celsius) {ECO:0000269|PubMed:9579066}; KM=6.9 uM for oxaloacetate (with acetyl-CoA at pH 8 and 23 degrees Celsius) {ECO:0000269|PubMed:9310359}; KM=7 uM for oxaloacetate (with acetyl-CoA at pH 8 and 23 degrees Celsius) {ECO:0000269|PubMed:9579066}; KM=16 uM for propionyl-CoA (at pH 8 and 23 degrees Celsius) {ECO:0000269|PubMed:9579066}; KM=229 uM for acetyl-CoA (at pH 8 and 23 degrees Celsius) {ECO:0000269|PubMed:9579066}; KM=230 uM for acetyl-CoA (at pH 8 and 23 degrees Celsius) {ECO:0000269|PubMed:9310359}; Vmax=12 umol/min/mg enzyme with propionyl-CoA as substrate (at pH 8 and 23 degrees Celsius) {ECO:0000269|PubMed:9579066}; Vmax=30 umol/min/mg enzyme with acetyl-CoA as substrate (at pH 8 and 23 degrees Celsius) {ECO:0000269|PubMed:9310359, ECO:0000269|PubMed:9579066}; Note=kcat is 8 sec(-1) for 2-methylcitrate synthase activity with propionyl-CoA as substrate (at pH 8 and 23 degrees Celsius). kcat is 21 sec(-1) for citrate synthase activity with acetyl-CoA as substrate (at pH 8 and 23 degrees Celsius). {ECO:0000269|PubMed:9310359, ECO:0000269|PubMed:9579066};
|
PATHWAY: Organic acid metabolism; propanoate degradation. {ECO:0000305|PubMed:9579066}.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2. {ECO:0000305|PubMed:9579066}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 31 degrees Celsius. Cold-active. Is rapidly inactivated at 45 degrees Celsius, and shows significant activity at 10 degrees Celsius and below. {ECO:0000269|PubMed:9310359};
|
FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA but with a lower specificity. {ECO:0000269|PubMed:9310359, ECO:0000269|PubMed:9579066}.
|
Antarctic bacterium DS2-3R
|
O34153
|
GLPK_ENTCA
|
MAEKNYVMAIDQGTTSSRAIIFDRNGKKIGSSQKEFPQYFPKSGWVEHNANEIWNSVQSVIAGAFIESGIRPEAIAGIGITNQRETTVVWDKTTGQPIANAIVWQSRQSSPIADQLKVDGHTEMIHEKTGLVIDAYFSATKVRWLLDNIEGAQEKADNGELLFGTIDSWLVWKLTDGQVHVTDYSNASRTMLYNIHKLEWDQEILDLLNIPSSMLPEVKSNSEVYGHTRSYHFYGSEVPIAGMAGDQQAALFGQMAFEKGMIKNTYGTGAFIVMNTGEEPQLSDNDLLTTIGYGINGKVYYALEGSIFVAGSAIQWLRDGLRMIETSPQSEELAAKAKGDNEVYVVPAFTGLGAPYWDSEARGAVFGLTRGTTKEDFVRATLQAVAYQSKDVIDTMKKDSGIDIPLLKVDGGAAKNDLLMQFQADILDIDVQRAANLETTALGAAYLAGLAVGFWKDLDELKSMAEEGQMFTPEMPAEERDNLYEGWKQAVAATQTFKFKAKKEGE
|
2.7.1.30
| null |
glycerol catabolic process [GO:0019563]; glycerol metabolic process [GO:0006071]; glycerol-3-phosphate biosynthetic process [GO:0046167]; phosphorylation [GO:0016310]; triglyceride metabolic process [GO:0006641]
|
cytosol [GO:0005829]
|
ATP binding [GO:0005524]; glycerol kinase activity [GO:0004370]
|
PF02782;PF00370;
|
3.30.420.40;
|
FGGY kinase family
|
PTM: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), including enzyme I, and histidine-containing protein (HPr) are required for the phosphorylation of His-232, which leads to the activation of the enzyme. {ECO:0000269|PubMed:9162046}.
| null |
CATALYTIC ACTIVITY: Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216; EC=2.7.1.30; Evidence={ECO:0000255|HAMAP-Rule:MF_00186};
| null |
PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00186}.
| null | null |
FUNCTION: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00186, ECO:0000269|PubMed:9162046}.
|
Enterococcus casseliflavus (Enterococcus flavescens)
|
O34154
|
GLPK_ENTFA
|
MAEEKYIMAIDQGTTSSRAIIFDKKGNKIGSSQKEFTQYFPNAGWVEHNANEIWNSVQSVIAGSLIESGVKPTDIAGIGITNQRETTVVWDKATGLPIYNAIVWQSRQTTPIADQLKEDGYSEMIHEKTGLIIDAYFSATKVRWILDHVEGAQERAENGELMFGTIDTWLVWKLTGDTHVTDYSNASRTMLFNIHDLDWDQEILDLLNIPRVMLPKVVSNSEVYGLTKNYHFYGSEVPIAGMAGDQQAALFGQMAFEPGMVKNTYGTGSFIVMNTGEEPQLSKNNLLTTIGYGINGKVYYALEGSIFVAGSAIQWLRDGLKMLQTAAESEAVAKASTGHNEVYVVPAFTGLGAPYWDSQARGAVFGLTRGTTREDFVKATLQAVAYQVRDIIDTMKEDTGIDIPVLKVDGGAANNDFLMQFQADILNTAVQRAHNLETTALGAAFLAGLAVGFWKDLEEIKAFQEEGQQFEPIMAEEEREDLYEGWQQAVAATQQFKRKNK
|
2.7.1.30
| null |
glycerol catabolic process [GO:0019563]; glycerol metabolic process [GO:0006071]; glycerol-3-phosphate biosynthetic process [GO:0046167]; phosphorylation [GO:0016310]; triglyceride metabolic process [GO:0006641]
|
cytosol [GO:0005829]
|
ATP binding [GO:0005524]; glycerol kinase activity [GO:0004370]
|
PF02782;PF00370;
|
3.30.420.40;
|
FGGY kinase family
|
PTM: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), including enzyme I, and histidine-containing protein (HPr) are required for the phosphorylation of His-231, which leads to the activation of the enzyme. {ECO:0000269|PubMed:3011747}.
| null |
CATALYTIC ACTIVITY: Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216; EC=2.7.1.30; Evidence={ECO:0000255|HAMAP-Rule:MF_00186};
| null |
PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00186}.
| null | null |
FUNCTION: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00186, ECO:0000269|PubMed:9162046}.
|
Enterococcus faecalis (strain ATCC 700802 / V583)
|
O34162
|
HEMN_CUPNH
|
MIPSAITSPAPDRRALSDFRALAGRIDGNGPRYTSYPTADRFHNGPDLSLYHDALAACRADAPAPLSLYLHIPFCENICYYCGCNKIITRDHGRSARYVNYLGREMALVADRLGPRRQVLQSHWGGGTPTFLDPGEMRRVMALLHEHFELAAEGEHSIEIDPRRVDHARMALLAELGFNRVSLGVQDFDPEVQQAIHRIQPFEETRAVVDAARTLGFRSVSLDLIYGLPHQTAARFGRTIDQVLALRPDRLSVYSYAHLPHVFKPQRRIDENALPPAGEKLDILVSTIERLSAEGYVYIGMDHFALPDDDLAVAQREGRLQRNFQGYSTHAGYDQVGLGISAIGAIAGRYVQNARTLDEYYGALDHGRLPLARGVAMSADDHLRREIIGALMCNGVLDIPALEARHGIRFGTAFAPELADLAALGADGLVQCAPDRITVTPLGRLLVRRVAMVFDRYLREDAARPASTGAQAVAANDGAQPVRFVPRARYSRVV
|
1.3.98.3
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P32131}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250|UniProtKB:P32131};
|
porphyrin-containing compound biosynthetic process [GO:0006779]; protoporphyrinogen IX biosynthetic process [GO:0006782]
|
cytoplasm [GO:0005737]
|
4 iron, 4 sulfur cluster binding [GO:0051539]; coproporphyrinogen dehydrogenase activity [GO:0051989]; coproporphyrinogen oxidase activity [GO:0004109]; metal ion binding [GO:0046872]
|
PF06969;PF04055;
|
1.10.10.920;3.80.30.20;
|
Anaerobic coproporphyrinogen-III oxidase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32131}.
|
CATALYTIC ACTIVITY: Reaction=coproporphyrinogen III + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + 2 CO2 + 2 L-methionine + protoporphyrinogen IX; Xref=Rhea:RHEA:15425, ChEBI:CHEBI:16526, ChEBI:CHEBI:17319, ChEBI:CHEBI:57307, ChEBI:CHEBI:57309, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=1.3.98.3; Evidence={ECO:0000250|UniProtKB:P32131};
| null |
PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet route): step 1/1.
| null | null |
FUNCTION: Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX. {ECO:0000269|PubMed:9396835}.
|
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha)
|
O34313
|
NTPES_BACSU
|
MRIQKRRTHVENILRILLPPIMILSLILPTPPIHAEESAAPQVHLSILATTDIHANMMDYDYYSDKETADFGLARTAQLIQKHREQNPNTLLVDNGDLIQGNPLGEYAVKYQKDDIISGTKTHPIISVMNALKYDAGTLGNHEFNYGLDFLDGTIKGADFPIVNANVKTTSGENRYTPYVINEKTLIDENGNEQKVKVGYIGFVPPQIMTWDKKNLEGQVQVQDIVESANETIPKMKAEGADVIIALAHTGIEKQAQSSGAENAVFDLATKTKGIDAIISGHQHGLFPSAEYAGVAQFNVEKGTINGIPVVMPSSWGKYLGVIDLKLEKADGSWKVADSKGSIESIAGNVTSRNETVTNTIQQTHQNTLEYVRKPVGKTEADINSFFAQVKDDPSIQIVTDAQKWYAEKEMKDTEYKNLPILSAGAPFKAGGRNGANYYTNIPAGDLAIKNVGDLYLYDNTVQIVKLTGSEVKDWLEMSAGQFNQIDPAKGGDQALLNENFRSYNFDVIDGVTYQVDVTKPAKYNENGKVINADSSRIINLSYEGKPISPSQEFLVVTNNYRASGGGGFPHLTSDKIVHGSAVENRQVLMDYIIEQKTVNPKADNNWSIAPVSGTNLTFESSLLAKPFADKADDVAYVGKSANEGYGVYKLQFDDDSNPDPPKDGLWDLTVMHTNDTHAHLDDAARRMTKINEVRSETNHNILLDAGDVFSGDLYFTKWNGLADLKMMNMMGYDAMTFGNHEFDKGPTVLSDFLSGNSATVDPANRYHFEAPEFPIVSANVDVSNEPKLKSFVKKPQTFTAGEKKEAGIHPYILLDVDGEKVAVFGLTTEDTATTSSPGKSIVFNDAFETAQNTVKAIQEEEKVNKIIALTHIGHNRDLELAKKVKGIDLIIGGHTHTLVDKMEVVNNEEPTIVAQAKEYGQFLGRVDVAFDEKGVVQTDKSNLSVLPIDEHTEENPEAKQELDQFKNELEDVKNEKVGYTDVALDGQREHVRTKETNLGNFIADGMLAKAKEAAGARIAITNGGGIRAGIDKGDITLGEVLNVMPFGNTLYVADLTGKQIKEALEQGLSNVENGGGAFPQVAGIEYTFTLNNKPGHRVLEVKIESPNGDKVAINTDDTYRVATNNFVGAGGDGYSVFTEASHGEDLGYVDYEIFTEQLKKLGNKVSPKVEGRIKEVFLPTKQKDGSWTLDEDKFAIYAKNANTPFVYYGIHEGSQEKPINLKVKKDQVKLLKERESDPSLTMFNYWYSMKMPMANLKTADTAIGIKSTGELDVSLSDVYDFTVKQKGKEIKSFKEPVQLSLRMFDIEEAHNPAIYHVDRKKKAFTKTGHGSVDDDMVTGYTNHFSEYTILNSGSNNKPPAFPSDQPTGGDDGNHGGGSDKPGGKQPTDGNGGNDTPPGTQPTNGSGGNGSGGSGTDGPAGGLLPDTATSMYSILLAGFLISALGTAMYLHQRRKQNRANQA
|
3.1.3.5; 3.1.3.6; 3.1.4.16
|
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250};
|
nucleotide catabolic process [GO:0009166]
|
extracellular region [GO:0005576]; outer membrane-bounded periplasmic space [GO:0030288]
|
2',3'-cyclic-nucleotide 2'-phosphodiesterase activity [GO:0008663]; 3'-nucleotidase activity [GO:0008254]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; XMP 5'-nucleosidase activity [GO:0106411]
|
PF02872;PF00149;
|
3.60.21.10;3.90.780.10;
|
5'-nucleotidase family
| null |
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:21800427, ECO:0000269|PubMed:21906378, ECO:0000305|PubMed:14688230}; Peptidoglycan-anchor {ECO:0000305|PubMed:14688230}. Note=Anchored to the cell wall by sortase SrtD. {ECO:0000269|PubMed:21800427, ECO:0000269|PubMed:21906378}.
|
CATALYTIC ACTIVITY: Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 3'-phosphate + H(+); Xref=Rhea:RHEA:19621, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:66949, ChEBI:CHEBI:66954; EC=3.1.4.16; Evidence={ECO:0000269|PubMed:14688230}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 3'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:10144, ChEBI:CHEBI:13197, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474; EC=3.1.3.6; Evidence={ECO:0000269|PubMed:14688230}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; Evidence={ECO:0000269|PubMed:14688230};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=The 2',3'-cyclic phosphodiesterase activity is higher than that of the 5'-nucleotidase with the four major nucleotides used as substrates. {ECO:0000269|PubMed:14688230};
| null | null | null |
FUNCTION: Catalyzes the release of inorganic phosphate from 2',3'-cyclic nucleotides through consecutive 2',3'-phosphodiesterase and 3'- (or 2') nucleotidase activities. Also possesses a 5'-nucleotidase activity. Does not catalyze the release of inorganic phosphate from 3',5'-cyclic nucleotides. Probably plays a role in the cellular reprocessing of nucleotides present in the medium, under conditions of phosphate shortage. {ECO:0000269|PubMed:14688230}.
|
Bacillus subtilis (strain 168)
|
O34327
|
RAPJ_BACSU
|
MRAKIPSEEVAVKLNEWYKLIRAFEADQAEALKQEIEYDLEDMEENQDLLLYFSLMEFRHRIMLDKLMPVKDSDTKPPFSDMLNEIESNQQKLTGLLEYYFYYFRGMYEFKQKNFILAIDHYKHAEEKLEYVEDEIEKAEFLFKVAEVYYHIKQTYFSMNYASQALDIYTKYELYGRRRVQCEFIIAGNLTDVYHHEKALTHLCSALEHARQLEEAYMIAAAYYNVGHCKYSLGDYKEAEGYFKTAAAIFEEHNFQQAVQAVFSLTHIYCKEGKYDKAVEAYDRGIKSAAEWEDDMYLTKFRLIHELYLGSGDLNVLTECFDLLESRQLLADAEDLLHDTAERFNQLEHYESAAFFYRRLMNIKKKLAEQRFQ
|
3.1.3.-
| null |
metabolic process [GO:0008152]; sporulation resulting in formation of a cellular spore [GO:0030435]
|
cytoplasm [GO:0005737]
|
phosphoprotein phosphatase activity [GO:0004721]
|
PF18801;
|
1.25.40.10;
|
Rap family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Involved in the regulation of sporulation (Probable). Acts as a phosphatase that specifically dephosphorylates the sporulation initiation phosphotransferase Spo0F and inhibits its activity (PubMed:21346797, PubMed:23526881). {ECO:0000269|PubMed:21346797, ECO:0000269|PubMed:23526881, ECO:0000305|PubMed:21346797}.
|
Bacillus subtilis (strain 168)
|
O34344
|
SDPC_BACSU
|
MKSKLLRLLIVSMVTILVFSLVGLSKESSTSAKENHTFSGEDYFRGLLFGQGEVGKLISNDLDPKLVKEANSTEGKKLVNDVVKFIKKDQPQYMDELKQSIDSKDPKKLIENMTKADQLIQKYAKKNENVKYSSNKVTPSCGLYAVCVAAGYLYVVGVNAVALQTAAAVTTAVWKYVAKYSSSASNNSDLEAAAAKTLKLIHQ
| null | null |
cell killing [GO:0001906]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]
|
extracellular region [GO:0005576]
|
toxin activity [GO:0090729]
| null | null | null |
PTM: Production of active SDP (able to induce SdpI and kill cells) is a multi-step process that requires signal peptide cleavage (probably by SipS or SipT) (PubMed:14568161) as well as SdpA and SdpB. The disulfide bond is not required for maximum toxicity (PubMed:23687264). {ECO:0000269|PubMed:14568161, ECO:0000269|PubMed:23687264}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12817086, ECO:0000269|PubMed:14568161, ECO:0000269|PubMed:23687264}. Note=Produces a secreted protein originating from this gene (PubMed:12817086), secreted by the general secretory pathway (PubMed:14568161).
| null | null | null | null | null |
FUNCTION: Produces a 42-residue extracellular sporulation delaying protein (SDP) that collapses the proton motive force (probably both the membrane potential and pH gradient) across the cell membrane, which leads to autolysis; may form a proton channel (PubMed:22469514). Induces the lysis of other B.subtilis cells that have not entered the sporulation pathway, inducing cannibalism to provide a source of nutrients to support sporulation, and at the same time delaying commitment to the energetically expensive and irreversible onset of sporulation (PubMed:12817086). Addition of SDP to liquid cultures halts growth, leads to increased cell permeability and eventually cell lysis in a significant subset of the population, although some cells survive and resume growth after a lag period (PubMed:20805502). Effects of SDP are irreversible within 10 minutes (PubMed:22469514). Addition of SDP to solid cultures induces killing, it is much more effective than SKF (AC O31422) (PubMed:20805502). Has antibiotic action against Gram-positive Firmicutes (L.acidophilus, M.megaterium, P.polymyxa, S.aureus, S.epidermidis) but not Actinobacteria M.luteus or Gram-negative P.aeruginosa or K.pneumoniae (PubMed:20805502, PubMed:22469514). SDP induces expression of the sdpR-sdpI operon (PubMed:12817086). Its maturation is dependent on SdpA and SdpB. Also functions as a ligand, binds to SdpI triggering a signal transduction cascade that protects the cell against the toxic effects of its own SDP. {ECO:0000269|PubMed:12817086, ECO:0000269|PubMed:16469701, ECO:0000269|PubMed:20805502, ECO:0000269|PubMed:22469514}.
|
Bacillus subtilis (strain 168)
|
O34398
|
LIGD_BACSU
|
MAFTMQPVLTSSPPIGAEWRYEVKYDGYRCILRIHSSGVTLTSRNGVELSSTFPEITQFAKTAFQHLEKELPLTLDGEIVCLVNPCRADFEHLQVRGRLKRPDKIQESANARPCCFLAFDLLERSGEDVTLLSYLDRKKSLRELISAAKLPASPDPYAKETIQSIPCYDHFDQLWEMVIKYDGEGIVAKKTNSKWLEKKRSSDWLKYKNFKQAYVCITGFNPNNGFLTVSVLKNGIMTPIASVSHGMRDEEKSAIREIMEQHGHQTPSGEFTLEPSICAAVQYLTILQGTLREVSFIGFEFQMDWTECTYAQVIRHSKPVHPKLQFTSLDKIIFEKNKKTKEDFIQYMIEVSDYLLPFLKNRAVTVIRYPHGSRSESFFQKNKPDYAPDFVQSFYDGSHEHIVCEDMSTLLWLCNQLALEFHVPFQTIKSRRPAEIVIDLDPPSRDDFLMAVQAANELKRLLDSFGITSYPKLSGNKGIQLYIPLSPEAFTYEETRQFTQLIAEYCTNAFPELFTTERLIKNRHCKLYLDYLQHAEGKTIICPYSTRGNELGTVAAPLYWHEVQSSLTPALFTIDTVIDRIKKQGCPFFDFYRNPQDEPLSAILHQLKKKS
|
6.5.1.1
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 3 Mn(2+); 2 Mn(2+) for polymerase/primase activity and 1 for ligase activity. {ECO:0000250};
|
DNA recombination [GO:0006310]; DNA repair [GO:0006281]; sporulation resulting in formation of a cellular spore [GO:0030435]
| null |
ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; DNA-directed DNA polymerase activity [GO:0003887]; exonuclease activity [GO:0004527]; metal ion binding [GO:0046872]
|
PF01068;PF21686;
|
3.30.470.30;3.90.920.10;
|
LigD polymerase family; ATP-dependent DNA ligase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1;
| null | null | null | null |
FUNCTION: With Ku forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity (Probable). Probably involved in DNA repair during spore germination. {ECO:0000305}.; FUNCTION: The preference of the polymerase domain for rNTPs over dNTPs may be advantageous in dormant cells, where the dNTP pool may be limiting. {ECO:0000250}.
|
Bacillus subtilis (strain 168)
|
O34403
|
FPG_BACSU
|
MPELPEVETVRRTLTGLVKGKTIKSVEIRWPNIIKRPAEPEEFARKLAGETIQSIGRRGKFLLFHLDHYVMVSHLRMEGKYGLHQAEEPDDKHVHVIFTMTDGTQLRYRDVRKFGTMHLFKPGEEAGELPLSQLGPEPDAEEFTSAYLKDRLAKTNRAVKTALLDQKTVVGLGNIYVDEALFRAGVHPETKANQLSDKTIKTLHAEIKNTLQEAIDAGGSTVRSYINSQGEIGMFQLQHFVYGKKDEPCKNCGTMISKIVVGGRGTHFCAKCQTKK
|
3.2.2.23; 4.2.99.18
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
base-excision repair [GO:0006284]
| null |
8-oxo-7,8-dihydroguanine DNA N-glycosylase activity [GO:0034039]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; zinc ion binding [GO:0008270]
|
PF01149;PF06831;PF06827;
|
1.10.8.50;3.20.190.10;
|
FPG family
| null | null |
CATALYTIC ACTIVITY: Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.; EC=3.2.2.23; CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18;
| null | null | null | null |
FUNCTION: Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 8-oxo-dGTP. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base. {ECO:0000250}.
|
Bacillus subtilis (strain 168)
|
O34425
|
G3P2_BACSU
|
MKVKVAINGFGRIGRMVFRKAMLDDQIQVVAINASYSAETLAHLIKYDTIHGRYDKEVVAGEDSLIVNGKKVLLLNSRDPKQLPWREYDIDIVVEATGKFNAKDKAMGHIEAGAKKVILTAPGKNEDVTIVMGVNEDQFDAERHVIISNASCTTNCLAPVVKVLDEEFGIESGLMTTVHAYTNDQKNIDNPHKDLRRARACGESIIPTTTGAAKALSLVLPHLKGKLHGLALRVPVPNVSLVDLVVDLKTDVTAEEVNEAFKRAAKTSMYGVLDYSDEPLVSTDYNTNPHSAVIDGLTTMVMEDRKVKVLAWYDNEWGYSCRVVDLIRHVAARMKHPSAV
|
1.2.1.59
| null |
gluconeogenesis [GO:0006094]; glucose metabolic process [GO:0006006]
|
cytosol [GO:0005829]
|
glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity [GO:0043891]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity [GO:0047100]; NAD binding [GO:0051287]; NADP binding [GO:0050661]
|
PF02800;PF00044;
|
3.40.50.720;
|
Glyceraldehyde-3-phosphate dehydrogenase family
|
PTM: In response to oxidative stress, the active site Cys likely reacts with bacillithiol (BSH) to form mixed disulfides to protect the Cys residue against overoxidation. S-bacillithiolation presumably leads to loss of catalytic activity. Debacillithiolation by monothiol bacilliredoxin BrxC restores the activity. {ECO:0000305|PubMed:33722570}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.59; Evidence={ECO:0000269|PubMed:10799476}; CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.59; Evidence={ECO:0000269|PubMed:10799476};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.86 mM for NADP (at pH 9.2 and 25 degrees Celsius) {ECO:0000269|PubMed:10799476}; KM=5.7 mM for NAD (at pH 9.2 and 25 degrees Celsius) {ECO:0000269|PubMed:10799476}; Note=kcat is 1 sec(-1) for dehydrogenase activity with NAD (at pH 9.2 and 25 degrees Celsius). kcat is 8 sec(-1) for dehydrogenase activity with NADP (at pH 9.2 and 25 degrees Celsius). {ECO:0000269|PubMed:10799476};
|
PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000269|PubMed:10799476}.
| null | null |
FUNCTION: Involved in the gluconeogenesis. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NADP. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NADP to NADPH. The reduced NADPH is then exchanged with the second NADP, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. {ECO:0000269|PubMed:10799476}.
|
Bacillus subtilis (strain 168)
|
O34431
|
ATCL_BACSU
|
MKFHEMGQTDLLEATNTSMKQGLTEKEVKKRLDKHGPNELQEGKKTSALLLFFAQFKDFMVLVLLAATLISGFLGEYVDAVAIIAIVFVNGILGFFQERRAEQSLQALKELSTPHVMALREGSWTKIPSKELVPGDIVKFTSGDRIGADVRIVEARSLEIEESALTGESIPVVKHADKLKKPDVSLGDITNMAFMGTIVTRGSGVGVVVGTGMNTAMGKIADMLESAGTLSTPLQRRLEQLGKILIVVALLLTVLVVAVGVIQGHDLYSMFLAGVSLAVAAIPEGLPAIVTVALSLGVQRMIKQKSIVRKLPAVETLGCASIICSDKTGTMTQNKMTVTHVWSGGKTWRVAGAGYEPKGSFTLNEKEISVNEHKPLQQMLLFGALCNNSNIEKRDGEYVLDGDPTEGALLTAARKGGFSKEFVESNYRVIEEFPFDSARKMMTVIVENQDRKRYIITKGAPDVLMQRSSRIYYDGSAALFSNERKAETEAVLRHLASQALRTIAVAYRPIKAGETPSMEQAEKDLTMLGLSGIIDPPRPEVRQAIKECREAGIKTVMITGDHVETAKAIAKDLRLLPKSGKIMDGKMLNELSQEELSHVVEDVYVFARVSPEHKLKIVKAYQENGHIVAMTGDGVNDAPAIKQADIGVSMGITGTDVAKEASSLVLVDDNFATIKSAIKEGRNIYENIRKFIRYLLASNVGEILVMLFAMLLALPLPLVPIQILWVNLVTDGLPAMALGMDQPEGDVMKRKPRHPKEGVFARKLGWKVVSRGFLIGVATILAFIIVYHRNPENLAYAQTIAFATLVLAQLIHVFDCRSETSVFSRNPFQNLYLIGAVLSSILLMLVVIYYPPLQPIFHTVAITPGDWMLVIGMSAIPTFLLAGSLLTRKK
|
7.2.2.10
| null |
monoatomic ion transmembrane transport [GO:0034220]
|
plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type calcium transporter activity [GO:0005388]; P-type ion transporter activity [GO:0015662]
|
PF13246;PF00689;PF00690;PF00122;
|
3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIA subfamily
|
PTM: Phosphorylated in a Ca(2+)-dependent manner starting 4 hours after shifting to sporulation medium. {ECO:0000269|PubMed:12161109}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12161109}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000269|PubMed:12161109};
| null | null | null | null |
FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. {ECO:0000269|PubMed:12161109}.
|
Bacillus subtilis (strain 168)
|
O34450
|
NAGA_BACSU
|
MAESLLIKDIAIVTENEVIKNGYVGINDGKISTVSTERPKEPYSKEIQAPADSVLLPGMIDIHIHGGYGADTMDASFSTLDIMSSRLPEEGTTSFLATTITQEHGNISQALVNAREWKAAEESSLLGAELLGIHLEGPFVSPKRAGAQPKEWIRPSDVELFKKWQQEAGGLIKIVTLAPEEDQHFELIRHLKDESIIASMGHTDADSALLSDAAKAGASHMTHLYNAMSPFHHREPGVIGTALAHDGFVTELIADGIHSHPLAAKLAFLAKGSSKLILITDSMRAKGLKDGVYEFGGQSVTVRGRTALLSDGTLAGSILKMNEGARHMREFTNCSWTDIANITSENAAKQLGIFDRKGSVTVGKDADLVIVSSDCEVILTICRGNIAFISKEADQI
|
3.5.1.25
|
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:14557261}; Note=Binds 2 divalent metal cations per subunit. {ECO:0000269|PubMed:14557261};
|
N-acetylglucosamine catabolic process [GO:0006046]; N-acetylneuraminate catabolic process [GO:0019262]
| null |
iron ion binding [GO:0005506]; N-acetylgalactosamine-6-phosphate deacetylase activity [GO:0047419]; N-acetylglucosamine-6-phosphate deacetylase activity [GO:0008448]; protein homodimerization activity [GO:0042803]
|
PF01979;
|
3.20.20.140;2.30.40.10;
|
Metallo-dependent hydrolases superfamily, NagA family
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-glucosamine 6-phosphate; Xref=Rhea:RHEA:22936, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=3.5.1.25; Evidence={ECO:0000269|PubMed:14557261};
| null |
PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 4/5. {ECO:0000305}.
| null | null |
FUNCTION: Involved in the first committed step in the biosynthesis of amino-sugar-nucleotides (PubMed:14557261). Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate (PubMed:14557261). Essential for growth on N-acetylglucosamine (PubMed:23667565). {ECO:0000269|PubMed:14557261, ECO:0000269|PubMed:23667565}.
|
Bacillus subtilis (strain 168)
|
O34481
|
RECD2_BACSU
|
MQQHPDQLKLEEEPYLKGTVNTVIYHNDTNLYTVLKVKVTETSEAIEDKAVSVTGYFPALQEEETYTFYGKIVTHPKFGLQFQAEHFKKEIPTTKEGIIQYLSSDLFEGIGKKTAEEIVKKLGDSAINKILADASVLYDVPRLSKKKADTLAGALQRHQGLEQIMISLNQFGFGPQLSMKIYQAYESETLEKIQENPYQLVKDVEGIGFGKADELGSRMGLSGNHPERVKAAILYTLETTCLSEGHTYIETEQLIIDTQSLLNQSAREGQRITEMDAANAIIALGENKDIVIEDGRCYFPSLFYAEQNVAKRVKHIASQTEYENQFPESEFLLALGELEERMDVQYAPSQKEAIQKALSSPMLLLTGGPGTGKTTVIRGIVELYGELHGVSLDPSAYKKDEAFPIVLAAPTGRAAKRMSESTGLPAVTIHRLLGWNGAEGFTHTEDQPIEGKLLIIDEASMLDIWLANHLFKAIPDHIQIIIVGDEDQLPSVGPGQVLRDLLASQVIPTVRLTDIYRQAEGSSIVELAHQMKNGLLPNNLTAPTKDRSFIRCGGSQIKEVVEKVVANALKKGYTAKDIQVLAPMYRGKAGINELNVMLQDILNPPKEKRRELKFGDVVYRTGDKILQLVNQPENNVFNGDIGEITSIFYAKENTEKEDMAVVSFDGNEMTFTKKDFNQFTHAYCCSIHKSQGSEFPIVVLPVVKGYYRMLRRNLLYTAITRAKKFLILCGEEEALEWGVKNNDATVRQTSLKNRLSVQVEEMDAELEALQKELPFSVHDANIGMEGITPFDFMKEEQQ
|
5.6.2.3
| null |
DNA recombination [GO:0006310]
|
cytoplasm [GO:0005737]; exodeoxyribonuclease V complex [GO:0009338]; nucleoid [GO:0009295]
|
5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; isomerase activity [GO:0016853]; single-stranded DNA helicase activity [GO:0017116]
|
PF13245;PF14490;PF18335;PF13538;
|
1.10.10.2220;2.30.30.940;3.40.50.300;
|
RecD family, RecD2 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:21170359}. Note=Found at the replication fork (PubMed:21170359). {ECO:0000269|PubMed:21170359}.
|
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction. This creates two antiparallel DNA single strands (ssDNA). The leading ssDNA polymer is the template for DNA polymerase III holoenzyme which synthesizes a continuous strand.; EC=5.6.2.3; Evidence={ECO:0000269|PubMed:24443534}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.3; Evidence={ECO:0000269|PubMed:35234892};
| null | null | null | null |
FUNCTION: In vivo may favor replication restart by preventing RecA from binding to blocked replication forks, avoiding unnecessary recombination during replication restart. Acts as a negative modulator of the RecA-ssDNA filament, may dissasemble RecA threads, can act as both a positive and negative regulator of strand exchange (PubMed:35234892). Probably stabilizes or aids normal replication fork progression, is important for survival after treatment with DNA-damaging agents that can result in replication fork stress (PubMed:24443534). Overcomes the inhibition of replication restart by RecA/RecO, probably by displacing RecA (PubMed:35234892). Increasing levels inhibit PriA-dependent DNA replication initiation (but have little effect on ongoing replication) in vitro; may act by disturbing SsbA assembly (PubMed:35234892). Does not seem to contribute to mismatch repair (PubMed:24443534). Has 5'-3' helicase activity that is probably ATP-dependent (PubMed:24443534). {ECO:0000255|HAMAP-Rule:MF_01488, ECO:0000269|PubMed:24443534, ECO:0000269|PubMed:35234892}.
|
Bacillus subtilis (strain 168)
|
O34483
|
HPRK_BACSU
|
MAKVRTKDVMEQFNLELISGEEGINRPITMSDLSRPGIEIAGYFTYYPRERVQLLGKTELSFFEQLPEEEKKQRMDSLCTDVTPAIILSRDMPIPQELIDASEKNGVPVLRSPLKTTRLSSRLTNFLESRLAPTTAIHGVLVDIYGVGVLITGKSGVGKSETALELVKRGHRLVADDCVEIRQEDQDTLVGNAPELIEHLLEIRGLGIINVMTLFGAGAVRSNKRITIVMNLELWEQGKQYDRLGLEEETMKIIDTEITKLTIPVRPGRNLAVIIEVAAMNFRLKRMGLNAAEQFTNKLADVIEDGEQEE
|
2.7.11.-; 2.7.4.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12009882}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12009882}; Note=The enzyme may harbor two different cation-binding sites, one that interacts specifically with the nucleotide, and the other that is involved in the binding of the protein substrate. {ECO:0000269|PubMed:12009882};
|
regulation of carbohydrate metabolic process [GO:0006109]
|
cytosol [GO:0005829]
|
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phosphorelay sensor kinase activity [GO:0000155]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]
|
PF07475;PF02603;
|
3.40.1390.20;3.40.50.300;
|
HPrK/P family
| null | null |
CATALYTIC ACTIVITY: Reaction=[HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:46600, Rhea:RHEA-COMP:11602, Rhea:RHEA-COMP:11603, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; CATALYTIC ACTIVITY: Reaction=[HPr protein]-O-phospho-L-serine + H(+) + phosphate = [HPr protein]-L-serine + diphosphate; Xref=Rhea:RHEA:46604, Rhea:RHEA-COMP:11602, Rhea:RHEA-COMP:11603, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=78 uM for HPr; KM=85 uM for P-Ser-HPr; KM=265 uM for phosphate; KM=785 uM for pyrophosphate;
| null | null | null |
FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of 'Ser-45' in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Also phosphorylates/dephosphorylates the HPr-like catabolite repression protein crh on 'Ser-46'. Therefore, by controlling the phosphorylation state of HPr and crh, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion. {ECO:0000269|PubMed:9987110}.
|
Bacillus subtilis (strain 168)
|
O34507
|
PRKC_BACSU
|
MLIGKRISGRYQILRVIGGGGMANVYLAEDIILDREVAIKILRFDYANDNEFIRRFRREAQSASSLDHPNIVSIYDLGEEDDIYYIVMEYVEGMTLKEYITANGPLHPKEALNIMEQIVSAIAHAHQNQIVHRDIKPHNILIDHMGNIKVTDFGIATALSSTTITHTNSVLGSVHYLSPEQARGGLATKKSDIYALGIVLFELLTGRIPFDGESAVSIALKHLQAETPSAKRWNPSVPQSVENIILKATAKDPFHRYETAEDMEADIKTAFDADRLNEKRFTIQEDEEMTKAIPIIKDEELAKAAGEKEAEVTTAQENKTKKNGKRKKWPWVLLTICLVFITAGILAVTVFPSLFMPKDVKIPDVSGMEYEKAAGLLEKEGLQVDSEVLEISDEKIEEGLMVKTDPKADTTVKEGATVTLYKSTGKAKTEIGDVTGQTVDQAKKALKDQGFNHVTVNEVNDEKNAGTVIDQNPSAGTELVPSEDQVKLTVSIGPEDITLRDLKTYSKEAASGYLEDNGLKLVEKEAYSDDVPEGQVVKQKPAAGTAVKPGNEVEVTFSLGPEKKPAKTVKEKVKIPYEPENEGDELQVQIAVDDADHSISDTYEEFKIKEPTERTIELKIEPGQKGYYQVMVNNKVVSYKTIEYPKDE
|
2.7.11.1
| null |
cellular response to peptidoglycan [GO:0071224]; protein phosphorylation [GO:0006468]; signal transduction [GO:0007165]; spore germination [GO:0009847]
|
plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; peptidoglycan binding [GO:0042834]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF03793;PF00069;PF21160;
|
2.60.40.2560;3.30.10.20;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
|
PTM: Autophosphorylation on threonine residue(s) and serine residue considerably increases the kinase activity of the protein. Dephosphorylated in vitro by PrpC. {ECO:0000269|PubMed:12406230, ECO:0000269|PubMed:12842463, ECO:0000269|PubMed:17218307}.
|
SUBCELLULAR LOCATION: Spore membrane {ECO:0000269|PubMed:18984160}; Single-pass type II membrane protein {ECO:0000269|PubMed:18984160}. Note=Is associated with the inner membrane of the spore.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Protein kinase that is responsible for triggering spore germination in response to muropeptides, signaling bacteria to exit dormancy. PrkC is thus a germination receptor that binds peptidoglycan fragments containing m-Dpm (meso-diaminopimelate), which act as spore germinants. Autophosphorylates and phosphorylates EF-G (elongation factor G, fusA); the latter modification is likely necessary for germination in response to peptidoglycan (PubMed:12399479). Another group did not detect phosphorylation of EF-G (PubMed:19246764). PrkC is a substrate in vitro of the cotranscribed phosphatase PrpC, which suggests that they form a functional couple in vivo. Might also be involved in sporulation and biofilm formation. Does not seem to be involved in stress response. {ECO:0000269|PubMed:12399479, ECO:0000269|PubMed:12406230, ECO:0000269|PubMed:18984160, ECO:0000269|PubMed:19246764}.
|
Bacillus subtilis (strain 168)
|
O34513
|
TMCAL_BACSU
|
MKAVGLVVEYNPFHNGHLYHAQTAKLQTGCDTAVAVMSGHFLQRGEPAVVSKWARTKMALQSGVDLVIELPYLYAVQKADIFARGSVSILNELECEALFFGSENGDIKPFLETAQLIDEHKHILNDRIKEELKKGASYPAAAAIAFSSILHTESALDLSKPNNILGYQYVTSILTGGYPMKPYTTARISSDYHDADLPEGENHIASATSIRKAMIGQNLEACLRFLPAASARELAAYRKSFGLWHTPESYFSYLKYSLSTVTARELQQVYEVEEGLEHRIIRSIRKSSSYQEFMELLKTKRYTWTRLQRMNTHILTRTKKQDMQKLLDNDKAPYIRLLGMTKKGQAYLSEKKKALSVPLVSKLSSFSHPALDLDVKASRIYSLPIEEPLRTEFDLQEYGHAPIRYDEDEQHFLNV
|
6.3.4.-
| null |
tRNA modification [GO:0006400]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; ligase activity, forming carbon-nitrogen bonds [GO:0016879]; tRNA binding [GO:0000049]
|
PF05636;
|
3.40.50.620;
|
TmcAL family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01539, ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP + diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met); Xref=Rhea:RHEA:58144, Rhea:RHEA-COMP:10693, Rhea:RHEA-COMP:10694, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456215; Evidence={ECO:0000255|HAMAP-Rule:MF_01539, ECO:0000269|PubMed:30150682};
| null | null | null | null |
FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34. {ECO:0000255|HAMAP-Rule:MF_01539, ECO:0000269|PubMed:30150682}.
|
Bacillus subtilis (strain 168)
|
O34521
|
PTWCB_BACSU
|
MLSFLQKLGKSFMLPIAVLPAVGIILALGREDVFNIPFVYQAGTAVFDHLPLIFAIGIAIGISKDSNGAAGLSGAISYLMLDAATKTIDKTNNMAVFGGIIAGLIAGYTYNRFKDTKLPEYLGFFSGRRLVPILTAIITIILAGIFGVVWPPIQSCINSFGEWMLGLGGIGAGIFGLFNRLLIPLGLHHVLNNIFWFQFGEYNGVTGDLARFFAKDPTAGTYMTGFFPIMMFGLPAACLAMVVTAKPSKRKATAGMMIGFALTAFITGITEPIEFAFMFLSPLLYAVHAVLTGLSLFIVNWLGIRSGFSFSAGAIDYVLSYGIAEKPLLLLLVGICYAAVYFIVFYVLIKALNLKTPGREDDDVDEVLDENTVQDVNENIMLKGLGGKENLQTIDHCATRLRLTVKDTALVDEALLKKAGAKGVVKSGGQSVQVIIGPNVEFAAEELRAAVK
|
2.7.1.193
| null |
N-acetylglucosamine transport [GO:0015764]; phosphoenolpyruvate-dependent sugar phosphotransferase system [GO:0009401]; phosphorylation [GO:0016310]
|
membrane raft [GO:0045121]; organelle inner membrane [GO:0019866]; plasma membrane [GO:0005886]
|
kinase activity [GO:0016301]; N-acetylglucosamine transmembrane transporter activity [GO:0015572]; protein-N(PI)-phosphohistidine-sugar phosphotransferase activity [GO:0008982]; protein-phosphocysteine-sugar phosphotransferase activity [GO:0090563]
|
PF00367;PF02378;
|
3.30.1360.60;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00426, ECO:0000269|PubMed:23651456}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00426}. Membrane raft {ECO:0000269|PubMed:23651456}; Multi-pass membrane protein. Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion. {ECO:0000269|PubMed:23651456}.
|
CATALYTIC ACTIVITY: Reaction=N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) = L-histidyl-[protein] + N-acetyl-D-glucosamine 6-phosphate(in); Xref=Rhea:RHEA:49240, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:29979, ChEBI:CHEBI:57513, ChEBI:CHEBI:64837, ChEBI:CHEBI:506227; EC=2.7.1.193; Evidence={ECO:0000305|PubMed:23667565};
| null | null | null | null |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (By similarity). This system is involved in N-acetylglucosamine transport (PubMed:23667565). {ECO:0000250|UniProtKB:P09323, ECO:0000269|PubMed:23667565}.
|
Bacillus subtilis (strain 168)
|
O34525
|
SPPA_BACSU
|
MNAKRWIALVIALGIFGVSIIVSISMSFFESVKGAQTDLTSLTDESQEKTLENGSPSSKIAVLEVSGTIQDNGDSSSLLGADGYNHRTFLKNLERAKDDKTVKGIVLKVNSPGGGVYESAEIHKKLEEIKKETKKPIYVSMGSMAASGGYYISTAADKIFATPETLTGSLGVIMESVNYSKLADKLGISFETIKSGAHKDIMSPSREMTKEEKNIMQSMVDNSYEGFVDVISKGRGMPKAEVKKIADGRVYDGRQAKKLNLVDELGFYDDTITAMKKDHKDLKNASVISYEESFGLGSLFSMGANKMFKSEIDFLNMREILSQSGSPRMMYLYAK
|
3.4.21.-
| null |
proteolysis [GO:0006508]
|
membrane raft [GO:0045121]; plasma membrane [GO:0005886]
|
serine-type peptidase activity [GO:0008236]
|
PF01343;
| null |
Peptidase S49 family
|
PTM: Autocatalytically cleaves its own C-terminus.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23651456, ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Membrane raft {ECO:0000269|PubMed:23651456}; Single-pass membrane protein. Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion. {ECO:0000269|PubMed:23651456}.
| null | null | null | null | null |
FUNCTION: Digestion of cleaved signal peptides (By similarity). Required for efficient processing of precursors under conditions of hyper-secretion. Has a preference for leucine-rich substrate peptides. {ECO:0000250, ECO:0000269|PubMed:10455123}.
|
Bacillus subtilis (strain 168)
|
O34527
|
CYMR_BACSU
|
MKISTKGRYGLTIMIELAKKHGEGPTSLKSIAQTNNLSEHYLEQLVSPLRNAGLVKSIRGAYGGYVLGSEPDAITAGDIIRVLEGPISPVEVLEDEEPAKRELWIRIRDAVKEVLDSTTLEDLASYTDGEQEAYMFYI
| null | null |
protein heterooligomerization [GO:0051291]; regulation of DNA-templated transcription [GO:0006355]
|
cytosol [GO:0005829]; protein-containing complex [GO:0032991]; protein-DNA complex [GO:0032993]
|
core promoter sequence-specific DNA binding [GO:0001046]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
|
PF02082;
|
1.10.10.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Master repressor of cysteine metabolism in B.subtilis. Controls the expression of genes involved either in cysteine synthesis from sulfide (cysK), sulfonates (ssu), or methionine (mccAB) or in cystine uptake (tcyP). Activity of CymR is positively regulated by CysK in response to cysteine availability. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression. {ECO:0000269|PubMed:16513748, ECO:0000269|PubMed:18974048}.
|
Bacillus subtilis (strain 168)
|
O34530
|
RSGA_BACSU
|
MPEGKIIKALSGFYYVLDESEDSDKVIQCRGRGIFRKNKITPLVGDYVVYQAENDKEGYLMEIKERTNELIRPPICNVDQAVLVFSAVQPSFSTALLDRFLVLVEANDIQPIICITKMDLIEDQDTEDTIQAYAEDYRNIGYDVYLTSSKDQDSLADIIPHFQDKTTVFAGQSGVGKSSLLNAISPELGLRTNEISEHLGRGKHTTRHVELIHTSGGLVADTPGFSSLEFTDIEEEELGYTFPDIREKSSSCKFRGCLHLKEPKCAVKQAVEDGELKQYRYDHYVEFMTEIKDRKPRY
|
3.6.1.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01820, ECO:0000269|PubMed:15223319}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01820, ECO:0000269|PubMed:15223319};
|
ribosomal small subunit biogenesis [GO:0042274]
|
cytoplasm [GO:0005737]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; rRNA binding [GO:0019843]
|
PF03193;PF16745;
|
2.40.50.140;3.40.50.300;
|
TRAFAC class YlqF/YawG GTPase family, RsgA subfamily
|
PTM: In vitro phosphorylated mostly on Thr (with lower signal on Ser) by PrkC in the presence of poly-L-Lys or myelin basic protein, dephosphorylated by PrpC (PubMed:19246764). Most in vitro phosphorylation occurs on Thr-166, in vivo phosphorylation has not been detected, but it might vary during the cell cycle (PubMed:22544754). {ECO:0000269|PubMed:19246764, ECO:0000269|PubMed:22544754}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01820}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30.5 uM for GTP {ECO:0000269|PubMed:16485133}; Note=kcat for GTP is 13.6 h(-1), in the absence of ribosomes. {ECO:0000269|PubMed:16485133};
| null | null | null |
FUNCTION: One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase with a low level of activity and slow catalytic turnover, does not act on ATP (PubMed:16485133). GTPase activity is stimulated by the presence of 30S or 70S ribosomes, phosphorylation increases stimulation (PubMed:22544754). Depletion results in increased sensitivity to protein synthesis inhibitors that block the peptide channel or peptidyl transferase center on the ribosome, suggesting this protein functions in conjunction with the ribosome in vivo (PubMed:15828870). Decreasing levels of protein lead to an increase in free 30S and 50S ribosomal subunits and a decrease in assembled 70S ribosomes (PubMed:15828870). Suggested to serve as a specific transcription factor for proteins involved in late stages of peptidoglycan synthesis (PubMed:18344364). {ECO:0000269|PubMed:15828870, ECO:0000269|PubMed:16485133, ECO:0000269|PubMed:18344364, ECO:0000269|PubMed:22544754}.
|
Bacillus subtilis (strain 168)
|
O34539
|
NDPGT_BACSU
|
MKKYHISMINIPAYGHVNPTLALVEKLCEKGHRVTYATTEEFAPAVQQAGGEALIYHTSLNIDPKQIREMMEKNDAPLSLLKESLSILPQLEELYKDDQPDLIIYDFVALAGKLFAEKLNVPVIKLCSSYAQNESFQLGNEDMLKKIREAEAEFKAYLEQEKLPAVSFEQLAVPEALNIVFMPKSFQIQHETFDDRFCFVGPSLGERKEKESLLIDKDDRPLMLISLGTAFNAWPEFYKMCIKAFRDSSWQVIMSVGKTIDPESLEDIPANFTIRQSVPQLEVLEKADLFISHGGMNSTMEAMNAGVPLVVIPQMYEQELTANRVDELGLGVYLPKEEVTVSSLQEAVQAVSSDQELLSRVKNMQKDVKEAGGAERAAAEIEAFMKKSAVPQ
|
2.4.1.384
| null |
antibiotic biosynthetic process [GO:0017000]; cellular glucuronidation [GO:0052695]
| null |
enzyme binding [GO:0019899]; hexosyltransferase activity [GO:0016758]; UDP-glycosyltransferase activity [GO:0008194]
|
PF06722;
|
3.40.50.2000;
|
UDP-glycosyltransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=an NDP-glycose + an acceptor = a glycosylated acceptor + NDP.; EC=2.4.1.384; Evidence={ECO:0000269|PubMed:28315700, ECO:0000269|PubMed:33152360};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=19.4 uM for apigenin {ECO:0000269|PubMed:28315700}; KM=22.6 uM for genistein {ECO:0000269|PubMed:28315700}; KM=6.795 uM for 2-chloro-4-nitrophenyl glycoside {ECO:0000269|PubMed:33152360}; Note=kcat is 1.9 sec(-1) with apigenin as substrate. kcat is 1.6 sec(-1) with genistein as substrate (PubMed:28315700). kcat is 164 min(-1) with 2-chloro-4-nitrophenyl glycoside as substrate (PubMed:33152360). {ECO:0000269|PubMed:28315700, ECO:0000269|PubMed:33152360};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is approximately 8.0. {ECO:0000269|PubMed:28315700};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-40 degrees Celsius. {ECO:0000269|PubMed:28315700};
|
FUNCTION: Glycosyltransferase that can glycosylate a wide range of substrates, including various flavonoids, phenyl ketones, curcuminoid, lignins, zingerone, triterpenes, stilbene and anthraquinone, using UDP-glucose or ADP-glucose as sugar donor (PubMed:28315700, PubMed:33152360). It also exhibits O-, N- and S-glycosylation activities towards simple aromatics (PubMed:28315700). In vivo, the broad acceptor tolerance of YjiC might function as a detoxification agent against exogenous xenobiotics to make the strain adaptable to the changeable environment (Probable). {ECO:0000269|PubMed:28315700, ECO:0000269|PubMed:33152360, ECO:0000305|PubMed:28315700}.
|
Bacillus subtilis (strain 168)
|
O34559
|
URHG2_BACSU
|
MGSMDQSIAVKSPLTYAEALANTIMNTYTVEELPPANRWHYHQGVFLCGVLRLWEATGEKRYFEYAKAYADLLIDDNGNLLFRRDELDAIQAGLILFPLYEQTKDERYVKAAKRLRSLYGTLNRTSEGGFWHKDGYPYQMWLDGLYMGGPFALKYANLKQETELFDQVVLQESLMRKHTKDAKTGLFYHAWDEAKKMPWANEETGCSPEFWARSIGWYVMSLADMIEELPKKHPNRHVWKNTLQDMIKSICRYQDKETGLWYQIVDKGDRSDNWLESSGSCLYMYAIAKGINKGYLDRAYETTLLKAYQGLIQHKTETSEDGAFLVKDICVGTSAGFYDYYVSRERSTNDLHGAGAFILAMTELEPLFRSAGK
|
3.2.1.172
| null |
carbohydrate metabolic process [GO:0005975]
|
cytoplasm [GO:0005737]
|
unsaturated rhamnogalacturonyl hydrolase activity [GO:0102211]
|
PF07470;
|
1.50.10.10;
|
Glycosyl hydrolase 105 family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnose + H2O = 5-dehydro-4-deoxy-D-glucuronate + L-rhamnopyranose; Xref=Rhea:RHEA:30927, ChEBI:CHEBI:15377, ChEBI:CHEBI:17117, ChEBI:CHEBI:62346, ChEBI:CHEBI:62478; EC=3.2.1.172;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=100 uM for unsaturated rhamnogalacturonan disaccharide (at pH 4 and 30 degrees Celsius) {ECO:0000269|PubMed:16781735};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. {ECO:0000269|PubMed:16781735};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. It is stable below 50 degrees Celsius. {ECO:0000269|PubMed:16781735};
|
FUNCTION: Catalyzes the hydrolysis of unsaturated rhamnogalacturonan disaccharide to yield unsaturated D-galacturonic acid and L-rhamnose. It cannot act on unsaturated glucuronyl hydrolase (UGL) substrates containing unsaturated D-glucuronic acid at the non-reducing terminus, although the active pockets of YesR and UGL are very similar. {ECO:0000269|PubMed:16781735}.
|
Bacillus subtilis (strain 168)
|
O34614
|
MNMM_BACSU
|
MILKKILPYSKELLKMAAGEGDIVVDATMGNGHDTQFLAELVGENGHVYAFDIQESAVANTKERLGDMYQARTTLFHKSHDKIAESLPPETHGKVAAAVFNLGYLPGGDKSITTNGSSTIKAIEQLLSIMKDEGLIVLVVYHGHPEGKAEKNDVLEFCRDLDQQTARVLTYGFINQQNDPPFIVAIEKKAQISK
|
2.1.1.61
| null |
methylation [GO:0032259]; tRNA processing [GO:0008033]
| null |
tRNA (5-methylaminomethyl-2-thiouridylate)(34)-methyltransferase activity [GO:0004808]
|
PF06962;
|
3.40.50.150;
|
Methyltransferase superfamily, MnmM family
| null | null |
CATALYTIC ACTIVITY: Reaction=5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19569, Rhea:RHEA-COMP:10195, Rhea:RHEA-COMP:10197, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74454, ChEBI:CHEBI:74455; EC=2.1.1.61; Evidence={ECO:0000269|PubMed:36762482}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19570; Evidence={ECO:0000269|PubMed:36762482};
| null |
PATHWAY: tRNA modification. {ECO:0000269|PubMed:36762482}.
| null | null |
FUNCTION: Involved in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA (PubMed:36762482). Catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34 to form mnm(5)s(2)U34 (PubMed:36762482). {ECO:0000269|PubMed:36762482}.
|
Bacillus subtilis (strain 168)
|
O34676
|
KAMA_BACSU
|
MKNKWYKPKRHWKEIELWKDVPEEKWNDWLWQLTHTVRTLDDLKKVINLTEDEEEGVRISTKTIPLNITPYYASLMDPDNPRCPVRMQSVPLSEEMHKTKYDLEDPLHEDEDSPVPGLTHRYPDRVLFLVTNQCSMYCRYCTRRRFSGQIGMGVPKKQLDAAIAYIRETPEIRDCLISGGDGLLINDQILEYILKELRSIPHLEVIRIGTRAPVVFPQRITDHLCEILKKYHPVWLNTHFNTSIEMTEESVEACEKLVNAGVPVGNQAVVLAGINDSVPIMKKLMHDLVKIRVRPYYIYQCDLSEGIGHFRAPVSKGLEIIEGLRGHTSGYAVPTFVVDAPGGGGKIALQPNYVLSQSPDKVILRNFEGVITSYPEPENYIPNQADAYFESVFPETADKKEPIGLSAIFADKEVSFTPENVDRIKRREAYIANPEHETLKDRREKRDQLKEKKFLAQQKKQKETECGGDSS
|
5.4.3.2
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:10839984}; Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000269|PubMed:10839984}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:10839984};
|
L-lysine catabolic process to acetate [GO:0019475]
| null |
4 iron, 4 sulfur cluster binding [GO:0051539]; lysine 2,3-aminomutase activity [GO:0050066]; metal ion binding [GO:0046872]
|
PF12544;PF04055;
|
6.10.140.1170;6.20.120.40;3.20.20.70;
|
Radical SAM superfamily, KamA family
| null | null |
CATALYTIC ACTIVITY: Reaction=L-lysine = (3S)-3,6-diaminohexanoate; Xref=Rhea:RHEA:19177, ChEBI:CHEBI:32551, ChEBI:CHEBI:57434; EC=5.4.3.2;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 mM for L-lysine;
|
PATHWAY: Amino-acid degradation; L-lysine degradation via acetate pathway.
| null | null |
FUNCTION: Catalyzes the interconversion of L-alpha-lysine and L-beta-lysine. {ECO:0000269|PubMed:21538109}.
|
Bacillus subtilis (strain 168)
|
O34680
|
YDIP_BACSU
|
MKVVSLFSGIGGIELGLHQSGHTTEIFCEVDPLAKAVLSKNFPGVKIEDDINEIRELPSCDLVAAGFPCQDLSQAGGKEGIDGSRSGLVKKLFELIEKKEHANRPPWILIENVPYMLRLNRGKAMSYLTSVLSELGYTWAYRTVDARCFGLPQRRHRVILLASLFEDPKDVIFSQDHSEPDLDGKPSVVDHSNYYGFYWTEGLRGVGWAREAVPPIKCGSSVGIASPPAVWSPYEDIVGTINIRDAERLQGFPEDWTNITTETGKDIKEGARWRLVGNAVSVRVSKWIGENLSQPKGSISDFEGELVTKTWPSAAWGYGDKKYKVPVSKWVANTEQIAISEFLNHPLKPLSARALNGFLGRAARCTNVNYSDEFINSLERCKDRQLQKV
|
2.1.1.37
| null |
DNA restriction-modification system [GO:0009307]; methylation [GO:0032259]
| null |
DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA binding [GO:0003677]; site-specific DNA-methyltransferase (adenine-specific) activity [GO:0009007]
|
PF00145;
|
3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37; Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.6 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:3150363}; KM=3 nM for DNA {ECO:0000269|PubMed:3150363};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:3150363};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Rapidly loses activity at 37 degrees Celsius in the absence of DNA. {ECO:0000269|PubMed:3150363};
|
FUNCTION: A methylase, recognizes the double-stranded sequence 5'-YTCGAR-3', methylates C-3 on both strands, and protects the DNA from cleavage by the BsuMI endonuclease. {ECO:0000269|PubMed:11751814, ECO:0000269|PubMed:3150363, ECO:0000269|PubMed:32324221}.
|
Bacillus subtilis (strain 168)
|
O34693
|
RQCH_BACSU
|
MSFDGMFTYGMTHELNEKIMGGRITKIHQPYKHDVIFHIRAKGKNQKLLLSAHPSYSRVHITAQAYENPSEPPMFCMLLRKHIEGGFIEKIEQAGLDRIMIFHIKSRNEIGDETVRKLYVEIMGRHSNIILTDAAENVIIDGLKHLSPSMNSYRTVLPGQDYKLPPAQDKISPLEASEDDILRHLSFQEGRLDKQIVDHFSGVSPLFAKEAVHRAGLANKVTLPKALLALFAEVKEHRFIPNITTVNGKEYFYLLELTHLKGEARRFDSLSELLDRFYFGKAERDRVKQQAQDLERFVVNERKKNANKIKKLEKTLEYSENAKEFQLYGELLTANLYMLKKGDKQAEVINYYDEESPTITIPLNPNKTPSENAQAYFTKYQKAKNSVAVVEEQIRLAQEEIEYFDQLIQQLSSASPRDISEIREELVEGKYLRPKQQKGQKKQKPHNPVLETYESTSGLTILVGKNNRQNEYLTTRVAARDDIWLHTKDIPGSHVVIRSSEPDEQTIMEAATIAAYFSKAKDSSSVPVDYTKIRHVKKPNGAKPGFVTYDSQHTVFVTPDADTVIKLKKS
| null | null |
rescue of stalled ribosome [GO:0072344]; ribosome-associated ubiquitin-dependent protein catabolic process [GO:1990116]
|
RQC complex [GO:1990112]
|
ribosomal large subunit binding [GO:0043023]; tRNA binding [GO:0000049]
|
PF05670;PF18297;PF05833;
|
1.10.8.50;3.40.970.40;2.30.310.10;
|
NEMF family
| null | null | null | null | null | null | null |
FUNCTION: Part of the ribosome quality control system (RQC). Recruits Ala-charged tRNA and directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal Ala extensions (Ala tail). The Ala tail promotes nascent chain degradation. Selectively binds tRNA(Ala)(UGC), which is presumably the sole source of tRNA(Ala) used for Ala tailing directed by this protein. May add between 1 and at least 8 Ala residues; detection of the Ala tail requires either deletion of clpP or its inhibition. Binds to 50S ribosomal subunits, at least 30% of which contain a P-site tRNA and thus are obstructed. {ECO:0000269|PubMed:31155236}.
|
Bacillus subtilis (strain 168)
|
O34714
|
OXDC_BACSU
|
MKKQNDIPQPIRGDKGATVKIPRNIERDRQNPDMLVPPETDHGTVSNMKFSFSDTHNRLEKGGYAREVTVRELPISENLASVNMRLKPGAIRELHWHKEAEWAYMIYGSARVTIVDEKGRSFIDDVGEGDLWYFPSGLPHSIQALEEGAEFLLVFDDGSFSENSTFQLTDWLAHTPKEVIAANFGVTKEEISNLPGKEKYIFENQLPGSLKDDIVEGPNGEVPYPFTYRLLEQEPIESEGGKVYIADSTNFKVSKTIASALVTVEPGAMRELHWHPNTHEWQYYISGKARMTVFASDGHARTFNYQAGDVGYVPFAMGHYVENIGDEPLVFLEIFKDDHYADVSLNQWLAMLPETFVQAHLDLGKDFTDVLSKEKHPVVKKKCSK
|
4.1.1.2
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11546787, ECO:0000269|PubMed:12056897}; Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:12056897};
|
oxalate metabolic process [GO:0033609]
|
cytoplasm [GO:0005737]; outer membrane-bounded periplasmic space [GO:0030288]
|
metal ion binding [GO:0046872]; oxalate decarboxylase activity [GO:0046564]
|
PF00190;
|
2.60.120.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:11546787}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + oxalate = CO2 + formate; Xref=Rhea:RHEA:16509, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:30623; EC=4.1.1.2; Evidence={ECO:0000269|PubMed:10960116, ECO:0000269|PubMed:11546787, ECO:0000269|PubMed:12056897};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15 mM for oxalate {ECO:0000269|PubMed:11546787}; Vmax=75 umol/min/mg enzyme {ECO:0000269|PubMed:11546787};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:10960116};
| null |
FUNCTION: Converts oxalate to formate and CO(2) in an O(2)-dependent reaction. Can also catalyze minor side reactions: oxalate oxidation to produce H(2)O(2), and oxalate-dependent, H(2)O(2)-independent dye oxidations. {ECO:0000269|PubMed:10960116, ECO:0000269|PubMed:11546787, ECO:0000269|PubMed:12056897}.
|
Bacillus subtilis (strain 168)
|
O34746
|
FABH1_BACSU
|
MKAGILGVGRYIPEKVLTNHDLEKMVETSDEWIRTRTGIEERRIAADDVFSSHMAVAAAKNALEQAEVAAEDLDMILVATVTPDQSFPTVSCMIQEQLGAKKACAMDISAACAGFMYGVVTGKQFIESGTYKHVLVVGVEKLSSITDWEDRNTAVLFGDGAGAAVVGPVSDDRGILSFELGADGTGGQHLYLNEKRHTIMNGREVFKFAVRQMGESCVNVIEKAGLSKEDVDFLIPHQANIRIMEAARERLELPVEKMSKTVHKYGNTSAASIPISLVEELEAGKIKDGDVVVMVGFGGGLTWGAIAIRWGR
|
2.3.1.180; 2.3.1.300
| null |
fatty acid biosynthetic process [GO:0006633]
|
cytoplasm [GO:0005737]
|
3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; beta-ketoacyl-acyl-carrier-protein synthase III activity [GO:0033818]; beta-ketodecanoyl-[acyl-carrier-protein] synthase activity [GO:0061990]
|
PF08545;PF08541;
|
3.40.47.10;
|
Thiolase-like superfamily, FabH family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=(2S)-2-methylbutanoyl-CoA + H(+) + malonyl-[ACP] = (4S)-4-methyl-3-oxohexanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42276, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:17148, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:78449, ChEBI:CHEBI:88166, ChEBI:CHEBI:167462; EC=2.3.1.300; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42277; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=2-methylpropanoyl-CoA + H(+) + malonyl-[ACP] = 4-methyl-3-oxopentanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42268, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9940, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338, ChEBI:CHEBI:78449, ChEBI:CHEBI:78820; EC=2.3.1.300; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42269; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=3-methylbutanoyl-CoA + H(+) + malonyl-[ACP] = 5-methyl-3-oxohexanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42272, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9941, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57345, ChEBI:CHEBI:78449, ChEBI:CHEBI:78822; EC=2.3.1.300; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42273; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12081; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + propanoyl-CoA = 3-oxopentanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42244, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9939, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:78449, ChEBI:CHEBI:78818; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42245; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=butanoyl-CoA + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42248, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9629, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:78449, ChEBI:CHEBI:78456; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42249; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + pentanoyl-CoA = 3-oxoheptanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42252, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9943, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57389, ChEBI:CHEBI:78449, ChEBI:CHEBI:78824; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42253; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=H(+) + hexanoyl-CoA + malonyl-[ACP] = 3-oxooctanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42256, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9633, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620, ChEBI:CHEBI:78449, ChEBI:CHEBI:78460; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42257; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=H(+) + heptanoyl-CoA + malonyl-[ACP] = 3-oxononanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42260, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9944, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:78449, ChEBI:CHEBI:78811, ChEBI:CHEBI:78826; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42261; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + octanoyl-CoA = 3-oxodecanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42264, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9637, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:78449, ChEBI:CHEBI:78464; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42265; Evidence={ECO:0000269|PubMed:10629181};
| null |
PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01815}.
| null | null |
FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for branched chain acyl-CoA, determining the biosynthesis of branched-chain of fatty acids instead of straight-chain. {ECO:0000269|PubMed:10629181}.
|
Bacillus subtilis (strain 168)
|
O34748
|
RECQ_BACSU
|
MLHRAQSLLAHYFGYEKFRSGQDEAIRLVTEARQNTACIMPTGGGKSICYQIPALMFEGTTIVISPLISLMKDQVDALEEAGINAAYINSTQSNQEIYERLNGLKEGAYKLFYITPERLTSIEFIRILQGIDVPLVAIDEAHCISQWGHDFRPSYRNIEILFRELHDKPVIMALTATATPEVHDDICKQLHIQKENTVYTGFSRENLTFKVVKGENKDRFIDEYVQNNRHEAGIVYTATRKEADRIYERLKRNQVRAGRYHGGLADDVRKEQQERFLNDELQVMVATSAFGMGIDKSNIRFVLHAQIPKDMESYYQEAGRAGRDGLASECVLLFSPQDIMVQRFLIEQSEHEEKQKQDLKKLRQMVDYCHTEDCLQRFILMYFGEKEPDACGQCGNCTDTRAAHDVTREAQMVLSCIIRMKERFGKTMVAQVLAGSKNKKVLENGFSDLSTYGILKHQSVGEISDFIEFLISDDFIRMSDGTFPTLFVSSKGRNVLKGELSVARKEALKAAAITENDELFERLRMVRKEIAAEQGVPPFVVFSDQTLKEMSGKQPVNDDELLSIKGVGEQKRAKYGRLFLQEIQAYARMTD
|
5.6.2.4
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25246477}; Note=Optimal helicase activity requires 0.8-1.2 Mg(2+) per ATP molecule (PubMed:25246477). {ECO:0000269|PubMed:25246477}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:25246477}; Note=Bind 1 Zn(2+) per monomer (PubMed:25246477). {ECO:0000269|PubMed:25246477};
|
DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via homologous recombination [GO:0000724]; G-quadruplex DNA unwinding [GO:0044806]; SOS response [GO:0009432]; telomere maintenance [GO:0000723]
|
bacterial nucleoid [GO:0043590]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; replisome [GO:0030894]
|
3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; four-way junction helicase activity [GO:0009378]; isomerase activity [GO:0016853]; metal ion binding [GO:0046872]
|
PF00270;PF00271;PF00570;PF16124;PF09382;
|
1.10.150.80;3.40.50.300;1.10.10.10;
|
Helicase family, RecQ subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:16385024}. Note=Localized throughout the nucleoid in the presence or absence of DNA double-strand breaks (PubMed:16385024). {ECO:0000269|PubMed:16385024}.
|
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000269|PubMed:25246477}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:25246477};
| null | null | null | null |
FUNCTION: An ATP-dependent DNA helicase which unwinds DNA in a 3'-5' direction (PubMed:25246477). Requires between 2 and 5 single-stranded nucleotides on the 3'-end to initiate unwinding, is not active on blunt-ended DNA (PubMed:25246477). Can target DNA replication, repair, and recombination intermediates; is active on forked, gapped and 3'-overhang DNA as well as 5'-flaps, Kappa joints, synthetic replication forks, and Holliday junctions (PubMed:25246477). Prefers ATP over dATP, is not active with other nucleotides (PubMed:25246477). Only unwinds short partial duplexes in vitro; SsbA enhances its activity on longer substrates (PubMed:25246477). Has ss- and dsDNA-stimulated ATPase activity (PubMed:25246477). Binds forked DNA strongly, ssDNA less well and dsDNA poorly (PubMed:25246477). Required for DNA repair and intramolecular recombination; probably has overlapping function with RecS (PubMed:16385024). It probably acts to help generate ssDNA from dsDNA breaks (PubMed:16385024, PubMed:25246477). {ECO:0000269|PubMed:16385024, ECO:0000269|PubMed:25246477}.
|
Bacillus subtilis (strain 168)
|
O34777
|
OHRR_BACSU
|
MENKFDHMKLENQLCFLLYASSREMTKQYKPLLDKLNITYPQYLALLLLWEHETLTVKKMGEQLYLDSGTLTPMLKRMEQQGLITRKRSEEDERSVLISLTEDGALLKEKAVDIPGTILGLSKQSGEDLKQLKSALYTLLETLHQKN
| null | null |
negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of DNA-templated transcription [GO:0006355]; response to hydrogen peroxide [GO:0042542]
|
cytoplasm [GO:0005737]
|
DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF01047;
|
1.10.10.10;
| null |
PTM: Cys-15 is oxidized by organic peroxides to cysteine sulfenic acid (Cys-SOH). This can react with the alpha-amido of the following residue to form the sulfenamide cross-link. Oxidation or cross-linking results in the loss of DNA-binding activity and the inactivation of repressor function. Both the cysteine sulfenic acid and the sulfenamide cross-link can react with free cysteine or bacillithiol (BSH) to form mixed disulfides. Further reduction of OhrR by free sulfhydryl compounds restores repressor activity. {ECO:0000269|PubMed:11983871, ECO:0000269|PubMed:17502599, ECO:0000269|PubMed:19578333, ECO:0000269|PubMed:24313874, ECO:0000269|PubMed:33722570}.
|
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Organic peroxide sensor (PubMed:11418552). Represses the expression of the peroxide-inducible gene ohrA by cooperative binding to two inverted repeat elements (PubMed:11418552, PubMed:24313874). {ECO:0000269|PubMed:11418552, ECO:0000269|PubMed:24313874}.
|
Bacillus subtilis (strain 168)
|
O34798
|
PDAC_BACSU
|
MLAKRIKWFHVLIAVVCVVGLIGFFHNHSLKKETVMNKVRTDSQYGNVEIATLVNDGKTFNYAVNYPVFKNEKMDSALKRFAEKEVRQFQKETKDVDQEHTTKRNELNVDYKIVHYAKQTVAIVFNEYKYIGGAHGQTVKKTFNYDFSKQAFLSIDDIFKEDADYLHKLSLIAYHELKKNKDIAADDALLKEGTAPKKENFSRFAIKEDYIELYFDTYQVAAGYLGEQSIAIKKSLLKDILKEQYIDKAKNKNKIKEQKPKHEVISLPKEETVDPNQKVIALTFDDGPNPATTNQILDSLKKYKGHATFFVLGSRVQYYPETLIRMLKEGNEVGNHSWSHPLLTRLSVKEALKQINDTQDIIEKISGYRPTLVRPPYGGINDELRSQMKMDVALWDVDPEDWKDRNKKTIVDRVMNQAGDGRTILIHDIYRTSADAADEIIKKLTDQGYQLVTVSQLEEVKKQREAK
|
3.5.1.-
| null |
carbohydrate metabolic process [GO:0005975]
|
plasma membrane [GO:0005886]
|
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]; metal ion binding [GO:0046872]
|
PF11738;PF13739;PF01522;
|
3.30.565.40;3.20.20.370;3.90.640.20;
|
RsiV family; Polysaccharide deacetylase family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.8 mM for non-treated B.subtilis peptidoglycan {ECO:0000269|PubMed:22277649}; KM=12.3 mM for GlcNAc4 {ECO:0000269|PubMed:22277649}; Note=kcat is 0.32 sec(-1) for the deacetylation of MurNAc residues in peptidoglycan, and 0.24 sec(-1) for the deacetylation of GlcNAc4.;
| null | null | null |
FUNCTION: Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in peptidoglycan, a modification that confers resistance to lysosyme. Is not able to deacetylate N-acetylglucosamine (GlcNAc) residues in peptidoglycan, but can deacylate chitin oligomers such as GlcNAc4 and GlcNAc5. Is essentially not active toward chitosan (partially deacetylated GlcNAc polymer) and has very low activity toward chitin (GlcNAc polymer). Does not deacetylate GlcNAc. {ECO:0000269|PubMed:22277649}.
|
Bacillus subtilis (strain 168)
|
O34817
|
NAGR_BACSU
|
MNINKQSPIPIYYQIMEQLKTQIKNGELQPDMPLPSEREYAEQFGISRMTVRQALSNLVNEGLLYRLKGRGTFVSKPKMEQALQGLTSFTEDMKSRGMTPGSRLIDYQLIDSTEELAAILGCGHPSSIHKITRVRLANDIPMAIESSHIPFELAGELNESHFQSSIYDHIERYNSIPISRAKQELEPSAATTEEANILGIQKGAPVLLIKRTTYLQNGTAFEHAKSVYRGDRYTFVHYMDRLS
| null | null |
negative regulation of DNA-templated transcription [GO:0045892]
| null |
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]
|
PF00392;PF07702;
|
3.40.1410.10;1.10.10.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Main transcriptional repressor of genes involved in N-acetylglucosamine (GlcNAc) transport and utilization (PubMed:20047956, PubMed:21602348, PubMed:23667565, PubMed:24673833). Represses the expression of the nagAB and nagP operons by binding directly within their upstream regions (PubMed:21602348, PubMed:24673833). Binds to the DNA consensus sequence 5'-ATTGGTATAGACAACT-3' (PubMed:21602348). Also acts as a weak repressor of mapB expression (PubMed:16207374). {ECO:0000269|PubMed:16207374, ECO:0000269|PubMed:20047956, ECO:0000269|PubMed:21602348, ECO:0000269|PubMed:23667565, ECO:0000269|PubMed:24673833}.
|
Bacillus subtilis (strain 168)
|
O34840
|
CHAA_BACSU
|
MNRIFFILVAAGVPLSVIGSLMHWPSAVLFAVYCVTIIALASYMGRATESLSIIAGPRIGGLLNATFGNAVELIISLFALKEGLTGIVLASLTGSVLGNLLLVAGLSFFVGGLKYKRQEFNIHDARHNSGLLIFAIIVAFVIPEVFSVGMGNASKLNLSIGISIIMILLYVAALYFKLVTHRGVYQPNNAAQTEEEEEPEWSGKVATIVLFAATIVVAYISENLVHTFHSVAEQFGWSELFIGVIIVAIVGNAAEHASAIIMAFKNKMDIAVEIAVGSTLQIAMFVAPVLVICSIFFPTSMPLVFTLPELVAMVSAVLLMIAISNDGDSNWFEGATLLAAYVIMAIGFFLL
| null | null |
calcium ion transmembrane transport [GO:0070588]; intracellular calcium ion homeostasis [GO:0006874]
|
plasma membrane [GO:0005886]
|
calcium:proton antiporter activity [GO:0015369]
|
PF01699;
|
1.20.1420.30;
|
Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family, Cation/proton exchanger (CAX) subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23798403}; Multi-pass membrane protein {ECO:0000269|PubMed:23798403}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.5 uM for Ca(2+) (at pH 8.5) {ECO:0000269|PubMed:19543710}; KM=37.5 uM for Ca(2+) (at pH 8.0) {ECO:0000269|PubMed:19543710}; KM=113 uM for Ca(2+) (at pH 7.5) {ECO:0000269|PubMed:19543710};
| null | null | null |
FUNCTION: Ca(+)/H(+) antiporter that extrudes calcium in exchange for external protons. Does not transport sodium or potassium. {ECO:0000269|PubMed:19543710}.
|
Bacillus subtilis (strain 168)
|
O34860
|
RSBRB_BACSU
|
MKLNEKLYAFFSEHVEQMAEEWIETMEESDPNSLYALHNATVTEELKEQDREFYRHLNYMYVLPEKQFLEEFQEWVIELTNDQKHLDTPVQYVIREFMRNRRLYTKYFEKFAEENESAFEPGEKQKWADLIVKVFDFTIYTFVDHAEMNAKQQLNAQREMILELSSPVITLSKSTALLPLVGDIDTERAKFILENTLQACAKRRVEHLLIDLSGVVVVDTMVAHQIFKLIEALNLIGVRSTLSGIRPEIAQTAVQLGIDFSNITIKTNLAQALNYHQ
| null | null | null | null | null |
PF01740;
|
3.30.750.24;
| null |
PTM: Phosphorylated by RsbT. {ECO:0000269|PubMed:11157946, ECO:0000269|PubMed:17218307}.
| null | null | null | null | null | null |
FUNCTION: One of 4 functionally non-identical RsbR paralogs, it functions in the environmental signaling branch of the general stress response.; FUNCTION: Negative regulator of sigma-B activity. Non-phosphorylated RsbS binds to RsbT, preventing its association with RsbU. Requires any one of RsbRA, RsbRB, RsbRC or RsbRD to sequester RsbT. When RsbS and the RsbR paralog(s) are phosphorylated, they release RsbT, which can then bind and activate RsbU.
|
Bacillus subtilis (strain 168)
|
O34876
|
FTSX_BACSU
|
MIKILGRHLRESFKSLGRNTWMTFASISAVTVTLILVGVFLVIMLNLNNMATNAEKQVEIKVLIDLTADQKAQDKLQNDIKELKGIQSVTFSSKEKELDQLVDSFGDSGKSLTMKDQENPLNDAFVVKTTDPHDTPNVAKKIEKMDHVYKVTYGKEEVSRLFKVVGVSRNIGIALIIGLVFTAMFLISNTIKITIFARRKEIEIMKLVGATNWFIRWPFFLEGLLLGVFGSVIPIALVLSTYQYVIGWVVPKVQGSFVSLLPYNPFVFQVSLVLIAIGAVIGVWGSLTSIRKFLRV
| null | null |
asymmetric cell division [GO:0008356]; cell septum assembly [GO:0090529]; positive regulation of sporulation resulting in formation of a cellular spore [GO:0045881]; regulation of phosphorelay signal transduction system [GO:0070297]
|
cell division site [GO:0032153]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]
| null |
PF02687;PF18075;
|
3.30.70.3040;
|
ABC-4 integral membrane protein family, FtsX subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23651456, ECO:0000305|PubMed:18573177}; Multi-pass membrane protein {ECO:0000305|PubMed:18573177}. Membrane raft {ECO:0000269|PubMed:23651456}; Multi-pass membrane protein. Note=Unlike the E.coli ortholog, localization is not restricted to division septa, nor is it dependent on FtsZ. Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion (PubMed:23651456). {ECO:0000269|PubMed:23651456}.
| null | null | null | null | null |
FUNCTION: Part of the ABC transporter FtsEX involved in asymmetric cellular division facilitating the initiation of sporulation. May act as an importer, possibly at the top of a hierarchical cascade leading to the correct temporal initiation of sporulation. Acts upstream of the histidine kinases KinA, KinB and KinC, the RapA phosphatase and the Spo0A sporulation protein. {ECO:0000269|PubMed:18573177}.
|
Bacillus subtilis (strain 168)
|
O34919
|
YOSS_BACSU
|
MQIKIKYLDETQTRINKMEQGDWIDLRAAEDVAIKKDEFKLVPLGVAMELPEGYEAHVVPRSSTYKNFGVIQTNSMGVIDESYKGDNDFWFFPAYALRDTKIKKGDRICQFRIMKKMPAVDLIEVDRLGNGDRGGHGSTGTK
|
3.6.1.23
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15939294, ECO:0000269|PubMed:21358047}; Note=Binds 1 Mg(2+) per subunit, coordinated entirely by the nucleotide and ordered water molecules. {ECO:0000269|PubMed:21358047};
|
dUMP biosynthetic process [GO:0006226]; dUTP catabolic process [GO:0046081]
|
protein-containing complex [GO:0032991]
|
dUTP diphosphatase activity [GO:0004170]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]
|
PF00692;
|
2.70.40.10;
|
DUTPase family
| null | null |
CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000269|PubMed:15939294};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.6 uM for dUTP {ECO:0000269|PubMed:15939294};
|
PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:15939294};
| null |
FUNCTION: Involved in nucleotide metabolism: produces dUMP, the immediate precursor of thymidine nucleotides and decreases the intracellular concentration of dUTP, so that uracil cannot be incorporated into DNA (PubMed:9679200). The Ser-62 side chain changes its position upon ligand-binding to make contacts with the nucleotide phosphates (PubMed:21358047). {ECO:0000269|PubMed:21358047, ECO:0000269|PubMed:9679200}.
|
Bacillus subtilis (strain 168)
|
O34926
|
CYPX_BACSU
|
MSQSIKLFSVLSDQFQNNPYAYFSQLREEDPVHYEESIDSYFISRYHDVRYILQHPDIFTTKSLVERAEPVMRGPVLAQMHGKEHSAKRRIVVRSFIGDALDHLSPLIKQNAENLLAPYLERGKSDLVNDFGKTFAVCVTMDMLGLDKRDHEKISEWHSGVADFITSISQSPEARAHSLWCSEQLSQYLMPVIKERRVNPGSDLISILCTSEYEGMALSDKDILALILNVLLAATEPADKTLALMIYHLLNNPEQMNDVLADRSLVPRAIAETLRYKPPVQLIPRQLSQDTVVGGMEIKKDTIVFCMIGAANRDPEAFEQPDVFNIHREDLGIKSAFSGAARHLAFGSGIHNCVGAAFAKNEIEIVANIVLDKMRNIRLEEDFCYAESGLYTRGPVSLLVAFDGA
|
1.14.15.13
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:20690619};
|
pigment biosynthetic process [GO:0046148]
| null |
heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen [GO:0016713]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null | null |
CATALYTIC ACTIVITY: Reaction=cyclo(L-leucyl-L-leucyl) + 4 H(+) + 3 O2 + 6 reduced [2Fe-2S]-[ferredoxin] = 4 H2O + 6 oxidized [2Fe-2S]-[ferredoxin] + pulcherriminic acid; Xref=Rhea:RHEA:35555, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:67269, ChEBI:CHEBI:77663; EC=1.14.15.13; Evidence={ECO:0000269|PubMed:20690619};
| null | null | null | null |
FUNCTION: Involved in the biosynthesis of pulcherrimin, a red extracellular pigment. Catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms pulcherrimin via a nonenzymic reaction with Fe(3+). Substrates with small alkyl groups (cAA, cLG, cLP) exhibit weaker binding to CYP134A1, but substrates with larger hydrophobic side chains bind in a similar regime to cLL. {ECO:0000269|PubMed:20690619}.
|
Bacillus subtilis (strain 168)
|
O34928
|
PDAA_BACSU
|
MKWMCSICCAAVLLAGGAAQAEAVPNEPINWGFKRSVNHQPPDAGKQLNSLIEKYDAFYLGNTKEKTIYLTFDNGYENGYTPKVLDVLKKHRVTGTFFVTGHFVKDQPQLIKRMSDEGHIIGNHSFHHPDLTTKTADQIQDELDSVNEEVYKITGKQDNLYLRPPRGVFSEYVLKETKRLGYQTVFWSVAFVDWKINNQKGKKYAYDHMIKQAHPGAIYLLHTVSRDNAEALDDAITDLKKQGYTFKSIDDLMFEKEMRLPSL
|
3.5.1.-
| null |
carbohydrate metabolic process [GO:0005975]; cell wall organization [GO:0071555]; sporulation resulting in formation of a cellular spore [GO:0030435]
|
membrane [GO:0016020]
|
deacetylase activity [GO:0019213]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]; metal ion binding [GO:0046872]
|
PF01522;
|
3.20.20.370;
|
Polysaccharide deacetylase family
| null | null | null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:15687192};
| null |
FUNCTION: Catalyzes the deacetylation of N-acetylmuramic acid (MurNAc) residues in glycan strands of peptidoglycan, leading to the formation of muramic delta-lactam residues in spore cortex, after transpeptidation of deacetylated muramic acid residues. PdaA probably carries out both deacetylation and lactam ring formation and requires the product of CwlD activity on peptidoglycan as a substrate. Is required for germination. Cannot use chitin oligomer (hexa-N-acetylchitohexaose) as a substrate. {ECO:0000269|PubMed:12374835, ECO:0000269|PubMed:14679227, ECO:0000269|PubMed:15687192}.
|
Bacillus subtilis (strain 168)
|
O34939
|
YDIO_BACSU
|
MTNFILNENKQLSLAIEDENIENFYIDGTDLVRKIIRRSGSGVTSRVPVLSTQDLENKNLHELYDESWLRMKNRPNTELTTESINIADLFSGCGGLSLGVWEACRALGINPRFSFACDLNEAALSVYEKNFSPDFSLNESIEKHINGELGAPLTVEEQRIKDKVKKIDFILAGPPCQGHSDLNNHTRRKDPRNALLMRVSRVIELFQPSSVLVENVPGIIHDKSGSFKEFKNHLKTQGYYFDEIVLNAEKLGVSQARRRYFIFASKTPVSSLNQINEFYSTNSRPISWAISDLVENVGDDIFNTASEHSLENKRRIEYLFENNLFELPNSERPDCHRLKPHSYKSVYGRMYWDRPAPTITRGFGSTGQGRFVHSLLKRTITPHEAARIQFFPDFFNFGDLRRRQYQDVIGNAVPSKLSYLLALHQLR
|
2.1.1.37
| null |
DNA restriction-modification system [GO:0009307]; methylation [GO:0032259]
| null |
DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA binding [GO:0003677]; site-specific DNA-methyltransferase (adenine-specific) activity [GO:0009007]
|
PF00145;
|
3.90.120.10;3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.6 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:3150363}; KM=3 nM for DNA {ECO:0000269|PubMed:3150363};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:3150363};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Rapidly loses activity at 37 degrees Celsius in the absence of DNA. {ECO:0000269|PubMed:3150363};
|
FUNCTION: A methylase, recognizes the double-stranded sequence 5'-YTCGAR-3', methylates C-3 on both strands, and protects the DNA from cleavage by the BsuMI endonuclease. {ECO:0000269|PubMed:11751814, ECO:0000269|PubMed:3150363, ECO:0000269|PubMed:32324221}.
|
Bacillus subtilis (strain 168)
|
O34962
|
MAO4_BACSU
|
MSLREEALHLHKVNQGKLESKSKVEVRNAKDLSLAYSPGVAEPCKDIHEDINKVYDYTMKGNMVAVVTDGTAVLGLGNIGPEAALPVMEGKAVLFKSFAGVDAFPIALNTNDVDKIVETVKLLEPTFGGVNLEDIAAPNCFIIEERLKKETNIPVFHDDQHGTAIVTVAGLVNALKLSGKSMSSIKVVANGAGAAGIAIIKLLHHYGVRDIVMCDSKGAIYEGRPNGMNDVKNEVAKFTNQDRKDGSLKDVIVDADVFIGVSVAGALTKEMVQSMAKDPIIFAMANPNPEIMPEDAREAGASVVGTGRSDFPNQVNNVLAFPGIFRGALDVRATHINEEMKIAAVEAIASLVSEDELSADYVIPAPFDKRVAPAVAKAVAKAAMETGVARITVDPEEVAEKTRKLTIIGE
|
1.1.1.40; 4.1.1.101
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P76558}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P76558}; Note=Divalent metal cations. {ECO:0000250|UniProtKB:P76558};
| null | null |
malate dehydrogenase (decarboxylating) (NAD+) activity [GO:0004471]; malate dehydrogenase (decarboxylating) (NADP+) activity [GO:0004473]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; oxaloacetate decarboxylase activity [GO:0008948]
|
PF00390;PF03949;
|
3.40.50.10380;3.40.50.720;
|
Malic enzymes family
| null | null |
CATALYTIC ACTIVITY: Reaction=(S)-malate + NADP(+) = CO2 + NADPH + pyruvate; Xref=Rhea:RHEA:18253, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.40; Evidence={ECO:0000269|PubMed:16788182, ECO:0000269|PubMed:33824210}; CATALYTIC ACTIVITY: Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526; EC=1.1.1.40; Evidence={ECO:0000269|PubMed:16788182}; CATALYTIC ACTIVITY: Reaction=(S)-malate + H(+) = (S)-lactate + CO2; Xref=Rhea:RHEA:46276, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526, ChEBI:CHEBI:16651; EC=4.1.1.101; Evidence={ECO:0000269|PubMed:33824210};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.55 mM for malate {ECO:0000269|PubMed:16788182}; KM=5.3 mM for pyruvate {ECO:0000269|PubMed:33824210}; KM=2.8 mM for NAD {ECO:0000269|PubMed:16788182}; KM=0.055 mM for NADP {ECO:0000269|PubMed:16788182}; KM=0.8 mM for NADPH {ECO:0000269|PubMed:33824210};
| null | null | null |
FUNCTION: Bifunctional enzyme with both malic and malolactic enzyme activities (PubMed:33824210). In the absence of NADPH, catalyzes the reversible decarboxylation of malate to pyruvate (PubMed:16788182, PubMed:33824210). Can use NAD and NADP, but with a very strong preference for NADP (PubMed:16788182). In the presence of excess NADPH, catalyzes the non-oxidative decarboxylation of malate to lactate (PubMed:33824210). During growth on glucose, contributes to NADPH balancing via oxidation of the NADPH produced in excess by other enzymatic reactions (PubMed:33824210). Can also catalyze the decarboxylation of oxaloacetate (PubMed:16788182). {ECO:0000269|PubMed:16788182, ECO:0000269|PubMed:33824210}.
|
Bacillus subtilis (strain 168)
|
O35000
|
NAGB_BACSU
|
MKVMECQTYEELSQIAARITADTIKEKPDAVLGLATGGTPEGTYRQLIRLHQTENLSFQNITTVNLDEYAGLSSDDPNSYHFYMNDRFFQHIDSKPSRHFIPNGNADDLEAECRRYEQLVDSLGDTDIQLLGIGRNGHIGFNEPGTSFKSRTHVVTLNEQTRQANARYFPSIDSVPKKALTMGIQTILSSKRILLLISGKSKAEAVRKLLEGNISEDFPASALHLHSDVTVLIDREAASLRP
|
3.5.99.6
| null |
carbohydrate metabolic process [GO:0005975]; glucosamine catabolic process [GO:0006043]; N-acetylglucosamine catabolic process [GO:0006046]; N-acetylneuraminate catabolic process [GO:0019262]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
glucosamine-6-phosphate deaminase activity [GO:0004342]; identical protein binding [GO:0042802]
|
PF01182;
|
3.40.50.1360;
|
Glucosamine/galactosamine-6-phosphate isomerase family, NagB subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01241, ECO:0000269|PubMed:15755726};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 mM for glucosamine 6-phosphate {ECO:0000269|PubMed:15755726}; Note=kcat is 28 sec(-1). {ECO:0000269|PubMed:15755726};
|
PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5. {ECO:0000255|HAMAP-Rule:MF_01241}.
| null | null |
FUNCTION: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. {ECO:0000255|HAMAP-Rule:MF_01241, ECO:0000269|PubMed:15755726}.
|
Bacillus subtilis (strain 168)
|
O35002
|
CTPB_BACSU
|
MNQKIMAVIAAGSMLFGGAGVYAGINLLEMDKPQTAAVPATAQADSERDKAMDKIEKAYELISNEYVEKVDREKLLEGAIQGMLSTLNDPYSVYMDKQTAKQFSDSLDSSFEGIGAEVGMEDGKIIIVSPFKKSPAEKAGLKPNDEIISINGESMAGKDLNHAVLKIRGKKGSSVSMKIQRPGTKKQLSFRIKRAEIPLETVFASEKKVQGHSVGYIAISTFSEHTAEDFAKALRELEKKEIEGLVIDVRGNPGGYLQSVEEILKHFVTKDQPYIQIAERNGDKKRYFSTLTHKKAYPVNVITDKGSASASEILAGALKEAGHYDVVGDTSFGKGTVQQAVPMGDGSNIKLTLYKWLTPNGNWIHKKGIEPTIAIKQPDYFSAGPLQLKEPLKVDMNNEDVKHAQVLLKGLSFDPGREDGYFSKDMKKAVMAFQDQNKLNKTGVIDTRTAETLNQQIEKKKSDEKNDLQLQTALKSLFVN
|
3.4.21.102
| null |
peptide metabolic process [GO:0006518]; proteolysis [GO:0006508]; signal transduction [GO:0007165]; sporulation resulting in formation of a cellular spore [GO:0030435]
|
outer membrane-bounded periplasmic space [GO:0030288]
|
endopeptidase activity [GO:0004175]; identical protein binding [GO:0042802]; peptidase activity [GO:0008233]; peptide binding [GO:0042277]; protein homodimerization activity [GO:0042803]; serine-type endopeptidase activity [GO:0004252]
|
PF13180;PF03572;PF01471;
|
2.30.42.10;3.30.750.44;1.10.101.10;
|
Peptidase S41A family
|
PTM: Is cleaved by SpoIVB in vitro and in vivo but this cleavage does not appear to be necessary for CtpB activation. CtpB can also cleave itself in vivo. {ECO:0000269|PubMed:17557826, ECO:0000269|PubMed:24243021}.
|
SUBCELLULAR LOCATION: Forespore intermembrane space {ECO:0000269|PubMed:17557826}. Note=Is expressed in both the mother cell and forespore compartments but that synthesis in the forespore is both necessary and sufficient for the proper timing of pro-sigma-K processing.
|
CATALYTIC ACTIVITY: Reaction=The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala.; EC=3.4.21.102; Evidence={ECO:0000269|PubMed:24243021};
| null | null | null | null |
FUNCTION: Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro-sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation. {ECO:0000269|PubMed:14526016, ECO:0000269|PubMed:16818230, ECO:0000269|PubMed:17557826, ECO:0000269|PubMed:24243021}.
|
Bacillus subtilis (strain 168)
|
O35013
|
YTKD_BACSU
|
MYEFKDYYQNTVQLSFDDQPFSDSPKHVWVICRFGGKWLLTEHEDRGYEFPGGKVEPMECAEEAALREVKEETGARVKSLKYLGQYKVLGKEKVIVKNIYFADIEKLEKQADYFETKGPVLFHELPENLSRNKKFSFIMKDSVLPISLKKLKESGWIE
|
3.6.1.55
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
| null |
cytoplasm [GO:0005737]
|
8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity [GO:0035539]; hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides [GO:0016818]; metal ion binding [GO:0046872]
|
PF00293;
|
3.90.79.10;
|
Nudix hydrolase family
| null | null |
CATALYTIC ACTIVITY: Reaction=8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+); Xref=Rhea:RHEA:31575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:63224, ChEBI:CHEBI:77896; EC=3.6.1.55;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.16 mM for dGTP {ECO:0000269|PubMed:15576788}; KM=0.43 mM for 8-oxo-dGTP {ECO:0000269|PubMed:15576788}; KM=0.89 mM for dATP {ECO:0000269|PubMed:15576788}; Vmax=2.4 umol/min/mg enzyme with dGTP as substrate {ECO:0000269|PubMed:15576788}; Vmax=3.1 umol/min/mg enzyme with 8-oxo-dGTP as substrate {ECO:0000269|PubMed:15576788}; Vmax=4.7 umol/min/mg enzyme with dATP as substrate {ECO:0000269|PubMed:15576788};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9. {ECO:0000269|PubMed:15576788};
| null |
FUNCTION: Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). Functions, in conjunction with MutT, to protect vegetatively growing cells from DNA-damaging agents such as H(2)O(2) or t-BHP (t-butylhydroperoxide). The 2 proteins do not however protect spores. According to PubMed:15576788, phosphohydrolase that catalyzes the hydrolysis of all common nucleoside triphosphates as well as of the mutagenic analog 8-oxo-dGTP. The high catalytic efficiency on dGTP is in contrast to results from PubMed:14761999. According to PubMed:14761999, catalyzes the hydrolysis of 8-oxo-dGTP with a specific activity 413 times higher than that exhibited against dGTP. Preferentially catalyzes the hydrolysis of 8-oxo-dGTP and 8-oxo-GTP. According to PubMed:15576788, hydrolyzes nucleoside triphosphates in a stepwise fashion through the diphosphate to the monophosphate, releasing two molecules of inorganic orthophosphate. {ECO:0000250, ECO:0000269|PubMed:14761999, ECO:0000269|PubMed:15576788}.
|
Bacillus subtilis (strain 168)
|
O35047
|
HOP2_MOUSE
|
MSKSRAEAAAGAPGIILRYLQEQNRPYSAQDVFGNLQKEHGLGKAAVVKALDQLAQEGKIKEKTYGKQKIYFADQNQFDTVSDADLHGLDASIVALTAKVQSLQQSCRHMEAELKELTSALTTPEMQKEIQELKKECAQYTERLKNIKAATNHVTPEEKEKVYRDRQKYCKEWRKRKRMTTELCDAILEGYPKSKKQFFEEVGIETDEDHNVLLPDP
| null | null |
homologous chromosome pairing at meiosis [GO:0007129]; meiotic joint molecule formation [GO:0000709]; meiotic strand invasion involved in reciprocal meiotic recombination [GO:0010774]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
condensed nuclear chromosome [GO:0000794]; DNA recombinase auxiliary factor complex [GO:0120231]; nucleoplasm [GO:0005654]
|
DNA binding domain binding [GO:0050692]; double-stranded DNA binding [GO:0003690]; nuclear androgen receptor binding [GO:0050681]; nuclear estrogen receptor binding [GO:0030331]; nuclear glucocorticoid receptor binding [GO:0035259]; nuclear receptor coactivator activity [GO:0030374]; nuclear thyroid hormone receptor binding [GO:0046966]; protein-containing complex binding [GO:0044877]; recombinase activator activity [GO:0120230]
|
PF18517;PF07106;
|
1.10.10.10;
|
HOP2 family
|
PTM: Phosphorylated by PKA, PKC and MAPK. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11739747}.
| null | null | null | null | null |
FUNCTION: Plays an important role in meiotic recombination. Stimulates DMC1-mediated strand exchange required for pairing homologous chromosomes during meiosis. The complex PSMC3IP/MND1 binds DNA, stimulates the recombinase activity of DMC1 as well as DMC1 D-loop formation from double-strand DNA. This complex stabilizes presynaptic RAD51 and DMC1 filaments formed on single strand DNA to capture double-strand DNA. This complex stimulates both synaptic and presynaptic critical steps in RAD51 and DMC1-promoted homologous pairing. May inhibit HIV-1 viral protein TAT activity and modulate the activity of proteasomes through association with PSMC3. {ECO:0000269|PubMed:15192114, ECO:0000269|PubMed:16675459, ECO:0000269|PubMed:17426123, ECO:0000269|PubMed:17639080, ECO:0000269|PubMed:17639081, ECO:0000269|PubMed:9345291}.
|
Mus musculus (Mouse)
|
O35048
|
3BHS7_RAT
|
MADSAQVPALVYLVTGGCGFLGEHIVRMLLEWEPRLRELRVFDLHLSSWLEELKTGPVQVTAIQGDVTQAHEVAAAMAGSHVVIHTAGLVDVFGKASPETIHKVNVQGTQNVIDACVQTGTRLLVYTSSMEVVGPNVKGHPFYRGNEDTPYEAIHRHPYPCSKALAEQLVLEANGRKGLRFGGRLFRAIPASVEHGRVYVGNVAWMHILVARELEQRAALMGGQVYFCYDKSPYKSYEDFNMEFLSPCGLRLIGTHPLLPYWLLVLLTALNALLQWLLRPLVLYTPLLNPYTLAVANTTFTVSTNKAQRHFGYKPLFSWEESRARTIHWVQAMEGSAW
|
1.1.1.-; 1.1.1.181
| null |
B cell chemotaxis [GO:0035754]; bile acid metabolic process [GO:0008206]; cholesterol catabolic process [GO:0006707]; liver regeneration [GO:0097421]; regulation of cell growth [GO:0001558]; steroid biosynthetic process [GO:0006694]
|
endoplasmic reticulum membrane [GO:0005789]
|
3-beta-hydroxy-delta5-steroid dehydrogenase activity [GO:0003854]; cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase activity [GO:0047016]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]
|
PF01073;
|
3.40.50.720;
|
3-beta-HSD family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=7alpha-hydroxycholesterol + NAD(+) = 7alpha-hydroxycholest-4-en-3-one + H(+) + NADH; Xref=Rhea:RHEA:11896, ChEBI:CHEBI:15378, ChEBI:CHEBI:17500, ChEBI:CHEBI:17899, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.181; Evidence={ECO:0000250|UniProtKB:Q9H2F3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11897; Evidence={ECO:0000250|UniProtKB:Q9H2F3}; CATALYTIC ACTIVITY: Reaction=7alpha,25-dihydroxycholesterol + NAD(+) = 7alpha,25-dihydroxy-4-cholesten-3-one + H(+) + NADH; Xref=Rhea:RHEA:47156, ChEBI:CHEBI:15378, ChEBI:CHEBI:37623, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:81013; Evidence={ECO:0000250|UniProtKB:Q9H2F3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47157; Evidence={ECO:0000250|UniProtKB:Q9H2F3}; CATALYTIC ACTIVITY: Reaction=(25R)-cholest-5-en-3beta,7alpha,26-triol + NAD(+) = (25R)-7alpha,26-dihydroxycholest-4-en-3-one + H(+) + NADH; Xref=Rhea:RHEA:47180, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76592, ChEBI:CHEBI:87476; Evidence={ECO:0000250|UniProtKB:Q9H2F3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47181; Evidence={ECO:0000250|UniProtKB:Q9H2F3}; CATALYTIC ACTIVITY: Reaction=(24S)-7alpha-dihydroxycholesterol + NAD(+) = (24S)-7alpha,24-dihydroxycholest-4-en-3-one + H(+) + NADH; Xref=Rhea:RHEA:47200, ChEBI:CHEBI:15378, ChEBI:CHEBI:37640, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:63838; Evidence={ECO:0000250|UniProtKB:Q9H2F3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47201; Evidence={ECO:0000250|UniProtKB:Q9H2F3};
| null |
PATHWAY: Lipid metabolism; steroid biosynthesis. {ECO:0000250|UniProtKB:Q9H2F3}.
| null | null |
FUNCTION: The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. HSD VII is active against four 7-alpha-hydroxylated sterols. Does not metabolize several different C(19/21) steroids as substrates. Involved in bile acid synthesis. Plays a key role in cell positioning and movement in lymphoid tissues by mediating degradation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC): 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells. {ECO:0000250|UniProtKB:Q9EQC1}.
|
Rattus norvegicus (Rat)
|
O35049
|
NSMA2_RAT
|
MVLYTTPFPNSCLSALHAVSWALIFPCYWLVDRLVASFIPTTYEKRQRADDPCYLQLFCTVLFTPVYLALLVAALPFAFLGFIFWSPLQSARRPYSYSRLEDKSPAGGAALLSEWKGTGAGKSFCFATANVCLLPDSLARLNNVFNTQARAKEIGQRIRNGAARPQIKIYIDSPTNTSISAASFSSLVSPQGSDGARAVPGSIKRTASVEYKGDGGRHPSDEAANGPASGEQADGSLEDSCIVRIGGEEGGRAQEADDPAPGSQARNGAGGTPKGQTPNHNQRDGDSGSLGSPSASRESLVKARAGQDSGGSGEPGSNSKLLYKTSVVKKAAARRRRHPDEAFDHEVSAFFPANLDFLCLQEVFDKRAAAKLKEQLHGYFEYILYDVGVYGCHGCCNFKCLNSGLFFASRYPVMDVAYHCYPNGCSFDALASKGALFLKVQVGSTPQDQRIVGYIACTHLHAPPEDSAIRCEQLDLLQDWLADFRKSTSSTSTANPEELVVFDVICGDLNFDNCSSDDKLEQQHSLFTRYKDPCRLGPGEEKPWAIGTLLDINGLYDEDVCTPDNLQKVLESEEGRREYLAFPTSKSPGAGQKGRKDLLKGNGRRIDYMLHAEEGLCPDWKAEVEEFSFITQLSGLTDHLPVAMRLMVSAGEEEA
|
3.1.4.12
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15059969};
|
artery smooth muscle contraction [GO:0014824]; BMP signaling pathway [GO:0030509]; bone development [GO:0060348]; bone growth [GO:0098868]; bone mineralization [GO:0030282]; cartilage development [GO:0051216]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to interleukin-1 [GO:0071347]; cellular response to magnesium ion [GO:0071286]; cellular response to oxidised low-density lipoprotein particle stimulus [GO:0140052]; cellular response to peptide [GO:1901653]; cellular response to reactive oxygen species [GO:0034614]; cellular response to redox state [GO:0071461]; cellular response to tumor necrosis factor [GO:0071356]; ceramide metabolic process [GO:0006672]; chondrocyte development [GO:0002063]; chondrocyte development involved in endochondral bone morphogenesis [GO:0003433]; collagen metabolic process [GO:0032963]; dentinogenesis [GO:0097187]; DNA biosynthetic process [GO:0071897]; dopamine uptake [GO:0090494]; endochondral ossification [GO:0001958]; extracellular matrix assembly [GO:0085029]; G1 to G0 transition [GO:0070314]; hematopoietic progenitor cell differentiation [GO:0002244]; lung alveolus development [GO:0048286]; lung development [GO:0030324]; mitotic nuclear division [GO:0140014]; multicellular organism growth [GO:0035264]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; negative regulation of hyaluronan biosynthetic process [GO:1900126]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; ossification [GO:0001503]; peptide hormone secretion [GO:0030072]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; polysaccharide transport [GO:0015774]; positive regulation of ceramide biosynthetic process [GO:2000304]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of smooth muscle cell proliferation [GO:0048661]; regulation of cartilage development [GO:0061035]; regulation of hyaluronan biosynthetic process [GO:1900125]; regulation of leukocyte migration [GO:0002685]; regulation of protein phosphorylation [GO:0001932]; respiratory system development [GO:0060541]; signal transduction [GO:0007165]; skeletal system development [GO:0001501]; sphingolipid mediated signaling pathway [GO:0090520]; sphingolipid metabolic process [GO:0006665]; sphingomyelin catabolic process [GO:0006685]; sphingomyelin metabolic process [GO:0006684]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi cis cisterna [GO:0000137]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; neutral sphingomyelin phosphodiesterase activity [GO:0061751]; phosphatidic acid binding [GO:0070300]; phosphatidylserine binding [GO:0001786]; phosphoric diester hydrolase activity [GO:0008081]; sphingomyelin phosphodiesterase activity [GO:0004767]
|
PF03372;
|
3.60.10.10;
|
Neutral sphingomyelinase family
|
PTM: Palmitoylated, palmitoylation-deficient proteins are targeted for lysosomal degradation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:10823942}; Lipid-anchor {ECO:0000269|PubMed:10823942}. Cell membrane {ECO:0000269|PubMed:15059969}; Lipid-anchor {ECO:0000269|PubMed:15059969}. Note=May localize to detergent-resistant subdomains of Golgi membranes of hypothalamic neurosecretory neurons (PubMed:10823942).
|
CATALYTIC ACTIVITY: Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639, ChEBI:CHEBI:295975; EC=3.1.4.12; Evidence={ECO:0000269|PubMed:15059969}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19254; Evidence={ECO:0000250|UniProtKB:Q9NY59}; CATALYTIC ACTIVITY: Reaction=H2O + N-(15Z-tetracosenoyl)sphing-4-enine-1-phosphocholine = H(+) + N-(15Z-tetracosenoyl)-sphing-4-enine + phosphocholine; Xref=Rhea:RHEA:45320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74450, ChEBI:CHEBI:74535, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q9NY59}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45321; Evidence={ECO:0000250|UniProtKB:Q9NY59}; CATALYTIC ACTIVITY: Reaction=H2O + N-(tetracosanoyl)-sphing-4-enine-1-phosphocholine = H(+) + N-tetracosanoyl-sphing-4-enine + phosphocholine; Xref=Rhea:RHEA:45324, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72965, ChEBI:CHEBI:83360, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q9NY59}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45325; Evidence={ECO:0000250|UniProtKB:Q9NY59}; CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine + H2O = an N-acyl-sphingoid base + H(+) + phosphocholine; Xref=Rhea:RHEA:45300, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64583, ChEBI:CHEBI:83273, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q9NY59}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45301; Evidence={ECO:0000250|UniProtKB:Q9NY59}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:75542, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q9NY59}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41120; Evidence={ECO:0000250|UniProtKB:Q9NY59}; CATALYTIC ACTIVITY: Reaction=1-O-octadecyl-sn-glycero-3-phosphocholine + H2O = 1-O-octadecyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:39923, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74001, ChEBI:CHEBI:75216, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q9NY59}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39924; Evidence={ECO:0000250|UniProtKB:Q9NY59}; CATALYTIC ACTIVITY: Reaction=a sphingosylphosphocholine + H2O = a sphingoid base + H(+) + phosphocholine; Xref=Rhea:RHEA:45296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84410, ChEBI:CHEBI:85171, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q9NY59}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45297; Evidence={ECO:0000250|UniProtKB:Q9NY59}; CATALYTIC ACTIVITY: Reaction=H2O + N-(hexadecanoyl)-sphing-4-enine-1-phosphocholine = H(+) + N-hexadecanoylsphing-4-enine + phosphocholine; Xref=Rhea:RHEA:45644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72959, ChEBI:CHEBI:78646, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:Q9JJY3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45645; Evidence={ECO:0000250|UniProtKB:Q9JJY3};
| null |
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:15059969}.
| null | null |
FUNCTION: Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Binds to anionic phospholipids (APLs) such as phosphatidylserine (PS) and phosphatidic acid (PA) that modulate enzymatic activity and subcellular location (By similarity). Regulates the cell cycle by acting as a growth suppressor in confluent cells. Acts as a regulator of postnatal development and participates in bone and dentin mineralization. May be involved in IL-1-beta-induced JNK activation in hepatocytes. May act as a mediator in transcriptional regulation of NOS2/iNOS via the NF-kappa-B activation under inflammatory conditions. {ECO:0000250|UniProtKB:Q9JJY3, ECO:0000269|PubMed:14720208, ECO:0000269|PubMed:15059969}.
|
Rattus norvegicus (Rat)
|
O35052
|
CDS1_RAT
|
MLELRHRGGCPGPGGAGTPPPREGEAAGGDHETESTSDKETDIDDRYGDLDARGDSDVPEVPPSSDRTPEILKKALSGLSSRWKNWWIRGILTLTMISLFFLIIYMGSFMLMLLVLGIQVKCFQEIITIGYRVYHSYDLPWFRTLSWYFLLCVNYFFYGETVADYFATFVQREEQLQFLIRYHRFISFALYLAGFCMFVLSLVKKHYRLQFYMFAWTHVTLLITVTQSHLVIQNLFEGMIWFLVPISSVICNDITAYLFGFFFGRTPLIKLSPKKTWEGFIGGFFSTVIFGFIAAYVLSKYQYFVCPVEYRSDVNSFVTECEPSELFQLQNYSLPPFLQAVLSRETVSLYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVHVYITSFIRGPNPSKVLQQLLVLQPEQQLNIYRTLKIHLTEKGILQPTWKV
|
2.7.7.41
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9345289};
|
CDP-diacylglycerol biosynthetic process [GO:0016024]; lipid droplet formation [GO:0140042]; phosphatidylinositol biosynthetic process [GO:0006661]; positive regulation of fat cell differentiation [GO:0045600]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
|
phosphatidate cytidylyltransferase activity [GO:0004605]
|
PF01148;
| null |
CDS family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29253589, ECO:0000269|PubMed:6271231, ECO:0000269|PubMed:9083091}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41; Evidence={ECO:0000269|PubMed:29253589, ECO:0000269|PubMed:30862571, ECO:0000269|PubMed:9083091, ECO:0000269|PubMed:9345289}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16230; Evidence={ECO:0000305|PubMed:9083091}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + CTP + H(+) = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45648, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77091, ChEBI:CHEBI:85349; Evidence={ECO:0000250|UniProtKB:Q92903}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45649; Evidence={ECO:0000250|UniProtKB:Q92903}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + CTP + H(+) = 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45660, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77098, ChEBI:CHEBI:85352; Evidence={ECO:0000250|UniProtKB:Q92903}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45661; Evidence={ECO:0000250|UniProtKB:Q92903}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + CTP + H(+) = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45652, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:72864, ChEBI:CHEBI:85350; Evidence={ECO:0000250|UniProtKB:Q92903}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45653; Evidence={ECO:0000250|UniProtKB:Q92903}; CATALYTIC ACTIVITY: Reaction=1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CTP + H(+) = 1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45656, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77126, ChEBI:CHEBI:85351; Evidence={ECO:0000250|UniProtKB:Q92903}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45657; Evidence={ECO:0000250|UniProtKB:Q92903}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CTP + H(+) = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45664, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74560, ChEBI:CHEBI:85353; Evidence={ECO:0000250|UniProtKB:Q92903}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45665; Evidence={ECO:0000250|UniProtKB:Q92903}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphate + CTP + H(+) = 1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45668, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77130, ChEBI:CHEBI:85354; Evidence={ECO:0000250|UniProtKB:Q92903}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45669; Evidence={ECO:0000250|UniProtKB:Q92903}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + CTP + H(+) = 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45672, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77128, ChEBI:CHEBI:85355; Evidence={ECO:0000250|UniProtKB:Q92903}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45673; Evidence={ECO:0000250|UniProtKB:Q92903}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CTP + H(+) = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45676, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74546, ChEBI:CHEBI:85356; Evidence={ECO:0000250|UniProtKB:Q92903}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45677; Evidence={ECO:0000250|UniProtKB:Q92903};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=102 uM for 1-stearoyl-2-arachidonoyl-sn-glycero-3-phosphate {ECO:0000269|PubMed:9083091}; KM=114 uM for 1,2-dioleoyl-sn-glycero-3-phosphate {ECO:0000269|PubMed:9083091}; KM=138 uM for phosphatidic acid {ECO:0000269|PubMed:9083091}; Vmax=268 pmol/min/mg enzyme for 1-stearoyl-2-arachidonoyl-sn-glycero-3-phosphate {ECO:0000269|PubMed:9083091}; Vmax=259 pmol/min/mg enzyme for 1,2-dioleoyl-sn-glycero-3-phosphate {ECO:0000269|PubMed:9083091}; Vmax=198 pmol/min/mg enzyme for phosphatidic acid {ECO:0000269|PubMed:9083091};
|
PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
| null | null |
FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol (PubMed:29253589, PubMed:30862571, PubMed:9083091, PubMed:9345289). Exhibits almost no acyl chain preference for PA, showing no discrimination for the sn-1/sn-2 acyl chain composition of PAs (By similarity). Plays an important role in regulatinng the growth of lipid droplets which are storage organelles at the center of lipid and energy homeostasis (By similarity). Positively regulates the differentiation and development of adipocytes (By similarity). {ECO:0000250|UniProtKB:P98191, ECO:0000250|UniProtKB:Q92903, ECO:0000269|PubMed:29253589, ECO:0000269|PubMed:30862571, ECO:0000269|PubMed:9083091, ECO:0000269|PubMed:9345289}.
|
Rattus norvegicus (Rat)
|
O35054
|
CLD4_MOUSE
|
MASMGLQVLGISLAVLGWLGIILSCALPMWRVTAFIGSNIVTAQTSWEGLWMNCVVQSTGQMQCKMYDSMLALPQDLQAARALMVISIIVGALGMLLSVVGGKCTNCMEDETVKAKIMITAGAVFIVASMLIMVPVSWTAHNVIRDFYNPMVASGQKREMGASLYVGWAASGLLLLGGGLLCCSCPPRSNDKPYSAKYSAARSVPASNYV
| null | null |
bicellular tight junction assembly [GO:0070830]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]; circadian rhythm [GO:0007623]; female pregnancy [GO:0007565]; renal absorption [GO:0070293]; response to progesterone [GO:0032570]
|
apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; basal plasma membrane [GO:0009925]; bicellular tight junction [GO:0005923]; chloride channel complex [GO:0034707]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; plasma membrane [GO:0005886]; tight junction [GO:0070160]
|
chloride channel activity [GO:0005254]; identical protein binding [GO:0042802]; structural molecule activity [GO:0005198]
|
PF00822;
|
1.20.140.150;
|
Claudin family
|
PTM: Phosphorylated. Phosphorylation by EPHA2 is stimulated by EFNA1 and alters interaction with TJP1 (By similarity). {ECO:0000250|UniProtKB:O14493}.
|
SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:20921420, ECO:0000269|PubMed:25831548, ECO:0000269|PubMed:9892664}. Cell membrane {ECO:0000269|PubMed:20921420, ECO:0000269|PubMed:9892664}; Multi-pass membrane protein {ECO:0000255}. Note=CLDN4 is required for tight junction localization in the kidney (PubMed:20921420, PubMed:25831548). {ECO:0000269|PubMed:20921420, ECO:0000269|PubMed:25831548}.
| null | null | null | null | null |
FUNCTION: Channel-forming tight junction protein that mediates paracellular chloride transport in the kidney (PubMed:20921420). Plays a critical role in the paracellular reabsorption of filtered chloride in the kidney collecting ducts (PubMed:20921420). Claudins play a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000269|PubMed:20921420}.
|
Mus musculus (Mouse)
|
O35074
|
PTGIS_MOUSE
|
MSWAALLGLLAVLLLLLLLLSRRRARRPGEPPLDLGSIPWLGHALEFGRDAASFLTRMKEKHGDIFTVLVGGRYVTVLLDPHSYDTVVWELRTRLDFHPYAIFLMERIFDLQLPNFNPSEEKARMKPTLMHRDLQALTEAMYTNLRTVLLGDSTEAGSGWQETGLLEFSYNALLSAGYLTLYGVEASPRTHESQAQDRVHSADVFHTFRQLDLLLPKLARGSLSAGDKDHACSVKNRLWKLLSPARLASRADRSSWLESYLRHLEEMGVSEEMQARALVLQLWATQGNMGPTAFWLLLFLLKNPEALAAVRAELKHTVWQAEQPVSQMTTLPQKILDSMPVLDSVLNETLRLTAAPFITREVMADLALPMADGREFSLRRGDRLLLFPFLSPQKDPEIYTEPEVFKYNRFLNPDGSEKKDFYKDGKRLKNYNMPWGAGHNQCLGKSYAINSIKQFVVLLLTHFDLELGSEDTEVPEFDLSRYGFGLMQPEEDVPIRYRARL
|
4.2.1.152; 5.3.99.4
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q16647};
|
cellular response to hypoxia [GO:0071456]; cellular response to interleukin-1 [GO:0071347]; cellular response to interleukin-6 [GO:0071354]; decidualization [GO:0046697]; embryo implantation [GO:0007566]; icosanoid metabolic process [GO:0006690]; negative regulation of inflammatory response [GO:0050728]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of nitric oxide biosynthetic process [GO:0045019]; positive regulation of angiogenesis [GO:0045766]; positive regulation of execution phase of apoptosis [GO:1900119]; positive regulation of peroxisome proliferator activated receptor signaling pathway [GO:0035360]; prostaglandin biosynthetic process [GO:0001516]; response to hypoxia [GO:0001666]
|
caveola [GO:0005901]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
heme binding [GO:0020037]; hydroperoxy icosatetraenoate dehydratase activity [GO:0106256]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; prostaglandin-I synthase activity [GO:0008116]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q29626}; Single-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin I2; Xref=Rhea:RHEA:23580, ChEBI:CHEBI:57403, ChEBI:CHEBI:57405; EC=5.3.99.4; Evidence={ECO:0000250|UniProtKB:Q16647}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23581; Evidence={ECO:0000250|UniProtKB:Q16647}; CATALYTIC ACTIVITY: Reaction=a hydroperoxyeicosatetraenoate = an oxoeicosatetraenoate + H2O; Xref=Rhea:RHEA:55556, ChEBI:CHEBI:15377, ChEBI:CHEBI:59720, ChEBI:CHEBI:131859; EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:Q16647}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55557; Evidence={ECO:0000250|UniProtKB:Q16647}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636, ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446; Evidence={ECO:0000250|UniProtKB:Q16647}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + AH2 = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57409, ChEBI:CHEBI:57446; Evidence={ECO:0000250|UniProtKB:Q16647};
| null | null | null | null |
FUNCTION: Catalyzes the biosynthesis and metabolism of eicosanoids. Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2), a potent mediator of vasodilation and inhibitor of platelet aggregation. Additionally, displays dehydratase activity, toward hydroperoxyeicosatetraenoates (HPETEs), especially toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE). {ECO:0000250|UniProtKB:Q16647}.
|
Mus musculus (Mouse)
|
O35077
|
GPDA_RAT
|
MAGKKVCIVGSGNWGSAIAKIVGSNASQLAHFDPRVTMWVFEEDIGGRKLTEIINTQHENVKYLPGHKLPPNVVAVPDVVQAATGADILVFVVPHQFIGKICDQLKGHLKANTIGISLIKGIDEGPNGLKLISEVIGESLGIPMSVLMGANIASEVAEEKFCETTIGCKDPAQGQLLKELMQTPNFRITVVQEVDTVEICGALKNIVAVGAGFCDGLGFGDNTKAAVIRLGLMEMIAFAKLFCSGSVSSATFLESCGVADLITTCYGGRNRKVAEAFARTGKSIEQLEKEMLNGQKLQGPQTARELHSILQHKGLVDKFPLFTAVYKVCYEGQPVGEFICCLQNHPEHM
|
1.1.1.8
| null |
cellular response to cAMP [GO:0071320]; cellular response to tumor necrosis factor [GO:0071356]; gluconeogenesis [GO:0006094]; glycerol-3-phosphate catabolic process [GO:0046168]; glycerol-3-phosphate metabolic process [GO:0006072]; glycerolipid metabolic process [GO:0046486]; glycerophosphate shuttle [GO:0006127]; NADH metabolic process [GO:0006734]; NADH oxidation [GO:0006116]; positive regulation of glycolytic process [GO:0045821]
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cytosol [GO:0005829]; glycerol-3-phosphate dehydrogenase complex [GO:0009331]
|
glycerol-3-phosphate dehydrogenase (quinone) activity [GO:0004368]; glycerol-3-phosphate dehydrogenase [NAD(P)+] activity [GO:0047952]; NAD binding [GO:0051287]; protein homodimerization activity [GO:0042803]
|
PF07479;PF01210;
|
3.40.50.720;
|
NAD-dependent glycerol-3-phosphate dehydrogenase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P21695}.
|
CATALYTIC ACTIVITY: Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57945; EC=1.1.1.8; Evidence={ECO:0000250|UniProtKB:P21695}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11093; Evidence={ECO:0000250|UniProtKB:P21695};
| null | null | null | null |
FUNCTION: Has glycerol-3-phosphate dehydrogenase activity. {ECO:0000250|UniProtKB:P21695}.
|
Rattus norvegicus (Rat)
|
O35078
|
OXDA_RAT
|
MRVAVIGAGVIGLSTALCIHERYHPAQPLHMKIYADRFTPFTTSDVAAGLWQPYLSDPSNPQEAEWNQQTFDHLQSCLHSPNAEKMGLALISGYNLFRDEVPDPFWKSTVLGFRKLTPSELDMFPDYSYGWFNTSLLLEGKSYLSWLTERLTERGVKFIHRKVASFEEVVRGGVDVIINCTGVWAGALQADASLQPGRGQIIQVEAPWIKHFILTHDPSLGIYNSPYIIPGSKTVTLGGVFQLGNWSELNSVHDHNTIWKSCCQLEPTLKNARIMGELTGFRPVRPQVRLERERLRFGSSSAEVIHNYGHGGYGLTIHWGCAMEAANLFGKILEEKNLSRMPPSHL
|
1.4.3.3
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:21981077};
|
D-alanine catabolic process [GO:0055130]; D-amino acid catabolic process [GO:0019478]; D-serine catabolic process [GO:0036088]; D-serine metabolic process [GO:0070178]; digestion [GO:0007586]; dopamine biosynthetic process [GO:0042416]; leucine metabolic process [GO:0006551]; neutrophil-mediated killing of gram-negative bacterium [GO:0070945]; proline catabolic process [GO:0006562]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]; presynaptic active zone [GO:0048786]
|
D-amino-acid dehydrogenase activity [GO:0008718]; D-amino-acid oxidase activity [GO:0003884]; FAD binding [GO:0071949]; identical protein binding [GO:0042802]
|
PF01266;
|
3.30.9.10;3.40.50.720;
|
DAMOX/DASOX family
|
PTM: Phosphorylated in the cerebellum; probably not by PRKACA, PRKCA or PRKCE. {ECO:0000250|UniProtKB:P14920}.; PTM: May be S-nitrosylated, which partially inactivates the enzyme. {ECO:0000250|UniProtKB:P14920}.
|
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:26961980, ECO:0000269|PubMed:2896644}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P14920}. Presynaptic active zone {ECO:0000269|PubMed:21700703}. Secreted {ECO:0000250|UniProtKB:P18894}. Note=Transiently present in the cytosol before being delivered to the peroxisomes (By similarity). In the cerebellum, a fraction of protein localizes to the presynaptic active zone, where its activity is regulated by protein BSN (PubMed:21700703). Secreted into the lumen of the small intestine (By similarity). {ECO:0000250|UniProtKB:P14920, ECO:0000250|UniProtKB:P18894, ECO:0000269|PubMed:21700703}.
|
CATALYTIC ACTIVITY: Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000269|PubMed:21981077, ECO:0000305|PubMed:21700703}; CATALYTIC ACTIVITY: Reaction=D-alanine + H2O + O2 = H2O2 + NH4(+) + pyruvate; Xref=Rhea:RHEA:22688, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57416; Evidence={ECO:0000269|PubMed:21981077, ECO:0000305|PubMed:21700703}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22689; Evidence={ECO:0000269|PubMed:21981077, ECO:0000305|PubMed:21700703}; CATALYTIC ACTIVITY: Reaction=D-cysteine + H2O + O2 = 2-oxo-3-sulfanylpropanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78791, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35236, ChEBI:CHEBI:57678; Evidence={ECO:0000250|UniProtKB:P14920}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78792; Evidence={ECO:0000250|UniProtKB:P14920}; CATALYTIC ACTIVITY: Reaction=D-dopa + H2O + O2 = 3-(3,4-dihydroxyphenyl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70971, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29055, ChEBI:CHEBI:149689; Evidence={ECO:0000250|UniProtKB:P14920}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70972; Evidence={ECO:0000250|UniProtKB:P14920}; CATALYTIC ACTIVITY: Reaction=D-leucine + H2O + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78211, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, ChEBI:CHEBI:143079; Evidence={ECO:0000250|UniProtKB:P14920}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78212; Evidence={ECO:0000250|UniProtKB:P14920}; CATALYTIC ACTIVITY: Reaction=D-lysine + H2O + O2 = 6-amino-2-oxohexanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:37583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32557, ChEBI:CHEBI:58183; EC=1.4.3.3; Evidence={ECO:0000250|UniProtKB:P00371}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37584; Evidence={ECO:0000250|UniProtKB:P00371}; CATALYTIC ACTIVITY: Reaction=D-methionine + H2O + O2 = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, ChEBI:CHEBI:28938, ChEBI:CHEBI:57932; Evidence={ECO:0000250|UniProtKB:P00371}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78208; Evidence={ECO:0000250|UniProtKB:P00371}; CATALYTIC ACTIVITY: Reaction=D-phenylalanine + H2O + O2 = 3-phenylpyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, ChEBI:CHEBI:57981; Evidence={ECO:0000269|PubMed:21981077}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70964; Evidence={ECO:0000269|PubMed:21981077}; CATALYTIC ACTIVITY: Reaction=D-proline + O2 = 1-pyrroline-2-carboxylate + H2O2; Xref=Rhea:RHEA:78259, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:39785, ChEBI:CHEBI:57726; Evidence={ECO:0000269|PubMed:21981077}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78260; Evidence={ECO:0000269|PubMed:21981077}; CATALYTIC ACTIVITY: Reaction=D-serine + H2O + O2 = 3-hydroxypyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17180, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; Evidence={ECO:0000269|PubMed:21981077}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70952; Evidence={ECO:0000269|PubMed:21981077}; CATALYTIC ACTIVITY: Reaction=D-tryptophan + H2O + O2 = H2O2 + indole-3-pyruvate + NH4(+); Xref=Rhea:RHEA:78247, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938, ChEBI:CHEBI:57719; Evidence={ECO:0000269|PubMed:21981077}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78248; Evidence={ECO:0000269|PubMed:21981077}; CATALYTIC ACTIVITY: Reaction=D-valine + H2O + O2 = 3-methyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78203, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:74338; Evidence={ECO:0000250|UniProtKB:P14920}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78204; Evidence={ECO:0000250|UniProtKB:P14920};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=140 mM for D-alanine (at 25 degrees Celsius and at pH 8.3) {ECO:0000269|PubMed:21981077}; KM=310 mM for D-serine (at 25 degrees Celsius and at pH 8.3) {ECO:0000269|PubMed:21981077}; KM=86 mM for D-proline (at 25 degrees Celsius and at pH 8.3) {ECO:0000269|PubMed:21981077}; KM=15 mM for D-tryptophan (at 25 degrees Celsius and at pH 8.3) {ECO:0000269|PubMed:21981077}; KM=35 mM for D-phenylalanine (at 25 degrees Celsius and at pH 8.3) {ECO:0000269|PubMed:21981077}; Note=kcat is 27 sec(-1) with D-alanine as substrate (at 25 degrees Celsius and at pH 8.3) (PubMed:21981077). kcat is 6.4 sec(-1) with D-serine as substrate (at 25 degrees Celsius and at pH 8.3) (PubMed:21981077). kcat is 47 sec(-1) with D-proline as substrate (at 25 degrees Celsius and at pH 8.3) (PubMed:21981077). kcat is 3.7 sec(-1) with D-tryptophan as substrate (at 25 degrees Celsius and at pH 8.3) (PubMed:21981077). kcat is 8.5 sec(-1) with D-phenylalanine as substrate (at 25 degrees Celsius and at pH 8.3) (PubMed:21981077). {ECO:0000269|PubMed:21981077};
| null | null | null |
FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity (PubMed:21700703, PubMed:21981077). Required to catabolize D-amino acids synthesized endogenously, of gastrointestinal bacterial origin or obtained from the diet, and to use these as nutrients (By similarity). Regulates the level of D-amino acid neurotransmitters in the brain, such as D-serine, a co-agonist of N-methyl D-aspartate (NMDA) receptors, and may modulate synaptic transmission (PubMed:23631755). Catalyzes the first step of the racemization of D-DOPA to L-DOPA, for possible use in an alternative dopamine biosynthesis pathway (By similarity). Also catalyzes the first step of the chiral inversion of N(gamma)-nitro-D-arginine methyl ester (D-NNA) to its L-enantiomer L-NNA that acts as a nitric oxide synthase inhibitor (By similarity). The hydrogen peroxide produced in the reaction provides protection against microbial infection; it contributes to the oxidative killing activity of phagocytic leukocytes and protects against bacterial colonization of the small intestine (By similarity). Enzyme secreted into the lumen of the intestine may not be catalytically active and could instead be proteolytically cleaved into peptides with antimicrobial activity (By similarity). The hydrogen peroxide produced in the reaction may also play a role in promoting cellular senescence in response to DNA damage (By similarity). Could act as a detoxifying agent which removes D-amino acids accumulated during aging (PubMed:7903300). {ECO:0000250|UniProtKB:P14920, ECO:0000250|UniProtKB:P18894, ECO:0000269|PubMed:21700703, ECO:0000269|PubMed:21981077, ECO:0000269|PubMed:23631755, ECO:0000269|PubMed:7903300}.
|
Rattus norvegicus (Rat)
|
O35082
|
KLOT_MOUSE
|
MLARAPPRRPPRLVLLRLLLLHLLLLALRARCLSAEPGQGAQTWARFARAPAPEAAGLLHDTFPDGFLWAVGSAAYQTEGGWRQHGKGASIWDTFTHHSGAAPSDSPIVVAPSGAPSPPLSSTGDVASDSYNNVYRDTEGLRELGVTHYRFSISWARVLPNGTAGTPNREGLRYYRRLLERLRELGVQPVVTLYHWDLPQRLQDTYGGWANRALADHFRDYAELCFRHFGGQVKYWITIDNPYVVAWHGYATGRLAPGVRGSSRLGYLVAHNLLLAHAKVWHLYNTSFRPTQGGRVSIALSSHWINPRRMTDYNIRECQKSLDFVLGWFAKPIFIDGDYPESMKNNLSSLLPDFTESEKRLIRGTADFFALSFGPTLSFQLLDPNMKFRQLESPNLRQLLSWIDLEYNHPPIFIVENGWFVSGTTKRDDAKYMYYLKKFIMETLKAIRLDGVDVIGYTAWSLMDGFEWHRGYSIRRGLFYVDFLSQDKELLPKSSALFYQKLIEDNGFPPLPENQPLEGTFPCDFAWGVVDNYVQVDTTLSQFTDPNVYLWDVHHSKRLIKVDGVVAKKRKPYCVDFSAIRPQITLLREMRVTHFRFSLDWALILPLGNQTQVNHTVLHFYRCMISELVHANITPVVALWQPAAPHQGLPHALAKHGAWENPHTALAFADYANLCFKELGHWVNLWITMNEPNTRNMTYRAGHHLLRAHALAWHLYDDKFRAAQKGKISIALQADWIEPACPFSQNDKEVAERVLEFDIGWLAEPIFGSGDYPRVMRDWLNQKNNFLLPYFTEDEKKLVRGSFDFLAVSHYTTILVDWEKEDPMKYNDYLEVQEMTDITWLNSPSQVAVVPWGLRKVLNWLRFKYGDLPMYVTANGIDDDPHAEQDSLRIYYIKNYVNEALKAYVLDDINLCGYFAYSLSDRSAPKSGFYRYAANQFEPKPSMKHYRKIIDSNGFLGSGTLGRFCPEEYTVCTECGFFQTRKSLLVFISFLVFTFIISLALIFHYSKKGQRSYK
|
3.2.1.31
| null |
calcium ion homeostasis [GO:0055074]; carbohydrate metabolic process [GO:0005975]; determination of adult lifespan [GO:0008340]; energy reserve metabolic process [GO:0006112]; fibroblast growth factor receptor signaling pathway [GO:0008543]; negative regulation of systemic arterial blood pressure [GO:0003085]; norepinephrine biosynthetic process [GO:0042421]; positive regulation of bone mineralization [GO:0030501]; positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway [GO:0090080]; response to activity [GO:0014823]; response to angiotensin [GO:1990776]; response to vitamin D [GO:0033280]
|
apical plasma membrane [GO:0016324]; extracellular region [GO:0005576]; membrane [GO:0016020]
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beta-glucuronidase activity [GO:0004566]; fibroblast growth factor binding [GO:0017134]; fibroblast growth factor receptor binding [GO:0005104]
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PF00232;
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3.20.20.80;
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Glycosyl hydrolase 1 family, Klotho subfamily
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PTM: N-glycosylated. {ECO:0000269|PubMed:15135068}.
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SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:10631108, ECO:0000269|PubMed:12204354, ECO:0000269|PubMed:15135068, ECO:0000269|PubMed:9363890}; Single-pass type I membrane protein {ECO:0000305|PubMed:9363890}. Apical cell membrane {ECO:0000269|PubMed:15665504}; Single-pass type I membrane protein {ECO:0000305|PubMed:15665504}. Note=Isoform 1 shedding leads to a soluble peptide. {ECO:0000269|PubMed:16123266}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:10631108, ECO:0000269|PubMed:15135068}.; SUBCELLULAR LOCATION: [Klotho peptide]: Secreted {ECO:0000269|PubMed:16123266}.
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CATALYTIC ACTIVITY: Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate; Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31; Evidence={ECO:0000269|PubMed:14701853};
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BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.249 mM for 4-methylumbelliferylglucuronide {ECO:0000269|PubMed:14701853}; KM=0.251 mM for estrone 3-beta-D-glucuronide {ECO:0000269|PubMed:14701853}; KM=0.174 mM for beta-estradiol 3-beta-D-glucuronide {ECO:0000269|PubMed:14701853}; KM=0.251 mM for estriol 3-beta-D-glucuronide {ECO:0000269|PubMed:14701853}; Vmax=0.62 uM/h/ug enzyme {ECO:0000269|PubMed:14701853};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:14701853};
| null |
FUNCTION: May have weak glycosidase activity towards glucuronylated steroids. However, it lacks essential active site Glu residues at positions 241 and 874, suggesting it may be inactive as a glycosidase in vivo. May be involved in the regulation of calcium and phosphorus homeostasis by inhibiting the synthesis of active vitamin D. Essential factor for the specific interaction between FGF23 and FGFR1.; FUNCTION: The Klotho peptide generated by cleavage of the membrane-bound isoform may be an anti-aging circulating hormone which would extend life span by inhibiting insulin/IGF1 signaling.
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Mus musculus (Mouse)
|
O35083
|
PLCA_MOUSE
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MELWPGAWTALLLLLLLLLSTLWFCSSSAKYFFKMAFYNGWILFLAILAIPVCAVRGRNVENMKILRLLLLHAKYLYGIRVEVRGAHHFPPTQPYVVVSNHQSSLDLLGMMEVLPDRCVPIAKRELLWAGSAGLACWLAGIIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGTRNHNGSMLPFKRGAFHLAVQAQVPIIPIVMSSYQDFYSKKERRFTSPGRCQVRVLPPVSTEGLTPDDVPALADSVRHSMLTIFREISTDGLGGGDCLKKPGGAGEARL
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2.3.1.51
| null |
CDP-diacylglycerol biosynthetic process [GO:0016024]; phosphatidic acid biosynthetic process [GO:0006654]
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endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
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1-acylglycerol-3-phosphate O-acyltransferase activity [GO:0003841]
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PF01553;
| null |
1-acyl-sn-glycerol-3-phosphate acyltransferase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99943}; Multi-pass membrane protein {ECO:0000255}.
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CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709, ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342, ChEBI:CHEBI:58608; EC=2.3.1.51; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74544, ChEBI:CHEBI:74546; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74544, ChEBI:CHEBI:74551; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + heptadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-heptadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37155, ChEBI:CHEBI:57287, ChEBI:CHEBI:74307, ChEBI:CHEBI:74544, ChEBI:CHEBI:74558; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37156; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37147, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:74544, ChEBI:CHEBI:74552; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37159, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:74544, ChEBI:CHEBI:74563; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + tetradecanoyl-CoA = 1-(9Z)-octadecenoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37171, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:74544, ChEBI:CHEBI:74579; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + pentadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-pentadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37175, ChEBI:CHEBI:57287, ChEBI:CHEBI:74309, ChEBI:CHEBI:74544, ChEBI:CHEBI:74578; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37176; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57518, ChEBI:CHEBI:64839; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z,15Z)-octadecatrienoyl-sn-glycero-3-phosphate = 1-(9Z,12Z,15Z)-octadecatrienoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37139, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74549, ChEBI:CHEBI:74550; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37140; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(6Z,9Z,12Z-octadecatrienoyl)-sn-glycero-3-phosphate = (6Z,9Z,12Z)-octadecatrienoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37179, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74581, ChEBI:CHEBI:74582; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37180; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-eicosanoyl-sn-glycero-3-phosphate = 1-eicosanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37183, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74583, ChEBI:CHEBI:74584; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37184; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-tetradecanoyl-sn-glycerol 3-phosphate = 1-tetradecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:72683, ChEBI:CHEBI:74586; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37188; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37443, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74544, ChEBI:CHEBI:74928; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + dodecanoyl-CoA = 1-(9Z)-octadecenoyl-2-dodecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37591, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:74544, ChEBI:CHEBI:75076; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37592; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=(6Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(6Z)-octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37607, ChEBI:CHEBI:57287, ChEBI:CHEBI:74544, ChEBI:CHEBI:75123, ChEBI:CHEBI:75124; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37608; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=(11Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(11Z)-octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37603, ChEBI:CHEBI:57287, ChEBI:CHEBI:74544, ChEBI:CHEBI:75121, ChEBI:CHEBI:75122; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37604; Evidence={ECO:0000250|UniProtKB:Q99943}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z-octadecenoyl)-2-(9Z-hexadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:40195, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540, ChEBI:CHEBI:74544, ChEBI:CHEBI:74697; Evidence={ECO:0000250|UniProtKB:Q99943}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40196; Evidence={ECO:0000250|UniProtKB:Q99943};
| null |
PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
| null | null |
FUNCTION: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. {ECO:0000250|UniProtKB:Q99943}.
|
Mus musculus (Mouse)
|
O35084
|
CP27B_MOUSE
|
MTQAVKLASRVFHRIHLPLQLDASLGSRGSESVLRSLSDIPGPSTLSFLAELFCKGGLSRLHELQVHGAARYGPIWSGSFGTLRTVYVADPTLVEQLLRQESHCPERCSFSSWAEHRRRHQRACGLLTADGEEWQRLRSLLAPLLLRPQAAAGYAGTLDNVVRDLVRRLRRQRGRGSGLPGLVLDVAGEFYKFGLESIGAVLLGSRLGCLEAEVPPDTETFIHAVGSVFVSTLLTMAMPNWLHHLIPGPWARLCRDWDQMFAFAQRHVELREGEAAMRNQGKPEEDMPSGHHLTHFLFREKVSVQSIVGNVTELLLAGVDTVSNTLSWTLYELSRHPDVQTALHSEITAGTRGSCAHPHGTALSQLPLLKAVIKEVLRLYPVVPGNSRVPDRDIRVGNYVIPQDTLVSLCHYATSRDPTQFPDPNSFNPARWLGEGPTPHPFASLPFGFGKRSCIGRRLAELELQMALSQILTHFEVLPEPGALPIKPMTRTVLVPERSINLQFVDR
|
1.14.15.18
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:15972816};
|
bone mineralization [GO:0030282]; C21-steroid hormone biosynthetic process [GO:0006700]; calcitriol biosynthetic process from calciol [GO:0036378]; calcium ion homeostasis [GO:0055074]; calcium ion transport [GO:0006816]; cellular response to peptide hormone stimulus [GO:0071375]; cholesterol metabolic process [GO:0008203]; cortisol metabolic process [GO:0034650]; decidualization [GO:0046697]; G1 to G0 transition [GO:0070314]; glucocorticoid biosynthetic process [GO:0006704]; negative regulation of bone trabecula formation [GO:1900155]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of ossification [GO:0030279]; positive regulation of keratinocyte differentiation [GO:0045618]; positive regulation of parathyroid hormone secretion [GO:2000830]; positive regulation of vitamin D receptor signaling pathway [GO:0070564]; regulation of bone mineralization [GO:0030500]; response to cAMP [GO:0051591]; response to copper ion [GO:0046688]; response to estrogen [GO:0043627]; response to insulin [GO:0032868]; response to lipopolysaccharide [GO:0032496]; response to prostaglandin E [GO:0034695]; response to type II interferon [GO:0034341]; response to vitamin D [GO:0033280]; response to xenobiotic stimulus [GO:0009410]; vitamin D catabolic process [GO:0042369]; vitamin D metabolic process [GO:0042359]
|
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]
|
calcidiol 1-monooxygenase activity [GO:0004498]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; secalciferol 1-monooxygenase activity [GO:0062185]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Mitochondrion membrane.
|
CATALYTIC ACTIVITY: Reaction=calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = calcitriol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:20573, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17823, ChEBI:CHEBI:17933, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.14.15.18; Evidence={ECO:0000269|PubMed:10092858, ECO:0000269|PubMed:15972816}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20574; Evidence={ECO:0000305|PubMed:15972816}; CATALYTIC ACTIVITY: Reaction=2 H(+) + O2 + 2 reduced [adrenodoxin] + secalciferol = calcitetrol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:49064, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28818, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47799; EC=1.14.15.18; Evidence={ECO:0000269|PubMed:10092858}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49065; Evidence={ECO:0000305|PubMed:10092858}; CATALYTIC ACTIVITY: Reaction=25-hydroxy-24-oxocalciol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = (1S)-1,25-dihydroxy-24-oxocalciol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:49068, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47805, ChEBI:CHEBI:47812; Evidence={ECO:0000250|UniProtKB:O15528}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49069; Evidence={ECO:0000250|UniProtKB:O15528}; CATALYTIC ACTIVITY: Reaction=25-hydroxyvitamin D2 + 2 H(+) + O2 + 2 reduced [adrenodoxin] = 1alpha,25-dihydroxyvitamin D2 + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:49048, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:86319, ChEBI:CHEBI:86320; Evidence={ECO:0000250|UniProtKB:O15528}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49049; Evidence={ECO:0000250|UniProtKB:O15528};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.7 uM for 25-hydroxyvitamin D3 {ECO:0000269|PubMed:10092858}; KM=1.3 uM for 24,25-dihydroxyvitamin D3 {ECO:0000269|PubMed:10092858}; KM=0.28 uM for 25-hydroxyvitamin D3 {ECO:0000269|PubMed:15972816}; Vmax=9.5 pmol/min/mg enzyme with 25-hydroxyvitamin D3 as substrate {ECO:0000269|PubMed:10092858}; Vmax=16.7 pmol/min/mg enzyme with 24,25-dihydroxyvitamin D3 as substrate {ECO:0000269|PubMed:10092858};
|
PATHWAY: Hormone biosynthesis; vitamin D biosynthesis. {ECO:0000250|UniProtKB:O15528}.
| null | null |
FUNCTION: A cytochrome P450 monooxygenase involved in vitamin D metabolism and in calcium and phosphorus homeostasis. Catalyzes the rate-limiting step in the activation of vitamin D in the kidney, namely the hydroxylation of 25-hydroxyvitamin D3/calcidiol at the C1-alpha position to form the hormonally active form of vitamin D3, 1alpha,25-dihydroxyvitamin D3/calcitriol that acts via the vitamin D receptor (VDR) (PubMed:10092858, PubMed:15972816). Has 1-alpha-hydroxylase activity on vitamin D intermediates of the CYP24A1-mediated inactivation pathway. Converts 24R,25-dihydroxyvitamin D3/secalciferol to 1-alpha,24,25-trihydroxyvitamin D3, an active ligand of VDR. Also active on 25-hydroxyvitamin D2 (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via FDXR/adrenodoxin reductase and FDX1/adrenodoxin (PubMed:10092858, PubMed:15972816). {ECO:0000250|UniProtKB:O15528, ECO:0000269|PubMed:10092858, ECO:0000269|PubMed:15972816}.
|
Mus musculus (Mouse)
|
O35085
|
ARX_MOUSE
|
MSNQYQEEGCSERPECKSKSPTLLSSYCIDSILGRRSPCKMRLLGAAQSLPAPLASRADQEKAMQGSPKSSSAPFEAELHLPPKLRRLYGPGGGRLLQGAAAAAAAAAAAAAAATATGTAGPRGEVPPPPPPAARPGERQDSAGAVAAAAAAAAWDTLKISQAPQVSISRSKSYRENGAPFVPPPPALDELSGPGGVAHPEERLSAASGPGSAPAAGGGTGAEDDEEELLEDEEDEEEEEELLEDDDEELLEDDARALLKEPRRCSVATTGTVAAAAAAAAAAVATEGGELSPKEELLLHPEDAEGKDGEDSVCLSAGSDSEEGLLKRKQRRYRTTFTSYQLEELERAFQKTHYPDVFTREELAMRLDLTEARVQVWFQNRRAKWRKREKAGAQTHPPGLPFPGPLSATHPLSPYLDASPFPPHHPALDSAWTAAAAAAAAAFPSLPPPPGSASLPPSGAPLGLSTFLGAAVFRHPAFISPAFGRLFSTMAPLTSASTAAALLRQPTPAVEGAVASGALADPATAAADRRASSIAALRLKAKEHAAQLTQLNILPGTSTGKEVC
| null | null |
axon guidance [GO:0007411]; cell proliferation in forebrain [GO:0021846]; cerebral cortex GABAergic interneuron migration [GO:0021853]; cerebral cortex tangential migration [GO:0021800]; embryonic olfactory bulb interneuron precursor migration [GO:0021831]; epithelial cell fate commitment [GO:0072148]; forebrain development [GO:0030900]; globus pallidus development [GO:0021759]; interneuron migration [GO:1904936]; lipid digestion [GO:0044241]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron migration [GO:0001764]; olfactory bulb development [GO:0021772]; organ growth [GO:0035265]; positive regulation of gene expression [GO:0010628]; positive regulation of organ growth [GO:0046622]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of epithelial cell proliferation [GO:0050678]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF00046;PF03826;
|
1.10.10.60;
|
Paired homeobox family, Bicoid subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}.
| null | null | null | null | null |
FUNCTION: Transcription factor (By similarity). Binds to specific sequence motif 5'-TAATTA-3' in regulatory elements of target genes, such as histone demethylase KDM5C (By similarity). Positively modulates transcription of KDM5C (PubMed:31691806). Activates expression of KDM5C synergistically with histone lysine demethylase PHF8 and perhaps in competition with transcription regulator ZNF711; synergy may be related to enrichment of histone H3K4me3 in regulatory elements (By similarity). Required for normal brain development (PubMed:12379852). Plays a role in neuronal proliferation, interneuronal migration and differentiation in the embryonic forebrain (PubMed:12379852, PubMed:31691806). May also be involved in axonal guidance in the floor plate (PubMed:9256348). {ECO:0000250|UniProtKB:Q96QS3, ECO:0000269|PubMed:12379852, ECO:0000269|PubMed:31691806, ECO:0000269|PubMed:9256348}.
|
Mus musculus (Mouse)
|
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