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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O46600
|
GHR_BOVIN
|
MDLWQLLLTLAVAGSSDAFSGSEATPAFLVRASQSLQILYPVLETNSSGNPKFTKCRSPELETFSCHWTDGANHSLQSPGSVQMFYIRRDIQEWKECPDYVSAGENSCYFNSSYTSVWTPYCIKLTSNGGIVDHKCFSVEDIVQPDPPVGLNWTLLNISLTEIHADILVKWEPPPNTDVKMGWIILEYELHYKELNETQWKMMDPLMVTSVPMYSLRLDKEYEVRVRTRQRNTEKYGKFSEVLLITFPQMNPSACEEDFQFPWFLIIIFGILGLAVTLYLLIFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNTILAIHDNYKHEFYNDDSWVEFIELDIDDPDEKTEGSDTDRLLSNDHEKSLNIFGAKDDDSGRTSCYEPDILEADFHVSDMCDGTSEVAQPQRLKGEADISCLDQKNQNNSPSNDAAPASQQPSVILVEENKPRPLLIGGTESTHQAVHTQLSNPSSLANIDFYAQVSDITPAGNVVLSPGQKNKTGNPQCDTHPEVVTPCQANFIVDNAYFCEVDAKKYIALAPHVEAESHVEPSFNQEDIYITTESLTTTAGRSGTAEHVPSSEIPVPDYTSIHIVQSPQGLVLNATALPLPDKEFLSSCGYVSTDQLNKIMP
| null | null |
cytokine-mediated signaling pathway [GO:0019221]; endocytosis [GO:0006897]; growth hormone receptor signaling pathway [GO:0060396]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]
|
cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; growth hormone receptor complex [GO:0070195]; membrane [GO:0016020]
|
cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; growth hormone receptor activity [GO:0004903]; peptide hormone binding [GO:0017046]
|
PF09067;PF12772;
|
2.60.40.10;
|
Type I cytokine receptor family, Type 1 subfamily
|
PTM: On GH binding, phosphorylated on tyrosine residues in the cytoplasmic domain by JAK2. {ECO:0000250}.; PTM: On ligand binding, ubiquitinated on lysine residues in the cytoplasmic domain. This ubiquitination is not sufficient for GHR internalization (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non-degradative pathway. {ECO:0000250}.; SUBCELLULAR LOCATION: [Growth hormone-binding protein]: Secreted {ECO:0000250}. Note=Complexed to a substantial fraction of circulating GH. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to, and activates the JAK2/STAT5 pathway (By similarity). {ECO:0000250}.; FUNCTION: The soluble form (GHBP) acts as a reservoir of growth hormone in plasma and may be a modulator/inhibitor of GH signaling.
|
Bos taurus (Bovine)
|
O46606
|
DDHD1_BOVIN
|
MNYPGHGSPRSSERNGGRGGDGAAWELGSDTEPAFGGSVCRFDHLPVGEPGDDEVPLALLRGEPGLHLAPGAEDHNHHLALDPCLSDDNYDFSSAESGSSLRYYSEGESGGGGSSSSLHPPQQPLVPSNSGGGGAAGGGPGERKRTRPGGAAARHRYEVVTELGPEEVRWFYKEDKKTWKPFIGYDSLRIELAFRTLLQATGARARAQDPDGDHVCGPASPAGPASSSVEDEDEDRVCGFCPRIAGHGREMEELVNIERVCVRGGLYEVDVTQGECYPVYWNQSDKIPVMRGQWFIDGTWQPLEEEESNLIEQEHLSRFRGQQMQESFDIEVSKPIDGKDAIHSFKLSRNHVDWHSVDEVYLYSDATTSKIARTVTQKLGFSKASSSGTRLHRGYVEEATLEDKPSQTTHIVFVVHGIGQKMDQGRIIKNTAMMREAARKIEERHFSNHATHVEFLPVEWRSKLTLDGDTVDSITPDKVRGLRDMLNSSAMDIMYYTSPLYRDELVKGLQQELNRLYSLFCSRNPNFEEKGGKVSIVSHSLGCVITYDIMTGWNPVRLYEQLLQKEEELPDERWMSYEERHLLDELYITKRRLREIEERLHGLKASSMTQTPALKFKVENFFCMGSPLAVFLALRGIRPGNTGSQDHILPREICNRLLNIFHPTDPVAYRLEPLILKHYSNISPVQIHWYNTSNPLPYEYMKPSFLHPAKDPTSISENEGISTIPSPVTSPVLSRRHYGESITNIGKASILGAASIGKGLGGMLFSRFGRSSASQPSETSRDSIEDEKKPVASPPMTTVATQTLPHSSSGFLDSALELDHRIDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMYKHEHDNNVKPSLDPV
|
3.1.1.111; 3.1.1.118; 3.1.1.32
| null |
phosphatidylinositol metabolic process [GO:0046488]
|
cytoplasm [GO:0005737]
|
metal ion binding [GO:0046872]; phospholipase A1 activity [GO:0008970]; phospholipase activity [GO:0004620]
|
PF02862;
| null |
PA-PLA1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NEL9}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 2-acyl-sn-glycerol 3-phosphate + a fatty acid + H(+); Xref=Rhea:RHEA:44648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:58608, ChEBI:CHEBI:64982; EC=3.1.1.118; Evidence={ECO:0000269|PubMed:10924127, ECO:0000305|PubMed:7937808, ECO:0000305|PubMed:9488669}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44649; Evidence={ECO:0000269|PubMed:10924127, ECO:0000305|PubMed:7937808, ECO:0000305|PubMed:9488669}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = a 2-acyl-sn-glycero-3-phospho-D-myo-inositol + a fatty acid + H(+); Xref=Rhea:RHEA:35263, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57880, ChEBI:CHEBI:64872; EC=3.1.1.118; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35264; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + H(+) + octadecanoate; Xref=Rhea:RHEA:73967, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:133606, ChEBI:CHEBI:193055; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73968; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + a fatty acid + H(+); Xref=Rhea:RHEA:73971, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:75243, ChEBI:CHEBI:193055; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73972; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = 2-hexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + H(+) + hexadecanoate; Xref=Rhea:RHEA:66708, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72835, ChEBI:CHEBI:167448; Evidence={ECO:0000250|UniProtKB:Q80YA3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66709; Evidence={ECO:0000250|UniProtKB:Q80YA3}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:45128, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74546, ChEBI:CHEBI:77593; Evidence={ECO:0000269|PubMed:10924127, ECO:0000305|PubMed:7937808, ECO:0000305|PubMed:9488669}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45129; Evidence={ECO:0000269|PubMed:10924127, ECO:0000305|PubMed:7937808, ECO:0000305|PubMed:9488669}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + H2O = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + a fatty acid + H(+); Xref=Rhea:RHEA:73975, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:74922, ChEBI:CHEBI:78209; Evidence={ECO:0000305|PubMed:7937808}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73976; Evidence={ECO:0000305|PubMed:7937808}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + hexadecanoate; Xref=Rhea:RHEA:40943, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64839, ChEBI:CHEBI:77593; Evidence={ECO:0000269|PubMed:10924127, ECO:0000305|PubMed:7937808}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40944; Evidence={ECO:0000269|PubMed:10924127, ECO:0000305|PubMed:7937808}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H(+) + hexadecanoate; Xref=Rhea:RHEA:43968, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75029, ChEBI:CHEBI:77342; Evidence={ECO:0000250|UniProtKB:Q80YA3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43969; Evidence={ECO:0000250|UniProtKB:Q80YA3}; CATALYTIC ACTIVITY: Reaction=1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:74159, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:77126, ChEBI:CHEBI:78209; Evidence={ECO:0000305|PubMed:7937808}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74160; Evidence={ECO:0000305|PubMed:7937808}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + H2O = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + H(+) + octadecanoate; Xref=Rhea:RHEA:74163, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:77091, ChEBI:CHEBI:78209; Evidence={ECO:0000305|PubMed:7937808}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74164; Evidence={ECO:0000305|PubMed:7937808}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+); Xref=Rhea:RHEA:44408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64612, ChEBI:CHEBI:65213; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44409; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H2O = a 2-acyl-sn-glycero-3-phospho-L-serine + a fatty acid + H(+); Xref=Rhea:RHEA:42212, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57262, ChEBI:CHEBI:65214; EC=3.1.1.111; Evidence={ECO:0000250|UniProtKB:Q80YA3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42213; Evidence={ECO:0000250|UniProtKB:Q80YA3}; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = 2-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a fatty acid + H(+); Xref=Rhea:RHEA:67428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64716, ChEBI:CHEBI:76528; Evidence={ECO:0000250|UniProtKB:Q80YA3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67429; Evidence={ECO:0000250|UniProtKB:Q80YA3}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+) + hexadecanoate; Xref=Rhea:RHEA:74103, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72841, ChEBI:CHEBI:141490; Evidence={ECO:0000250|UniProtKB:Q80YA3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74104; Evidence={ECO:0000250|UniProtKB:Q80YA3}; CATALYTIC ACTIVITY: Reaction=1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:74247, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:75063, ChEBI:CHEBI:76079; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74248; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; CATALYTIC ACTIVITY: Reaction=1-acyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+); Xref=Rhea:RHEA:74251, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:75067, ChEBI:CHEBI:76091; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74252; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-2-(7Z,10Z,13Z,16Z,19Z-docosapentaenoyl)-sn-glycero-3-phospho-1D-myo-inositol + H2O = (9Z)-octadecenoate + 2-(7Z,10Z,13Z,16Z,19Z-docosapentaenoyl)-sn-glycero-3-phospho-1D-myo-inositol + H(+); Xref=Rhea:RHEA:76971, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:195484, ChEBI:CHEBI:195486; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76972; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-1D-myo-inositol + H2O = (9Z)-octadecenoate + 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + H(+); Xref=Rhea:RHEA:76975, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:78765, ChEBI:CHEBI:193055; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76976; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-1D-myo-inositol + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-1D-myo-inositol + H(+); Xref=Rhea:RHEA:76979, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:195485, ChEBI:CHEBI:195487; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76980; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-2-(8Z,11Z,14Z-eicosatrienoyl)-sn-glycero-3-phospho-1D-myo-inositol + H2O = (9Z)-octadecenoate + 2-(8Z,11Z,14Z-eicosatrienoyl)-sn-glycero-3-phospho-1D-myo-inositol + H(+); Xref=Rhea:RHEA:76983, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:195488, ChEBI:CHEBI:195489; Evidence={ECO:0000250|UniProtKB:Q8NEL9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76984; Evidence={ECO:0000250|UniProtKB:Q8NEL9};
| null |
PATHWAY: Phospholipid metabolism; phosphatidylinositol metabolism. {ECO:0000250|UniProtKB:Q8NEL9}.
| null | null |
FUNCTION: Phospholipase A1 (PLA1) that hydrolyzes ester bonds at the sn-1 position of glycerophospholipids producing a free fatty acid and a lysophospholipid (PubMed:10924127, PubMed:7937808, PubMed:9488669). Prefers phosphatidate (1,2-diacyl-sn-glycero-3-phosphate, PA) as substrate in vitro, but can efficiently hydrolyze phosphatidylinositol (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol), PI), as well as a range of other glycerophospholipid substrates such as phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE), phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) and phosphatidylglycerol (1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol), PG) (PubMed:10924127, PubMed:7937808). Involved in the regulation of the endogenous content of polyunsaturated PI and PS lipids in the nervous system. Changes in these lipids extend to downstream metabolic products like PI phosphates PIP and PIP2, which play fundamental roles in cell biology (By similarity). Regulates mitochondrial morphology. These dynamic changes may be due to PA hydrolysis at the mitochondrial surface (By similarity). May play a regulatory role in spermatogenesis or sperm function (PubMed:7937808). {ECO:0000250|UniProtKB:Q80YA3, ECO:0000250|UniProtKB:Q8NEL9, ECO:0000269|PubMed:10924127, ECO:0000269|PubMed:7937808, ECO:0000269|PubMed:9488669, ECO:0000303|PubMed:7937808}.
|
Bos taurus (Bovine)
|
O46629
|
ECHB_BOVIN
|
MISLLTYTLKNLPNTSKWALRFCMRPLSSSSQLQAAAASQTKSKKTLAKPNIRNIVVVDGVRTPFLLSGTSYKDLMPHDLARAALSGLLHRTSVPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDIPIRHSRKMRKMMLDLNKAKTLAQRLSIISKFRLNFLSPELPAVSEFSTSETMGHSADRLAAAFAISREEQDEYALRSHSLAKKAQDEGLLSDVVPFKVPGRDTVTQDNGIRPSSLDQMAKLKPAFIKPYGTVTAANSSFLTDGASAVLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDVFEFHEAFSGQILANLKAMDSDWFAQNYMGRKAKVGLPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK
|
2.3.1.155; 2.3.1.16
| null |
fatty acid beta-oxidation [GO:0006635]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
|
acetyl-CoA C-acetyltransferase activity [GO:0003985]; acetyl-CoA C-myristoyltransferase activity [GO:0050633]
|
PF02803;PF00108;
|
3.40.47.10;
|
Thiolase-like superfamily, Thiolase family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P55084}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P55084}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P55084}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P55084}. Note=Protein stability and association with membranes require HADHA. {ECO:0000250|UniProtKB:P55084}.
|
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA; Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16; Evidence={ECO:0000250|UniProtKB:P55084}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566; Evidence={ECO:0000250|UniProtKB:P55084}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + butanoyl-CoA = 3-oxohexanoyl-CoA + CoA; Xref=Rhea:RHEA:31111, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57371, ChEBI:CHEBI:62418; Evidence={ECO:0000250|UniProtKB:P55084}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31113; Evidence={ECO:0000250|UniProtKB:P55084}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + hexanoyl-CoA = 3-oxooctanoyl-CoA + CoA; Xref=Rhea:RHEA:31203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:62619, ChEBI:CHEBI:62620; Evidence={ECO:0000250|UniProtKB:P55084}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205; Evidence={ECO:0000250|UniProtKB:P55084}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + octanoyl-CoA = 3-oxodecanoyl-CoA + CoA; Xref=Rhea:RHEA:31087, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57386, ChEBI:CHEBI:62548; Evidence={ECO:0000250|UniProtKB:P55084}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089; Evidence={ECO:0000250|UniProtKB:P55084}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + decanoyl-CoA = 3-oxododecanoyl-CoA + CoA; Xref=Rhea:RHEA:31183, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61430, ChEBI:CHEBI:62615; Evidence={ECO:0000250|UniProtKB:P55084}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185; Evidence={ECO:0000250|UniProtKB:P55084}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + dodecanoyl-CoA = 3-oxotetradecanoyl-CoA + CoA; Xref=Rhea:RHEA:31091, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57375, ChEBI:CHEBI:62543; Evidence={ECO:0000250|UniProtKB:P55084}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093; Evidence={ECO:0000250|UniProtKB:P55084}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CoA; Xref=Rhea:RHEA:18161, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57349, ChEBI:CHEBI:57385; EC=2.3.1.155; Evidence={ECO:0000250|UniProtKB:P55084}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163; Evidence={ECO:0000250|UniProtKB:P55084};
| null |
PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000250|UniProtKB:P55084}.
| null | null |
FUNCTION: Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities, while the trifunctional enzyme subunit beta/HADHB described here bears the 3-ketoacyl-CoA thiolase activity. {ECO:0000250|UniProtKB:P55084}.
|
Bos taurus (Bovine)
|
O46631
|
SHPS1_BOVIN
|
MEPARPAPGRLRPLLCLLLAASNAWTGTAGDGELQVIQPERSVSVAAGETATLHCTVTSLSPVGPIKWFKGTGPGREFIYSQKEAPFPRVTNVSDATKRNNMDFSIRISNITPADAGVYYCVKFRKEERGDMEFKSGPGTHLTVSAKPSPPVLSGPTVRATPEQTVNFTCTSHGFSPRNISLKWFKNGNELSASQTSVDPEDNNVSYSINSTTKVLLATGDVHSQVICEVAHVTLQGGPPLRGTANLSETIRVPPTLEITGSPSAGNQVNVTCQVNKFYPRHLQLTWLENGNMSRTEAASVFVENKDGTFNQTSWFLVNSSAHREAVVLTCQVEHDGQPAVSKNHTLEVSAPQKDQDTGQTPGPNDSNWTSIFIVVGVVCALLVALLIAALYLLRIRQNKAKGSTSSTRLHEPEKNTRETTQIQDNNDITYADLNLPKGKKSTPKANEPNNHTEYASIQARPPPVSEDTLTYADLDMVHLNRTPKQPAPKPEPSYSEYASVQVQRK
| null | null |
cellular response to stimulus [GO:0051716]; positive regulation of phagocytosis [GO:0050766]; positive regulation of T cell activation [GO:0050870]
|
plasma membrane [GO:0005886]
|
SH3 domain binding [GO:0017124]
|
PF07654;PF07686;
|
2.60.40.10;
| null |
PTM: Phosphorylated on tyrosine residues. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function. Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Plays a role in antiviral immunity and limits new world arenavirus infection by decreasing virus internalization (By similarity). Receptor for THBS1 (By similarity). Interaction with THBS1 stimulates phosphorylation of SIRPA (By similarity). In response to THBS1, involved in ROS signaling in non-phagocytic cells, stimulating NADPH oxidase-derived ROS production (By similarity). {ECO:0000250|UniProtKB:P78324, ECO:0000250|UniProtKB:P97710, ECO:0000250|UniProtKB:P97797}.
|
Bos taurus (Bovine)
|
O46635
|
5HT2A_CANLF
|
MDVLFEDNAPLSPTTSSLMPSNGDPRLYGNDLNAGDANTSDAFNWTVDAENRTNLSCEGCLSPPCFSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDPGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDIIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKKDAKSTDNDYSMVALGKQHSEDAPTDNINTVNEKVSCV
| null | null |
behavior [GO:0007610]; chemical synaptic transmission [GO:0007268]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007187]; intracellular calcium ion homeostasis [GO:0006874]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of phosphatidylinositol biosynthetic process [GO:0010513]; release of sequestered calcium ion into cytosol [GO:0051209]; response to xenobiotic stimulus [GO:0009410]
|
axon [GO:0030424]; caveola [GO:0005901]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; G protein-coupled serotonin receptor complex [GO:0098666]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
|
1-(4-iodo-2,5-dimethoxyphenyl)propan-2-amine binding [GO:0071886]; G protein-coupled serotonin receptor activity [GO:0004993]; Gq/11-coupled serotonin receptor activity [GO:0001587]; identical protein binding [GO:0042802]; neurotransmitter receptor activity [GO:0030594]; serotonin binding [GO:0051378]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15862800}; Multi-pass membrane protein {ECO:0000269|PubMed:15862800}. Cell projection, dendrite {ECO:0000250|UniProtKB:P35363}. Cell projection, axon {ECO:0000250|UniProtKB:P14842}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P14842}. Membrane, caveola {ECO:0000250|UniProtKB:P14842}. Presynapse {ECO:0000250|UniProtKB:P14842}.
| null | null | null | null | null |
FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates phospholipase C and a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and promotes the release of Ca(2+) ions from intracellular stores. Affects neural activity, perception, cognition and mood. Plays a role in the regulation of behavior, including responses to anxiogenic situations and psychoactive substances. Plays a role in intestinal smooth muscle contraction, and may play a role in arterial vasoconstriction. {ECO:0000269|PubMed:15862800}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O46647
|
LIPL_NEOVI
|
MESKALLLVALGMWFQSLTATRGGVAAADRGGDFIDIESKFALRTPEDTAEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGKDVAKFINWMAEEFHYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESDTQTNQAFEISLYGTVAESENIPFTLPEVSANKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIEKIRVKAGETQKKVIFCSREKVSHLQKGKASVVFVKCHDKSLNKKSG
|
3.1.1.34
| null |
chylomicron remodeling [GO:0034371]; fatty acid biosynthetic process [GO:0006633]; fatty acid metabolic process [GO:0006631]; response to glucose [GO:0009749]; triglyceride catabolic process [GO:0019433]; very-low-density lipoprotein particle remodeling [GO:0034372]
|
chylomicron [GO:0042627]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; very-low-density lipoprotein particle [GO:0034361]
|
apolipoprotein binding [GO:0034185]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; lipoprotein lipase activity [GO:0004465]; lipoprotein particle binding [GO:0071813]; metal ion binding [GO:0046872]
|
PF00151;PF01477;
|
3.40.50.1820;2.60.60.20;
|
AB hydrolase superfamily, Lipase family
|
PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity. {ECO:0000250|UniProtKB:Q06000}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11151}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11151}; Extracellular side {ECO:0000250|UniProtKB:P11151}. Secreted {ECO:0000250|UniProtKB:P11151}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P11151}. Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells. Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles. {ECO:0000250|UniProtKB:P11151}.
|
CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.34; Evidence={ECO:0000250|UniProtKB:P11151};
| null | null | null | null |
FUNCTION: Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:9852258). Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (By similarity). {ECO:0000250|UniProtKB:P06858, ECO:0000269|PubMed:9852258}.
|
Neovison vison (American mink) (Mustela vison)
|
O46658
|
CP2DP_PIG
|
MGLLTGDLLGILALAMVIFLLLVDLMHRRSRWAPRYPPGPMPLPGLGNLLQVNFQDPRLSFIQLRRRFGDVFSLQQIWRPVVVLNGLAAVREALVSHSHETSDRPPVFILEHLGYGPRSEGVILARYGKAWREQRRFSVSTLRNFGLGKKSLEEWVTQEASCLCAAFADQAGRPFSPNNLLNKAVSNVIASLTFARRFEYNDPRMLKLLDLVLEGLKEEVGLMRQVLEAMPVLRHIPGLCAKLFPRQKAFLVMIDELITEHKMTRDLAQPPRDLTDAFLDEMKEAKGNPESSFNDENLRLVVAHLFSAGMITTSTTLAWALLLMILHPDVQRRVQQEIDEVIGHVRQPEIKDQALMPFTLAVLHEVQRFGDIVPLGVAHMTSCDIEVQGFLIPKGTTLITNLTSVLKDETVWKKPFRFYPEHFLDAQGRFTKQEAFMPFSAGRRSCLGEPLARMELFLFFTTLLQAFSFSVPTGQPCPSDHGVFAFLLFPSPYQLCAVPR
|
1.14.14.24
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
|
arachidonic acid metabolic process [GO:0019369]; xenobiotic metabolic process [GO:0006805]
|
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]
|
3-alpha,7-alpha,12-alpha-trihydroxycholestan-26-al 26-oxidoreductase activity [GO:0047103]; cholestanetriol 26-monooxygenase activity [GO:0047749]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]; vitamin D3 25-hydroxylase activity [GO:0030343]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
|
CATALYTIC ACTIVITY: Reaction=calciol + O2 + reduced [NADPH--hemoprotein reductase] = calcidiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:32903, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17933, ChEBI:CHEBI:28940, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.24; Evidence={ECO:0000269|PubMed:1445236, ECO:0000269|PubMed:2169238}; CATALYTIC ACTIVITY: Reaction=alfacalcidol + O2 + reduced [NADPH--hemoprotein reductase] = calcitriol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49272, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17823, ChEBI:CHEBI:31186, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:1445236, ECO:0000269|PubMed:2169238}; CATALYTIC ACTIVITY: Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 12-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:38947, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18262, ChEBI:CHEBI:36204, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:1445236, ECO:0000269|PubMed:2169238}; CATALYTIC ACTIVITY: Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39751, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76628; Evidence={ECO:0000269|PubMed:1445236, ECO:0000269|PubMed:2169238}; CATALYTIC ACTIVITY: Reaction=5beta-cholestane-3alpha,7alpha-diol + O2 + reduced [NADPH--hemoprotein reductase] = 5beta-cholestane-3alpha,7alpha,25-triol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:67384, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28047, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:169972; Evidence={ECO:0000269|PubMed:1445236, ECO:0000269|PubMed:2169238}; CATALYTIC ACTIVITY: Reaction=5beta-cholestane-3alpha,7alpha,12alpha-triol + O2 + reduced [NADPH--hemoprotein reductase] = 5beta-cholestane-3alpha,7alpha,12alpha,25-tetrol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:67396, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16496, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:169973; Evidence={ECO:0000269|PubMed:1445236, ECO:0000269|PubMed:2169238};
| null | null | null | null |
FUNCTION: Catalyzes the 25-hydroxylation of vitamin D(3) (calciol), 1alpha-hydroxyvitamin D(3) (alphacalcidiol) and some C27 steroids. In addition the enzyme catalyzes the hydroxylation of positions 11 and 12 of dodecanoate. {ECO:0000269|PubMed:1445236, ECO:0000269|PubMed:2169238}.
|
Sus scrofa (Pig)
|
O46669
|
SCNAA_CANLF
|
MEFPFGSLETTNFRRFTPESLVEIEKRIAAKQAAKKAKGKHREQKDQEEKPRPQLDLKACNQPPKFYGELPAELVGEPLEDLDPFYSTHRTFMVLDKGRTISRFSATRALWLFSPFNLIRRTAIKVSVHSWFSLFITVTILVNCVGMTQTELPDRIEYVFTVIYTFEALIKILARGFCLNEFAYLRDPWDWLDFSVITLAYIGEATALRGISGLRTFRVLRALKTVSVIPGLKVIVGALIHSVRKLADVTILTVFCLSVFALVGLQLFKGNLKNKCVKNCAALNETGNYSSYGKQEWNFCHRDEDFYYNKPGTSDPLLCGNGSDAGHCPKGYLCLKTSDNPDFNYTSFDSFAWAFLSLFRLMTQDSWERLYQQTLRASGKMYMVFFVLVIFLGSFYLVNLILAVVTMAYEEQNQATIDEIEAKEKTFQETLEMPRKEQEVLAALGIDTASLHSCNGSPLPSKNASERMRRMKPRVSEGSTDDNKSPQSDPYNQRRMSFLGLTSGRRRASHGSVFHFRTPCLDTSFPDGVTDDGVFPGDRESHRGSLLLGGGTSQQGPLLRSPLPQPPNPGSGHGEDGHSTLPTGELAPGGIEVSAFDAGQKKTFLSAEYLNEPFRAQRAMSVVSIMTSVLEELEESERRCPPCLTSFAQKYLIWECCPTWVKLKTVLFGIVTDPFAELTTTLCIVVNTVFMAMEHHGMSSAFEAMLQIGNIVFTVFFTAEMVFKIIAFDPYYYFQKRWNIFDCIIVTVSLIELGAARKGSLSVLRTFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTIILAIIVFVFALVGKQLLGENYRDNRRNISAPNEEWPRWHMHDFFHSFLIVFRILCGEWIENMWACMEVGQKSICLILFLTVMVLGNLVVLNLFTALLLNSFSADNLATPDEDGEVNNLQVALARIQAFGHRTKKAICNFFTRPCLLPWPKAEPQLVVKLPLSSSKAENHIAANAAVGSPGGLSVSRGLRDDHSDFITNPNIWVSVPIAEGESDLDDLEEDGEEDSQSSQQEVILQGQEQLQVETCEGHTAPRSPGSGMSSEDLASYVDEKWKDEAVAQAPAEGGDDSSSSGGSTVDCLDPEEILRKIPELADDLEEPDDCFTEGCLRRCPCCKVDISKFPWTVGWQVRKTCYRIVEHSWFESFIIFMILLSSGSLAFEDYHLDQKPTVKALLEYTDRMFTFIFVLEMLLKWVAYGFKKYFTNAWCWLDFLIVNISLISLIAKILQYSDVASIKALRTLRALRPLRALSRFEGMRVVVDALVGAIPSIMNVLLVCLIFWLIFSTMGVNFFAGKFGRCINKTNEYFSLVPLSIVNNISDCKYQNHTGSFFWVNVKVNFDNVAMGYLALLQVATFKGWMDIMYAAVDARDVNLQPKWEDNVYMYLYFVIFIIFGGFFTLNLFVGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQGFVFDIVTKQAFDIVIMVLICLNMITMMVETDEQSAEKTKILNKINQFFVAVFTGECVMKMFALRHYYFTNGWNVFDFIVVVLSIGSLVFSVILTSLENYFSPTLFRVIRLARIGRILRLIRAAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMASFPHVSWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPNLPNSNGSRGNCGSPAVGILFFTTYIIISFLIVVNMYIAVILENFNVATQESSEPLSEDDFDMFYETWEKFDPEATQFITFSALSDFADTLSGPLRIPKPNQNILIQMDLPLVPGDKIHCLDILFAFTKNVLGESGELDSLKANIEEKFMATNVSKASYEPIATTLRWKQEDISATVIQKAYRSYVLHRSMTISNPPAVPRAEEAVPPPDEAFVEFMVNENCALPDKSETASAASFPPSYDSVTRGLSDQINMSTSSSMQNEDEGTSKKVTAPGP
| null | null |
membrane depolarization during action potential [GO:0086010]; neuronal action potential [GO:0019228]; regulation of atrial cardiac muscle cell membrane depolarization [GO:0060371]; regulation of heart rate [GO:0002027]; sodium ion transmembrane transport [GO:0035725]
|
axon [GO:0030424]; plasma membrane [GO:0005886]; voltage-gated sodium channel complex [GO:0001518]
|
voltage-gated sodium channel activity [GO:0005248]; voltage-gated sodium channel activity involved in cardiac muscle cell action potential [GO:0086006]
|
PF00520;PF06512;
|
1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350;
|
Sodium channel (TC 1.A.1.10) family, Nav1.8/SCN10A subfamily
|
PTM: Ubiquitinated by NEDD4L; which promotes its endocytosis. {ECO:0000250}.; PTM: Phosphorylation at Ser-1458 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250}.; PTM: Lacks the cysteine which covalently binds the conotoxin GVIIJ. This cysteine (position 825) is speculated in other sodium channel subunits alpha to be implied in covalent binding with the sodium channel subunit beta-2 or beta-4. {ECO:0000250|UniProtKB:P15389}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D0E0C2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Note=It can be translocated to the cell membrane through association with S100A10. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q9Y5Y9};
| null | null | null | null |
FUNCTION: Tetrodotoxin-resistant channel that mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance with their electrochemical gradient. Plays a role in neuropathic pain mechanisms. {ECO:0000250|UniProtKB:Q9Y5Y9}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O46674
|
AT2A2_CANLF
|
MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDRVEGDSCSLNEFTITGSTYAPIGEVHKDDKPVKCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTPGVKQKVMSVIREWGSGSDTLRCLALATHDNPLRREEMNLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELSPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKSEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVSFYQLSHFLQCKDDNPDFEGVDCAIFESPYPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITPLNLTQWLMVLKISLPVILMDETLKFVARNYLEPAILE
|
7.2.2.10
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P11607};
|
autophagosome assembly [GO:0000045]; autophagosome membrane docking [GO:0016240]; calcium ion transmembrane transport [GO:0070588]; intracellular calcium ion homeostasis [GO:0006874]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; organelle localization by membrane tethering [GO:0140056]; regulation of cardiac muscle contraction by calcium ion signaling [GO:0010882]
|
sarcoplasmic reticulum membrane [GO:0033017]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type calcium transporter activity involved in regulation of cardiac muscle cell membrane potential [GO:0086039]
|
PF13246;PF00689;PF00690;PF00122;PF00702;
|
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: Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity. {ECO:0000250|UniProtKB:P16615}.; PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia, leading to its inactivation. {ECO:0000250|UniProtKB:O55143}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with FLVCR2 at the mitochondrial-ER contact junction. {ECO:0000250|UniProtKB:O55143}.
|
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:0000250|UniProtKB:P16615}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106; Evidence={ECO:0000250|UniProtKB:P16615};
| null | null | null | null |
FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation. Also modulates ER contacts with lipid droplets, mitochondria and endosomes (By similarity). In coordination with FLVCR2 mediates heme-stimulated switching from mitochondrial ATP synthesis to thermogenesis (By similarity). {ECO:0000250|UniProtKB:O55143, ECO:0000250|UniProtKB:P16615}.; FUNCTION: [Isoform 1]: Involved in the regulation of the contraction/relaxation cycle. Acts as a regulator of TNFSF11-mediated Ca(2+) signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca(2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca(2+) signaling cascades that promote osteoclast differentiation and activation. {ECO:0000250|UniProtKB:O55143}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O46680
|
TGFR1_BOVIN
|
MEAAAATPRPRLFLLMLAAAATLVPEATPLQCFCHLCTKDNFTCVTDGLCFVSVTETTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGSITTTYCCNQDHCNKIELPTVGKPSSGLGPVELAAVIAGPVCFVCISLMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEVARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLSQQEGIKM
|
2.7.11.30
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
|
activin receptor signaling pathway [GO:0032924]; apoptotic process [GO:0006915]; cardiac epithelial to mesenchymal transition [GO:0060317]; cellular response to growth factor stimulus [GO:0071363]; cellular response to transforming growth factor beta stimulus [GO:0071560]; endothelial cell activation [GO:0042118]; heart development [GO:0007507]; intracellular signal transduction [GO:0035556]; mesenchymal cell differentiation [GO:0048762]; nervous system development [GO:0007399]; phosphorylation [GO:0016310]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of gene expression [GO:0010628]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of gene expression [GO:0010468]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
activin receptor complex [GO:0048179]; bicellular tight junction [GO:0005923]; cell surface [GO:0009986]; endosome [GO:0005768]; membrane [GO:0016020]; membrane raft [GO:0045121]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
activin binding [GO:0048185]; activin receptor activity, type I [GO:0016361]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; SMAD binding [GO:0046332]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity, type I [GO:0005025]
|
PF01064;PF00069;PF08515;
|
2.10.60.10;1.10.510.10;
|
Protein kinase superfamily, TKL Ser/Thr protein kinase family, TGFB receptor subfamily
|
PTM: Phosphorylated at basal levels in the absence of ligand. Activated upon phosphorylation by TGFBR2, mainly in the GS domain. Phosphorylation in the GS domain abrogates FKBP1A-binding (By similarity). {ECO:0000250|UniProtKB:P36897}.; PTM: N-Glycosylated. {ECO:0000250|UniProtKB:P36897}.; PTM: Ubiquitinated; undergoes ubiquitination catalyzed by several E3 ubiquitin ligases including SMURF1, SMURF2 and NEDD4L2. Results in the proteasomal and/or lysosomal degradation of the receptor thereby negatively regulating its activity. Deubiquitinated by USP15, leading to stabilization of the protein and enhanced TGF-beta signal. Its ubiquitination and proteasome-mediated degradation is negatively regulated by SDCBP (By similarity). {ECO:0000250|UniProtKB:P36897}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P36897}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P36897}. Cell junction, tight junction {ECO:0000250|UniProtKB:P36897}. Membrane raft {ECO:0000250|UniProtKB:P36897}. Cell surface {ECO:0000250|UniProtKB:P36897}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.30; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.30;
| null | null | null | null |
FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation (By similarity). {ECO:0000250|UniProtKB:P36897}.
|
Bos taurus (Bovine)
|
O48528
|
OP163_ARATH
|
MDPAEMRYLEEEDGPLMKTIKGSITGFGAGTIYGTILATWKDVPRVERNVALPGLIRTLKMMGTHGLTFAAIGGVYIGVEQLVQNFRSKRDFYNGAIGGFVAGASVLGYRARSIPTAIAAGATLAVTSALIDSGGQTTRVDNGREYYPYTVEKRAEADS
| null | null |
monoatomic ion transport [GO:0006811]; protein insertion into mitochondrial inner membrane [GO:0045039]
|
chloroplast [GO:0009507]; chloroplast outer membrane [GO:0009707]; cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; plastid outer membrane [GO:0009527]; pore complex [GO:0046930]; TIM22 mitochondrial import inner membrane insertion complex [GO:0042721]
|
mitochondrion targeting sequence binding [GO:0030943]; porin activity [GO:0015288]; protein homodimerization activity [GO:0042803]; protein transmembrane transporter activity [GO:0008320]
|
PF02466;
| null |
Tim17/Tim22/Tim23 family, Plastid outer envelope porin OEP16 (TC 1.B.30) subfamily
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:18431481}; Multi-pass membrane protein. Mitochondrion outer membrane {ECO:0000269|PubMed:21841088}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000269|PubMed:21841088}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Voltage-dependent high-conductance channel with a slight cation-selectivity; selective for amino acids but excludes triosephosphates or uncharged sugars. Non-essential amino acid-selective channel protein and translocation pore for NADPH:protochlorophyllide oxidoreductase A (PORA) and possibly PORB (By similarity). {ECO:0000250}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48533
|
PYM_ARATH
|
MPEARDRIERQVDYPAAFLNRRSHGILLDEPATQHNLFGSPVQRVPSEATGGLGSIGQGSMTGRGGLVRGNFGIRRTGGGRRGQIQFRSPQGRENMSLGVTRRGRARASNSVLPSWYPRTPLRDISAVVRAIERRRARMGEGVGRDIETPTPQQLGVLDSLVPLSGAHLEHDYSMVTPGPSIGFKRPWPPSTAKVHQILLDITRENTGEEDALTPEKKLLNSIDKVEKVVMEEIQKMKSTPSAKRAEREKRVRTLMSMR
| null | null |
cell division [GO:0051301]; defense response [GO:0006952]; DNA endoreduplication [GO:0042023]; endosperm development [GO:0009960]; megagametogenesis [GO:0009561]; negative regulation of ubiquitin protein ligase activity [GO:1904667]; positive regulation of defense response to bacterium [GO:1900426]; regulation of nuclear division [GO:0051783]; response to UV-B [GO:0010224]; trichome branching [GO:0010091]
|
nucleus [GO:0005634]
| null | null | null | null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22167059}. Note=Follows a patchy nuclear accumulation pattern.
| null | null | null | null | null |
FUNCTION: Negative regulator of the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase required for proper mitotic progression and cell fate determination; inhibits premature cell differentiation. Prevents DNA endoreplication by promoting the maintenance of the mitotic state by preferentially inhibiting APC/C(FZR) and triggering cyclins accumulation (e.g. CYCB1-1, CYCB1-2 and CYCA2-3) in a temporal manner. Required for megagametophyte and endosperm development. Counteracts the activity of CCS52A1 thus inhibiting the turnover of CYCA2-3. Confers immunity to bacterial pathogens (e.g. Pseudomonas syringae pv. tomato DC3000), which is associated with increased expression of disease resistance (R) genes. {ECO:0000269|PubMed:10224275, ECO:0000269|PubMed:16623893, ECO:0000269|PubMed:22167058, ECO:0000269|PubMed:22167059, ECO:0000269|PubMed:22899078, ECO:0000269|PubMed:23345424}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48538
|
RBOHF_ARATH
|
MKPFSKNDRRRWSFDSVSAGKTAVGSASTSPGTEYSINGDQEFVEVTIDLQDDDTIVLRSVEPATAINVIGDISDDNTGIMTPVSISRSPTMKRTSSNRFRQFSQELKAEAVAKAKQLSQELKRFSWSRSFSGNLTTTSTAANQSGGAGGGLVNSALEARALRKQRAQLDRTRSSAQRALRGLRFISNKQKNVDGWNDVQSNFEKFEKNGYIYRSDFAQCIGMKDSKEFALELFDALSRRRRLKVEKINHDELYEYWSQINDESFDSRLQIFFDIVDKNEDGRITEEEVKEIIMLSASANKLSRLKEQAEEYAALIMEELDPERLGYIELWQLETLLLQKDTYLNYSQALSYTSQALSQNLQGLRGKSRIHRMSSDFVYIMQENWKRIWVLSLWIMIMIGLFLWKFFQYKQKDAFHVMGYCLLTAKGAAETLKFNMALILFPVCRNTITWLRSTRLSYFVPFDDNINFHKTIAGAIVVAVILHIGDHLACDFPRIVRATEYDYNRYLFHYFQTKQPTYFDLVKGPEGITGILMVILMIISFTLATRWFRRNLVKLPKPFDRLTGFNAFWYSHHLFVIVYILLILHGIFLYFAKPWYVRTTWMYLAVPVLLYGGERTLRYFRSGSYSVRLLKVAIYPGNVLTLQMSKPTQFRYKSGQYMFVQCPAVSPFEWHPFSITSAPEDDYISIHIRQLGDWTQELKRVFSEVCEPPVGGKSGLLRADETTKKSLPKLLIDGPYGAPAQDYRKYDVLLLVGLGIGATPFISILKDLLNNIVKMEEHADSISDFSRSSEYSTGSNGDTPRRKRILKTTNAYFYWVTREQGSFDWFKGVMNEVAELDQRGVIEMHNYLTSVYEEGDARSALITMVQALNHAKNGVDIVSGTRVRTHFARPNWKKVLTKLSSKHCNARIGVFYCGVPVLGKELSKLCNTFNQKGSTKFEFHKEHF
|
1.11.1.-; 1.6.3.-
| null |
abscisic acid-activated signaling pathway [GO:0009738]; carbohydrate homeostasis [GO:0033500]; defense response by callose deposition [GO:0052542]; ethylene-activated signaling pathway [GO:0009873]; hydrogen peroxide biosynthetic process [GO:0050665]; negative regulation of programmed cell death [GO:0043069]; osmosensory signaling pathway [GO:0007231]; regulation of stomatal movement [GO:0010119]; respiratory burst involved in defense response [GO:0002679]; response to ethylene [GO:0009723]
|
plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; NAD(P)H oxidase H2O2-forming activity [GO:0016174]; peroxidase activity [GO:0004601]
|
PF08022;PF01794;PF08030;PF08414;
|
1.10.238.10;3.40.50.80;2.40.30.10;
|
RBOH (TC 5.B.1.3) family
|
PTM: Not glycosylated. Phosphorylated by CIPK26. {ECO:0000269|PubMed:23335733}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23335733, ECO:0000269|PubMed:9490748}; Multi-pass membrane protein {ECO:0000269|PubMed:23335733, ECO:0000269|PubMed:9490748}.
| null | null | null | null | null |
FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide. Generates reactive oxygen species (ROS) during incompatible interactions with pathogens and is important in the regulation of the hypersensitive response (HR). Involved in abscisic acid-induced stomatal closing and in UV-B and abscisic acid ROS-dependent signaling. {ECO:0000269|PubMed:11756663, ECO:0000269|PubMed:12773379, ECO:0000269|PubMed:16428598, ECO:0000269|PubMed:16913867, ECO:0000269|PubMed:16961732}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48573
|
LAZ5_ARATH
|
MAASSEILPESWQVFINFRGADLRNGFISHLAGALTSAGITYYIDTEEVPSEDLTVLFKRIEESEIALSIFSSNYAESKWCLDELVKIMEQVKKGKLRIMPVFFNVKPEEVREQNGEFGLKLYGEGKSKRPNIPNWENALRSVPSKIGLNLANFRNEKELLDKIIDSIKKVLARITRASRVAESLNGISKDSEAKNVDTFSPNSSDFPSTSIDDDLSINSPQYQATIPPASREGERLNTISTVSSTGSIEHPPPNYGIEPRLKEMEEKLDFDSLETKTVGIVGMPGIGKTTLAETLYRKWEHKFERSMFFPDASKMANEHGMCWLQKRLLEELLKDTNLNIGYTTNEHEFCKDVLLLKKVFLVIDNVSSEEQIETLFGKWNWIKNGSKIVITSSDESMLKGFVKDTYVVPSLNSRDSLLWFTNHAFGLDDAQGNLVKLSKHFLNYAKGNPLALGAFGVELCGKDKADWEKRIKTLTLISNKMIQDVLRRRYDELTERQKDIFLDVACFFKSENESYVRHVVNSCDSESTKSWDEITDLKGKFLVNISGGRVEMHDILCTFAKELASQALTEDTRVHLRLWNYQDIMWFLNNELEMENVRGIFLDMSKVPEEMTFDGNIFSNMCNLRYLKIYSSVCHKEGEGIFKFDTVREIQLPLDKVRYLHWMKYPWEKLPSDFNPENLVDLELPYSSIKKVWEGVKDTPILKWANLSYSSKLTNLLGLSNAKNLERLNLEGCTSLLKLPQEMENMKSLVFLNMRRCTSLTCLQSIKVSSLKILILSDCSKLEEFEVISENLEELYLDGTAIKGLPPAAGDLTRLVVLNMEGCTELESLPKRLGKQKALQELVLSGCSKLESVPTDVKDMKHLRLLLLDGTRIRKIPKIKSLKCLCLSRNIAMVNLQDNLKDFSNLKCLVMKNCENLRYLPSLPKCLEYLNVYGCERLESVENPLVADRLTLFLDRSEELRSTFLFTNCHNLFQDAKDSISTYAKWKCHRLAVECYEQDIVSGAFFNTCYPGYIVPSWFDHQAVGSVLEPRLEPHWYNTMLSGIALCAVVSFHENQDPIIGSFSVKCTLQFENEDGSLRFDCDIGCLNEPGMIEADHVFIGYVTCSRLKDHHSIPIHHPTTVKMQFHLTDACKSKVVDCGFRLMYTQSRGCLLEEEVNANFTKLYLGLL
|
3.2.2.6
| null |
defense response to virus [GO:0051607]; plant-type hypersensitive response [GO:0009626]; response to virus [GO:0009615]; signal transduction [GO:0007165]
| null |
ADP binding [GO:0043531]; ATP binding [GO:0005524]; NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]
|
PF20160;PF07725;PF00931;PF01582;
|
1.10.8.430;3.40.50.300;3.80.10.10;3.40.50.10140;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU00204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
| null | null | null | null |
FUNCTION: TIR-NB-LRR receptor-like protein that may play a role in plant innate immunity. May trigger hypersensitive programmed cell death in response to pathogen attack (PubMed:20949080). Involved in tolerance to tobacco ringspot virus (TRSV) (PubMed:22057987). {ECO:0000269|PubMed:20949080, ECO:0000269|PubMed:22057987}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48593
|
SYNO_ARATH
|
MAATFLPATSLRLTQNSTLRFLSFFTISNPSYSLFRPLRRRVLPPFDAFPANSRRRCFCTAVSESLGSGDGNKVESYEKRFGSKVGEFRKKLRIAEVKGGADEGLSRVGQSLNIMGWVRTLRSQSSVTFIEINDGSCLSNLQCVMTSDAEGYDQVESGSILTGASVSVQGTIVASQGTKQKVELKVEKIIVVGECDSSYPIQKKRVSREFLRTKAHLRPRTNTFGAVARVRNTLAYATHKFFQESGFVWVASPIITASDCEGAGEQFCVTTLIPSSHENTDTSIDAIPKTKGGLIDWSQDFFGKPAFLTVSGQLNGETYATALSDVYTFGPTFRAENSNTSRHLAEFWMIEPELAFADLDDDMACATAYLQYVVKYVLDNCKEDMEFFDTWIEKGIIRRLSDVAEKEFLQLGYTDAIEILLKANKKFDFPVKWGLDLQSEHERYITEEAFGGRPVIIRDYPKEIKAFYMRENDDGKTVAAMDMLVPRIGELIGGSQREERLEVLEARLDELKLNKESYWWYLDLRRYGSVPHAGFGLGFERLVQFVTGIDNIRDVIPFPRTPASAEF
|
6.1.1.22
| null |
asparaginyl-tRNA aminoacylation [GO:0006421]; plant ovule development [GO:0048481]
|
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; mitochondrion [GO:0005739]
|
asparagine-tRNA ligase activity [GO:0004816]; ATP binding [GO:0005524]; DNA binding [GO:0003677]
|
PF00152;PF01336;
|
2.40.50.140;
|
Class-II aminoacyl-tRNA synthetase family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:10824085}. Mitochondrion {ECO:0000269|PubMed:10824085}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659, Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442, ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22; Evidence={ECO:0000305};
| null | null | null | null | null |
Arabidopsis thaliana (Mouse-ear cress)
|
O48626
|
ZW10_ARATH
|
MPEIDALFESINVRDLLAGHDLNDPTTPLSAPDLRLLINRLESHSLRIKSKVQSYLVAHHSDFSELFSLCQDTVSRTRLISDDVSDVLQLVSDRPIDVEIRSVVDEITEKTKEVKLKRESLDLVNAIVGICEALQETKEALKNGRFRFAAERIRELKVVLRIGEEEDGEPVAYALLRKEWSNCFDEIQEVLAKFMENAVRFELDSSRIRIKYQLSVGETAGIALSTVLEAMEVIGILDYGLAKAADSIFKHVITPAVTHASTFAAVEDLCKSAGEVTEATLRLEQSSDHKFEDVDGDAMYSGILKVVKFICSSLCFGNVTWIHSFGRLTWPRISELIISKFLSKVVPEDASKLADFQKIIERTSQFEAALKELNFVSSSDAESRLSKYAEDVEVHFASRKKIEILAKARNLLLQCNFTIPQDIAMRNAKHIVCLLFSSERCVVSEAASQLMNLVHKTLEDVCVSSARVASEFYNAARDSILLYEAVVPVKLEKQLDGLNEAAVLLHNDCLYLFEEILGLAFEYRASFPSSIKEYAVFADIAPRFKLMAEEVLQKQVHLVISSLREAIDSADGFQNTHQIKQFKSAEFSIDQVVFSLKNVHMIWEPVLRPKTYKQSMCAVLESVFRRIARDILLLDDMAADETFELQKLIYLMLKNLSSVLDSVRSADETSRPLDDIIPSLRKTRKLAELLDMPLMSITSAWESGELFRCNFTRTEVQDFIKAIFTDSPLRKECLWRIDEVNQ
| null | null |
cell division [GO:0051301]; chromosome segregation [GO:0007059]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; mitotic spindle assembly checkpoint signaling [GO:0007094]; protein exit from endoplasmic reticulum [GO:0032527]; protein transport [GO:0015031]
|
endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; RZZ complex [GO:1990423]; spindle [GO:0005819]
| null |
PF20666;PF20665;PF06248;
|
1.10.357.150;
|
ZW10 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Cytoplasm. Chromosome, centromere. Chromosome, centromere, kinetochore. Endoplasmic reticulum membrane; Peripheral membrane protein {ECO:0000269|PubMed:24118572}. Note=In prometaphase, associated with the kinetochore. At metaphase, mostly associated with the spindle. In early anaphase, found in the vicinity of the centromere. As anaphase progresses, dispersed in the cytoplasm.
| null | null | null | null | null |
FUNCTION: May be required for accurate chromosome segregation. Required for proper maturation of seed storage proteins. Forms a complex with MAG2, MIP2 and MIP3 on the endoplasmic reticulum that may be responsible for efficient transport of seed storage proteins. {ECO:0000269|PubMed:24118572, ECO:0000305}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48651
|
SQE1_PANGI
|
MNSSSSTTTTDTLHSFMEASALLIDQYFLGWIFAFLFGFLLLLNFKRKREKNNSTEFGTDDSNGYYTPENIAGSTDVIIVGAGVAGSALAYTLANDGRRVHVIERDLTEQDRIVGELLQPGGYLKLIELGLEDCVNEIDAQRVFGYALYMDGKNTRLSYPLEKFHSDVAGRSFHNGRFVQRMREKAASLPNVRMEQGTVTSLVEKKGSVKGVQYKTKDGQELSAFAPLTIVCDGCFSNLRRSLCNPKVEVPSCFVGLILENIDLPHINHGHVILADPSPILFYKISSTEIRCLVDVPGQKVPCISNGELANYLKTVVAPQVPKQLYNSFIAAVDKGNIRTMPNRSMPADPHPTPGALLLGDAFNMRHPLTGGGMTVALSDIVLIRDLLRPLRDLHDSSTLCKYLESFYTLRKPVASTINTLAGALYKVFCASPDKARQEMRNACFDYLSLGGICSQGPIALLSGLNPRPISLFLHFFAVAIYGVGRLLIPFPSPKRMWLGARLILGASGIIFPIIKSEGLRQMFFPAIVPAYYRAPPIH
|
1.14.14.17
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q14534};
|
response to ethylene [GO:0009723]; response to hydrogen peroxide [GO:0042542]; response to jasmonic acid [GO:0009753]; response to metal ion [GO:0010038]; response to molecule of fungal origin [GO:0002238]; response to nitric oxide [GO:0071731]; response to salicylic acid [GO:0009751]; response to vanadate(3-) [GO:1902438]; sterol biosynthetic process [GO:0016126]; terpene biosynthetic process [GO:0046246]
|
endoplasmic reticulum membrane [GO:0005789]
|
flavin adenine dinucleotide binding [GO:0050660]; squalene monooxygenase activity [GO:0004506]
|
PF01266;PF08491;
|
3.50.50.60;
|
Squalene monooxygenase family
| null |
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:P32476}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P32476}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P32476}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P32476}.
|
CATALYTIC ACTIVITY: Reaction=O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:25282, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15440, ChEBI:CHEBI:15441, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.17; Evidence={ECO:0000250|UniProtKB:Q9SM02}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25283; Evidence={ECO:0000303|PubMed:29509695};
| null |
PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 2/3.
| null | null |
FUNCTION: Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:19857882, PubMed:27746309, PubMed:29378087). Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway (By similarity). {ECO:0000250|UniProtKB:Q9SM02, ECO:0000269|PubMed:19857882, ECO:0000269|PubMed:27746309, ECO:0000303|PubMed:29378087}.
|
Panax ginseng (Korean ginseng)
|
O48652
|
UVR3_ARATH
|
MQRFCVCSPSSYRLNPITSMATGSGSLIWFRKGLRVHDNPALEYASKGSEFMYPVFVIDPHYMESDPSAFSPGSSRAGVNRIRFLLESLKDLDSSLKKLGSRLLVFKGEPGEVLVRCLQEWKVKRLCFEYDTDPYYQALDVKVKDYASSTGVEVFSPVSHTLFNPAHIIEKNGGKPPLSYQSFLKVAGEPSCAKSELVMSYSSLPPIGDIGNLGISEVPSLEELGYKDDEQADWTPFRGGESEALKRLTKSISDKAWVANFEKPKGDPSAFLKPATTVMSPYLKFGCLSSRYFYQCLQNIYKDVKKHTSPPVSLLGQLLWREFFYTTAFGTPNFDKMKGNRICKQIPWNEDHAMLAAWRDGKTGYPWIDAIMVQLLKWGWMHHLARHCVACFLTRGDLFIHWEQGRDVFERLLIDSDWAINNGNWMWLSCSSFFYQFNRIYSPISFGKKYDPDGKYIRHFLPVLKDMPKQYIYEPWTAPLSVQTKANCIVGKDYPKPMVLHDSASKECKRKMGEAYALNKKMDGKVDEENLRDLRRKLQKDEHEESKIRNQRPKLK
|
4.1.99.13
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:9421527}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:9421527};
|
circadian regulation of gene expression [GO:0032922]; entrainment of circadian clock by photoperiod [GO:0043153]; pyrimidine dimer repair [GO:0006290]; response to UV [GO:0009411]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
deoxyribodipyrimidine photo-lyase activity [GO:0003904]; DNA (6-4) photolyase activity [GO:0003914]; DNA binding [GO:0003677]; FAD binding [GO:0071949]
|
PF00875;PF03441;
|
1.25.40.80;1.10.579.10;3.40.50.620;
|
DNA photolyase class-1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=(6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA).; EC=4.1.99.13;
| null | null | null | null |
FUNCTION: Involved in repair of UV radiation-induced DNA damage. Catalyzes the photoreactivation of pyrimidine [6-4] pyrimidone photoproduct (6-4 products). Binds specifically to DNA containing 6-4 products and repairs these lesions in a visible light-dependent manner. Not required for repair of cyclobutane pyrimidine dimer (CPD). {ECO:0000269|PubMed:17164245, ECO:0000269|PubMed:9421527}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48653
|
DPOLA_ORYSJ
|
MDEGSADAGASGRRSRARGSEAVARSAALERLRAIRDGGARAAAAVQVRIEAPIYDTVAEEDYAALVARRRKDAGAFIVDDDGLGYADDGREEDWTHRTIHSSSDEGSDGEDGAPRKRKQPRPQSKRPPQQSAAAASLSAAAAMMGKQRLSSMFTSSVFRKPGSDRGRDSSLAADSIVDDVIAEFAPDDNDREERRRRVGRVCAPAPAPTTTAHIKAENVAVDTAMAFRSDNVFEAHEVSDHGNDMDMELKPDVEMEPKLDTPLGASAELANNSNSLEEPKQEANGEVKIEKVHRLNAKIKTEDSRNGDMASATAGWMKICGDGDNAGGEGAVAANSNTGVDESSEFELKDGALPFYILDAYEEPFGANSGTVYLFGKVEVGKRFHSCCVVVKNMQRCIYAIPSSSIFPRDTISRLEKNSTTSDSSPSLRASLHELASGLKSEIADKLSDFNVSNFAMTPVKRNYAFERTDLPNGEQYVLKINYPYKDPALPTDLRGQHFHALLGTNNSALELLLIKRKIKGPSWLSISKFLACPATQRVSWCKFEVTVDSPKDISVLMTSTTLEVPPVVVAAVNLKTIINEKHNVHEIVSASVICCHRVKIDSPMRSEDWQKRGMLSHFTVMRKLEGSIFPIGLSKESSDRNQKAGSNVLALESSERALLNRLMIELSKLDCDVLVGHNISGFDLDVLLHRAQTCKVPSNMWSKIGRLRRSVMPRLTKGNTLYGSGASPGIMSCIAGRLLCDTYLCSRDLLKEVSYSLTQLAETQLKKERKEVSPHDIPPMFQSSGALLKLVEYGETDACLALELMFHLSVLPLTRQLTNISGNLWGKTLQGSRAQRVEYLLLHAFHARKFIVPDKFARSKEFNSTKRKMNPDTEAARPDEADPSIDDEGHHVDQGKTKKGPSYAGGLVLEPKKGLYDKYVLLLDFNSLYPSIIQEYNICFTTVDRSADGNVPNLPASKTTGVLPELLKSLVERRRMVKSWLKTASGLKRQQFDIQQQALKLTANSMYGCLGFSNSRFYAKPLAELITLQGREILQNTVDLVQNNLNLEVIYGDTDSIMIHTGLDDISRAKGIAGKVIQEVNKKYRCLEIDLDGIYKRMLLLKKKKYAAIKVALDGSLRENIERKGLDMVRRDWSLLSKEIGDFCLNQILSGGSCDDVIESIHSSLVQVQEQMRGGQTELEKYIITKSLTKAPEDYPDAKNQPHVQVALRLKQNGYSGCSAGDTVPYIICSQQDSESTHSGGIAQRARHPEELKRNPDKWMIDIDYYLSQQIHPVVSRLCASIQGTSPARLAECLGLDSSKFQSRLTESDNQDTSSMLLSVIDDEDERYRGCEPLRLSCPSCSTTFDCPPVSSLIIGSSSGNVSNPNEGNDASINFWRRMRCPRCPDDTDESRVSPAVLANQMKRQADSFINLYYKGLLMCDDEGCKYSTHSVNLRVMGDSERGTICPNYPRCNGHLVRQYTEADLYRQLSYFCYVVDATRCLEKLDQKARLPFEKEFAALSQTINLALMEVQKIRDRCAFGWVQLKDLAISI
|
2.7.7.7
| null |
DNA replication initiation [GO:0006270]; lagging strand elongation [GO:0006273]; leading strand elongation [GO:0006272]; leaf morphogenesis [GO:0009965]; mitotic DNA replication initiation [GO:1902975]
|
alpha DNA polymerase:primase complex [GO:0005658]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA primase activity [GO:0003896]; DNA replication origin binding [GO:0003688]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; single-stranded DNA binding [GO:0003697]
|
PF12254;PF00136;PF03104;PF08996;
|
2.40.50.730;3.30.70.2820;1.10.3200.20;1.10.132.60;1.10.287.690;3.90.1600.10;3.30.420.10;
|
DNA polymerase type-B family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7;
| null | null | null | null |
FUNCTION: Polymerase alpha in a complex with DNA primase is a replicative polymerase.
|
Oryza sativa subsp. japonica (Rice)
|
O48666
|
SQS1_PANGI
|
MGSLGAILKHPEDFYPLLKLKFAARHAEKQIPPEPHWAFCYSMLHKVSRSFGLVIQQLGPQLRDAVCIFYLVLRALDTVEDDTSIPTEVKVPILMAFHRHIYDKDWHFSCGTKEYKVLMDEFHHVSNAFLELGSGYQEAIEDITMRMGAGMAKFICKEVETINDYDEYCHYVAGLVGLGLSKLFHASGAEDLATDSLSNSMGLFLQKTNIIRDYLEDINEIPKSRMFWPRQIWSKYVDKLEDLKYEENSAKAVQCLNDMVTDALVHAEDCLKYMSDLRGPAIFRFCAIPQIMAIGTLALCFNNTQVFRGVVKMRRGLTAKVIDQTKTMSDVYGAFFDFSCLLKSKVDNNDPNATKTLSRLEAIQKTCKESGTLSKRKSYIIESESGHNSALIAIIFIILAILYAYLSSNLLLNKQ
|
2.5.1.21
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P53799}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P53799};
|
cholesterol biosynthetic process [GO:0006695]; ergosterol biosynthetic process [GO:0006696]; farnesyl diphosphate metabolic process [GO:0045338]; response to ethylene [GO:0009723]; response to hydrogen peroxide [GO:0042542]; response to jasmonic acid [GO:0009753]; response to molecule of fungal origin [GO:0002238]; response to nitric oxide [GO:0071731]; response to salicylic acid [GO:0009751]; response to vanadate(3-) [GO:1902438]; saponin biosynthetic process [GO:0016135]; triterpenoid biosynthetic process [GO:0016104]
|
endoplasmic reticulum membrane [GO:0005789]
|
farnesyl-diphosphate farnesyltransferase activity [GO:0004310]; farnesyltranstransferase activity [GO:0004311]; squalene synthase activity [GO:0051996]
|
PF00494;
|
1.10.600.10;
|
Phytoene/squalene synthase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P53799}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene; Xref=Rhea:RHEA:32299, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; EC=2.5.1.21; Evidence={ECO:0000250|UniProtKB:P53799}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32300; Evidence={ECO:0000303|PubMed:29509695}; CATALYTIC ACTIVITY: Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 diphosphate + NADP(+) + squalene; Xref=Rhea:RHEA:32295, ChEBI:CHEBI:15378, ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:175763; EC=2.5.1.21; Evidence={ECO:0000250|UniProtKB:P53799}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32296; Evidence={ECO:0000303|PubMed:29509695};
| null |
PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3. {ECO:0000250|UniProtKB:P53799}.
| null | null |
FUNCTION: Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:15356323, PubMed:27746309, PubMed:29378087). Catalyzes the biosynthesis of squalene (PubMed:15356323). {ECO:0000269|PubMed:15356323, ECO:0000269|PubMed:27746309, ECO:0000303|PubMed:29378087}.
|
Panax ginseng (Korean ginseng)
|
O48676
|
U74B1_ARATH
|
MAETTPKVKGHVVILPYPVQGHLNPMVQFAKRLVSKNVKVTIATTTYTASSITTPSLSVEPISDGFDFIPIGIPGFSVDTYSESFKLNGSETLTLLIEKFKSTDSPIDCLIYDSFLPWGLEVARSMELSAASFFTNNLTVCSVLRKFSNGDFPLPADPNSAPFRIRGLPSLSYDELPSFVGRHWLTHPEHGRVLLNQFPNHENADWLFVNGFEGLEETQDCENGESDAMKATLIGPMIPSAYLDDRMEDDKDYGASLLKPISKECMEWLETKQAQSVAFVSFGSFGILFEKQLAEVAIALQESDLNFLWVIKEAHIAKLPEGFVESTKDRALLVSWCNQLEVLAHESIGCFLTHCGWNSTLEGLSLGVPMVGVPQWSDQMNDAKFVEEVWKVGYRAKEEAGEVIVKSEELVRCLKGVMEGESSVKIRESSKKWKDLAVKAMSEGGSSDRSINEFIESLGK
|
2.4.1.195
| null |
defense response by callose deposition in cell wall [GO:0052544]; defense response to bacterium [GO:0042742]; glucosinolate biosynthetic process [GO:0019761]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
quercetin 3-O-glucosyltransferase activity [GO:0080043]; quercetin 7-O-glucosyltransferase activity [GO:0080044]; thiohydroximate beta-D-glucosyltransferase activity [GO:0047251]; UDP-glucose: 4-methylthiobutylhydroximate S-glucosyltransferase activity [GO:0102659]; UDP-glucose: 6-methylthiohexylhydroximate S-glucosyltransferase activity [GO:0103100]; UDP-glucose: 9-methylthiononylhydroximate S-glucosyltransferase activity [GO:0103103]; UDP-glucose:5-methylthiopentylhydroximate S-glucosyltransferase activity [GO:0103099]; UDP-glucose:7-methylthioheptylhydroximate S-glucosyltransferase activity [GO:0103101]; UDP-glucose:8-methylthiooctylhydroximate S-glucosyltransferase activity [GO:0103102]
|
PF00201;
|
3.40.50.2000;
|
UDP-glycosyltransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=(Z)-2-phenyl-1-thioacetohydroximate + UDP-alpha-D-glucose = (Z)-desulfoglucotropeolin + UDP; Xref=Rhea:RHEA:13757, ChEBI:CHEBI:58176, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:136422; EC=2.4.1.195; Evidence={ECO:0000269|PubMed:15584955}; CATALYTIC ACTIVITY: Reaction=a (Z)-omega-(methylsulfanyl)alkyl-thiohydroximate + UDP-alpha-D-glucose = an aliphatic (Z)-desulfo-glucosinolate + UDP; Xref=Rhea:RHEA:52148, Rhea:RHEA-COMP:17746, Rhea:RHEA-COMP:18240, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:187900, ChEBI:CHEBI:192830; EC=2.4.1.195; Evidence={ECO:0000269|PubMed:15584955}; CATALYTIC ACTIVITY: Reaction=(Z)-2-(indol-3-yl)-1-thioacetohydroximate + UDP-alpha-D-glucose = (Z)-indolylmethyl desulfoglucosinolate + UDP; Xref=Rhea:RHEA:52152, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:136527, ChEBI:CHEBI:187899; EC=2.4.1.195; Evidence={ECO:0000269|PubMed:15584955};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.8 uM for PATH {ECO:0000269|PubMed:15584955}; KM=48 uM for UDP-glucose {ECO:0000269|PubMed:15584955};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. Stable between pH 5-9. {ECO:0000269|PubMed:15584955};
| null |
FUNCTION: Involved in the biosynthesis of glucosinolate. In in vitro assay, may use phenylacetothiohydroximate (PATH), but not phenylacetic acid (PAA), indole-3-acetic acid (IAA) or salicylic acid (SA) as substrate. Specific for the thiohydroximate functional group and does not glucosylate the carboxylate group or a hydroxyl group. {ECO:0000269|PubMed:15584955}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48709
|
PI5K3_ARATH
|
MQETVFLFTEENLNKEQSLGVKYKQSSRRVVPMTSCEVSDTAAEIRIVEKVLKNGDLYNGGLSAGVPHGTGKYLWSDGCMYEGEWTRGKASGKGRFSWPSGATYEGQFKDGRMDGEGTFIGIDGDTYRGHWLWGRKHGYGEKRYANGDGYQGNWKANLQDGNGRYVWSDGNEYVGEWKNGVISGKGKMTWANGNRYDGLWENGAPVGKGVLSWGEEKTSYNGWGRKSKKKDEEIVQNHKLSSVETLSANTNFPRICISELEDTGVCDHVEASPYTSESDTSGCGEQEWARSPLLLESGGAMSVQQSPRWLDEGDVKKPGHTVTAGHKNYDLMLNLQLGIRYSVGKHASLLRELRHSDFDPKDKQWTRFPPEGSKSTPPHLSAEFKWKDYCPIVFRHLRDLFAIDQADYMLAICGNESLREFASPGKSGSAFYLTQDERYMIKTMKKSEIKVLLKMLPNYYEHVSKYKNSLVTKFFGVHCVKPVGGQKTRFIVMGNLFCSEYRIHKRFDLKGSSHGRTIDKDEGEIDETTTLKDLDLKYVFRLETSWFQAFINQIDLDCEFLEAERIMDYSLLIGLHFRESGMRDDISLGIGRRDQEDKLMRGNGPLMRLGESTPAKAEQVSRFEEETWEEDAIDNSNPKGTRKEAVEVILYFGVIDILQDYDITKKLEHAYKSLHADPASISAVDPKLYSRRFRDFINKIFIEDK
|
2.7.1.68
| null |
phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310]; regulation of establishment of cell polarity [GO:2000114]; root hair cell tip growth [GO:0048768]; root hair elongation [GO:0048767]; root hair initiation [GO:0048766]
|
apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; ATP binding [GO:0005524]
|
PF02493;PF01504;
|
3.30.810.10;2.20.110.10;3.30.800.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27251533}. Note=Accumulates in a sterol-enriched, polar membrane domain during root hair initiation. {ECO:0000269|PubMed:27251533}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68; Evidence={ECO:0000250|UniProtKB:Q99755};
| null | null | null | null |
FUNCTION: With DRP1A and DRP2B, required for the precise coordination of polar ARAC3/ROP6 and ARAC4/ROP2 placement and subsequent root hair positioning during planar polarity formation in root hair-forming cells, probably by mediating the correct basal-to-planar polarity switching of D6PK into the polar, lipid-enriched domain. {ECO:0000269|PubMed:27251533}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48711
|
PME12_ARATH
|
MALSSFNLSSLLFLLFFTPSVFSYSYQPSLNPHETSATSFCKNTPYPDACFTSLKLSISINISPNILSFLLQTLQTALSEAGKLTDLLSGAGVSNNLVEGQRGSLQDCKDLHHITSSFLKRSISKIQDGVNDSRKLADARAYLSAALTNKITCLEGLESASGPLKPKLVTSFTTTYKHISNSLSALPKQRRTTNPKTGGNTKNRRLLGLFPDWVYKKDHRFLEDSSDGYDEYDPSESLVVAADGTGNFSTINEAISFAPNMSNDRVLIYVKEGVYDENIDIPIYKTNIVLIGDGSDVTFITGNRSVGDGWTTFRSATLAVSGEGFLARDIMITNTAGPEKHQAVALRVNADFVALYRCVIDGYQDTLYTHSFRQFYRECDIYGTIDYIFGNAAVVFQGCNIVSKLPMPGQFTVITAQSRDTQDEDTGISMQNCSILASEDLFNSSNKVKSYLGRPWREFSRTVVMESYIDEFIDGSGWSKWNGGEALDTLYYGEYNNNGPGSETVKRVNWPGFHIMGYEDAFNFTATEFITGDGWLGSTSFPYDNGI
|
3.1.1.11
| null |
cell wall modification [GO:0042545]; pectin catabolic process [GO:0045490]; response to bacterium [GO:0009617]
|
extracellular region [GO:0005576]
|
aspartyl esterase activity [GO:0045330]; pectinesterase activity [GO:0030599]; pectinesterase inhibitor activity [GO:0046910]
|
PF01095;PF04043;
|
1.20.140.40;2.160.20.10;
|
PMEI family; Pectinesterase family
| null |
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol; Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
| null |
PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
| null | null |
FUNCTION: Acts in the modification of cell walls via demethylesterification of cell wall pectin. {ECO:0000250}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48723
|
PLP2_ARATH
|
MQMDSPKSPLQPPTYGNLVTILSIDGGGIRGLIPAVILGFLESELQKLDGEEARLADYFDVIAGTSTGGLVTAMLTAPNKEGRPLFAASEIKDFYLEQCPKIFPQDHFPFSAAKKLVKSLTGPKYDGKYLHQLIHAKLGDTKLSQTLTNVVIPTFDIKHLQPTIFSSYEVKNHPLKDATLADIAISTSAAPTYLPAHFFKVEDLNGNAKEYNLIDGGVAANNPALLAIGEVTNEISGGSSDFFPIRPNDYGRFLVLSLGTGNHKAEEKFNAKEVAGWGLLNWLTHDNSTPIIDAFSQASSDMVDFHLSAVFRALHSEANYIRIQDDTLTGDAASVDIATVENLDILAKTGDELLKKPVARVNLDSGCNENAYETTNEHALIKLAGILSKEKKIRDIRSPHAKAPIRI
|
3.1.1.-
| null |
cellular response to hypoxia [GO:0071456]; D-xylose catabolic process [GO:0042843]; defense response to virus [GO:0051607]; lipid catabolic process [GO:0016042]; lipid metabolic process [GO:0006629]; oxylipin biosynthetic process [GO:0031408]; plant-type hypersensitive response [GO:0009626]; response to cadmium ion [GO:0046686]
|
cytoplasm [GO:0005737]; membrane [GO:0016020]; peroxisome [GO:0005777]
|
acylglycerol lipase activity [GO:0047372]; identical protein binding [GO:0042802]; lipase activity [GO:0016298]; phospholipase activity [GO:0004620]; xylose isomerase activity [GO:0009045]
|
PF01734;
|
3.40.1090.10;
|
Patatin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12226489, ECO:0000269|PubMed:16297072}.
| null | null | null | null | null |
FUNCTION: Possesses non-specific lipolytic acyl hydrolase (LAH) activity. Catalyzes the hydrolysis of the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), and less efficiently the phoshpolipids phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylglycerol (PG), phosphatidic acid (PA), phosphatidylserine (PS) and phosphatidylinositol (PI). Favors the release of fatty acid at the sn-1 position for PC or PE and the sn-2 position for PG, PA, PS and PI. Negatively affects disease resistance to the necrotic fungal pathogen Botrytis cinerea and the avirulent bacteria Pseudomonas syringae by promoting cell death and reducing the efficiency of the hypersensitive response, respectively. However, PLP2 contributes to resistance to cucumber mosaic virus (CMV), an obligate parasite inducing hypersensitive response. May negatively regulate oxylipin production, possibly via participating in membrane repair that includes removal of oxidatively modified lipids. {ECO:0000269|PubMed:16297072, ECO:0000269|PubMed:19271961, ECO:0000269|PubMed:22259021}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48726
|
RPN13_ARATH
|
MSSSEAFPVMQEIMLEFRAGKMSLQGTRVVPDARKGLVRIARGDEGLIHFQWLDRNQNTVEDDQIVFPDEALFEKVNQSSDRVYILKFNSDDRKLFFWMQEPRAEGDAELCSSVNQYLNQPLEFPGEEGLAAAITEELEDMAEDNTSSRAGNLVVPNLSSEVSDVTSSSGPVKLADLQRILNNLSGGPVGIAGDQDEGLALGDILKPELIMPLLEALPVQERLSSHLPEGHSRAEDILELLQSPPFRQQVDAFTYVLRTGQIDLTQFGIDPSKYKFTVDSFLEALEDSVSTQSRDAMDES
| null | null | null |
cytoplasm [GO:0005737]; nucleus [GO:0005634]; proteasome regulatory particle, lid subcomplex [GO:0008541]
|
endopeptidase activator activity [GO:0061133]; proteasome binding [GO:0070628]
|
PF04683;PF16550;
|
1.10.2020.20;2.30.29.70;
|
RPN13 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU01265}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU01265}.
| null | null | null | null | null |
FUNCTION: Functions as a proteasomal ubiquitin receptor. Binds and presumably selects ubiquitin-conjugates for destruction. Prefers multiubiquitin chains rather than single ubiquitins, with a binding affinity for 'Lys-63'-linked ubiquitin chains. {ECO:0000269|PubMed:21764993, ECO:0000269|PubMed:22751321}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48737
|
TRXM1_ARATH
|
MAAYTCTSRPPISIRSEMRIASSPTGSFSTRQMFSVLPESSGLRTRVSLSSLSKNSRVSRLRRGVICEAQDTATGIPVVNDSTWDSLVLKADEPVFVDFWAPWCGPCKMIDPIVNELAQKYAGQFKFYKLNTDESPATPGQYGVRSIPTIMIFVNGEKKDTIIGAVSKDTLATSINKFL
| null | null |
negative regulation of catalytic activity [GO:0043086]; positive regulation of catalytic activity [GO:0043085]; regulation of carbohydrate metabolic process [GO:0006109]; response to cold [GO:0009409]
|
apoplast [GO:0048046]; chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; extracellular region [GO:0005576]; stromule [GO:0010319]; thylakoid [GO:0009579]
|
enzyme activator activity [GO:0008047]; enzyme inhibitor activity [GO:0004857]; protein-disulfide reductase activity [GO:0015035]; salicylic acid binding [GO:1901149]
|
PF00085;
|
3.40.30.10;
|
Thioredoxin family, Plant M-type subfamily
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:19259774}.
| null | null | null | null | null |
FUNCTION: Thiol-disulfide oxidoreductase involved in the redox regulation of enzymes of both reductive pentose phosphate pathway (Calvin-Benson cycle) and oxidative pentose phosphate pathway. Under reducing conditions, activates the glyceraldehyde-3-phosphate dehydrogenase and the phosphoribulokinase, and inhibits. the glucose-6-phosphate dehydrogenase. Activates NADP-malate dehydrogenase. {ECO:0000269|PubMed:19631646, ECO:0000269|PubMed:19825612}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48741
|
PORC_ARATH
|
MALQAAYSLLPSTISIQKEGKFNASLKETTFTGSSFSNHLRAEKISTLLTIKEQRRQKPRFSTGIRAQTVTATPPANEASPEQKKTERKGTAVITGASSGLGLATAKALADTGKWHVIMACRNFLKAEKAARSVGMSKEDYTVMHLDLASLESVKQFVENFRRTEQPLDVLVCNAAVYQPTAKEPSFTAEGFEISVGTNHLGHFLLSRLLLDDLKKSDYPSKRMIIVGSITGNTNTLAGNVPPKANLGDLRGLASGLNGQNSSMIDGGEFDGAKAYKDSKVCNMLTMQELHRRYHEETGVTFASLYPGCIATTGLFREHIPLFRLLFPPFQKYITKGYVSEEEAGKRLAQVVSDPSLGKSGVYWSWNNNSSSFENQLSKEASDAEKAKKLWEVSEKLVGLA
|
1.3.1.33
| null |
chlorophyll biosynthetic process [GO:0015995]; photosynthesis [GO:0015979]
|
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast membrane [GO:0031969]; chloroplast thylakoid [GO:0009534]; chloroplast thylakoid membrane [GO:0009535]; extracellular region [GO:0005576]
|
NADPH dehydrogenase activity [GO:0003959]; protochlorophyllide reductase activity [GO:0016630]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family, POR subfamily
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000269|PubMed:22212719}. Note=Prolamellar body of etiolated seedling.
|
CATALYTIC ACTIVITY: Reaction=chlorophyllide a + NADP(+) = H(+) + NADPH + protochlorophyllide a; Xref=Rhea:RHEA:11132, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83348, ChEBI:CHEBI:83350; EC=1.3.1.33;
| null |
PATHWAY: Porphyrin-containing compound metabolism; chlorophyll biosynthesis.
| null | null |
FUNCTION: Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide). {ECO:0000269|PubMed:11785941, ECO:0000269|PubMed:12848821}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48773
|
PDI23_ARATH
|
MYKSPLTLLTLLTICFGFFDLSSALYGSSSPVVQLTASNFKSKVLNSNGVVLVEFFAPWCGHCKALTPTWEKVANILKGVATVAAIDADAHQSAAQDYGIKGFPTIKVFVPGKAPIDYQGARDAKSIANFAYKQIKGLLSDRLEGKSKPTGGGSKEKKSEPSASVELNASNFDDLVIESNELWIVEFFAPWCGHCKKLAPEWKRAAKNLQGKVKLGHVNCDVEQSIMSRFKVQGFPTILVFGPDKSSPYPYEGARSASAIESFASELVESSAGPVEVTELTGPDVMEKKCGSAAICFISFLPDILDSKAEGRNKYLEMLLSVAEKFKKQPYSFMWVAAVTQMDLEKRVNVGGYGYPAMVAMNVKKGVYAPLKSAFELQHLLEFVKDAGTGGKGNVPMNGTPEIVKTKEWDGKDGELIEEDEFSLDELMGGDDAVGSKDEL
|
5.3.4.1
| null |
response to endoplasmic reticulum stress [GO:0034976]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; Golgi apparatus [GO:0005794]; plant-type vacuole [GO:0000325]
|
protein disulfide isomerase activity [GO:0003756]; protein-disulfide reductase activity [GO:0015035]
|
PF00085;
|
3.40.30.10;
|
Protein disulfide isomerase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1;
| null | null | null | null |
FUNCTION: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds. {ECO:0000250}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48782
|
HMOX1_ARATH
|
MAYLAPISSSLSIFKNPQLSRFQFSSSSPNPLFLRPRIQILSMTMNKSPSLVVVAATTAAEKQKKRYPGESKGFVEEMRFVAMRLHTKDQAKEGEKETKSIEERPVAKWEPTVEGYLRFLVDSKLVYDTLELIIQDSNFPTYAEFKNTGLERAEKLSTDLEWFKEQGYEIPEPTAPGKTYSQYLKELAEKDPQAFICHFYNIYFAHSAGGRMIGRKVAERILDNKELEFYKWDGELSQLLQNVREKLNKVAEEWTREEKNHCLEETEKSFKYSGEILRLILS
|
1.14.14.18
| null |
carotenoid biosynthetic process [GO:0016117]; cellular response to UV-C [GO:0071494]; chloroplast-nucleus signaling pathway [GO:0010019]; flavonoid biosynthetic process [GO:0009813]; heme oxidation [GO:0006788]; photosynthesis [GO:0015979]; phytochromobilin biosynthetic process [GO:0010024]; regulation of meristem growth [GO:0010075]; regulation of stomatal movement [GO:0010119]
|
chloroplast [GO:0009507]
|
heme binding [GO:0020037]; heme oxygenase (decyclizing) activity [GO:0004392]; metal ion binding [GO:0046872]
|
PF01126;
|
1.20.910.10;
|
Heme oxygenase family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:10072395, ECO:0000269|PubMed:19860740}.
|
CATALYTIC ACTIVITY: Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18; Evidence={ECO:0000269|PubMed:10072395, ECO:0000269|PubMed:12481078};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 uM for hemin {ECO:0000269|PubMed:12481078, ECO:0000269|PubMed:19860740}; KM=1.9 uM for ferredoxin {ECO:0000269|PubMed:12481078, ECO:0000269|PubMed:19860740}; KM=420 uM for ascorbate {ECO:0000269|PubMed:12481078, ECO:0000269|PubMed:19860740};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:12481078, ECO:0000269|PubMed:19860740};
| null |
FUNCTION: Key enzyme in the synthesis of the chromophore of the phytochrome family of plant photoreceptors. Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Can form complex with heme, is ferredoxin-dependent and its activity is increased in the presence of ascorbate. Plays a role in salt acclimation signaling. May affect the plastid-to-nucleus signaling pathway by perturbing tetrapyrrole synthesis. The plastid-to-nucleus signal plays an important role in the coordinated expression of both nuclear- and chloroplast-localized genes that encode photosynthesis-related proteins. {ECO:0000269|PubMed:10072395, ECO:0000269|PubMed:10339624, ECO:0000269|PubMed:11135121, ECO:0000269|PubMed:11172074, ECO:0000269|PubMed:12232145, ECO:0000269|PubMed:12324588, ECO:0000269|PubMed:12481078, ECO:0000269|PubMed:16428602, ECO:0000269|PubMed:19860740, ECO:0000269|PubMed:20979354, ECO:0000269|PubMed:21205037, ECO:0000269|PubMed:7690685}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48791
|
SCAB1_ARATH
|
MTRVTRDFRDSLQRDGVPAVSADVKFASSRFPNYRIGANDQIFDVKDDPKVMSMKEVVARETAQLMDQQKRLSVRDLAHKFEKGLAAAAKLSEEAKLKEATSLEKHVLLKKLRDALESLRGRVAGRNKDDVEEAIAMVEALAVQLTQREGELFIEKAEVKKLASFLKQASEDAKKLVDEERAFARAEIESARAAVQRVEEALREHEQMSRASGKQDMEDLMKEVQEARRIKMLHQPSRVMDMEYELRALRNQLAEKSKHFLQLQKKLAMCRKSEENISLVYEIDGTEALGSCLRVRPCSNDAPDLSKCTIQWYRSSSDGSKKELISGATKSVYAPEPFDVGRVLHADIIYDGHSLSLSTVGKIDPAAGLGSYVEALVRKHDVDFNVVVTQMSGEDHTSESIHLFHVGKMRIKLCKGKTVIAKEYYSSAMQLCGVRGGGNAAAQALYWQAKKGVSFVIAFESERERNAAIMLARRFACDCNVTLAGPEDRTETGQSP
| null | null |
actin filament organization [GO:0007015]; regulation of stomatal movement [GO:0010119]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]
|
actin binding [GO:0003779]
|
PF16711;PF16709;PF17684;PF16712;
|
2.30.29.140;2.60.40.2700;1.20.5.440;
|
SCAB family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21719691}.
| null | null | null | null | null |
FUNCTION: Plant-specific actin binding protein that bundles and stabilizes microfilaments (MFs). Has no nucleation or capping activity. Regulates MF reorganization during stomatal closure. The binding to F-actin is insensitive to Ca(2+) and pH. Binds weakly to inositol phosphates (PubMed:22356912). {ECO:0000269|PubMed:21719691, ECO:0000269|PubMed:22356912}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48802
|
PHOX2_ARATH
|
MGKSGGRKKKSGGSNSNSSQVNSSETSGLSKPSTIVNGGVDFDASIFLKRAHELKEEGNKKFQARDYVGALEQYENGIKLIPKSHPDRAVFHSNRAACLMQMKPIDYESVISECSMALKSQPGFTRALLRRARAFEAVGKFDLAVQDVNVLLGSDPNHKDAGEISKRLKTALGPHQDLQSRPSPAALGASAALGGPIAGLGPCLPSRNVHKKGVTSPVGSVSLPNASNGKVERPQVVNPVTENGGSVSKGQASRVVLKPVSHSPKGSKVEELGSSSVAVVGKVQEKRIRWRPLKFVYDHDIRLGQMPVNCRFKELREIVSSRFPSSKAVLIKYKDNDGDLVTITSTAELKLAESAADCILTKEPDTDKSDSVGMLRLHVVDVSPEQEPMLLEEEEEEVEEKPVIEEVISSPTESLSETEINTEKTDKEVEKEKASSSEDPETKELEMDDWLFDFAHLFRTHVGIDPDAHIDLHELGMELCSEALEETVTSEKAQPLFDKASAKFQEVAALAFFNWGNVHMCAARKRIPLDESAGKEVVAAQLQTAYEWVKERYTLAKEKYEQALSIKPDFYEGLLALGQQQFEMAKLHWSYLLAQKIDISGWDPSETLNLFDSAEAKMKDATEMWEKLEEQRMDDLKNPNSNKKEEVSKRRKKQGGDGNEEVSETITAEEAAEQATAMRSQIHLFWGNMLFERSQVECKIGKDGWNKNLDSAVERFKLAGASEADIATVVKNHCSNEAAATEGDEKKVPAP
| null | null | null |
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
mRNA binding [GO:0003729]
|
PF00564;
|
1.25.40.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22025705}. Note=Localized to distinct foci in the cytoplasm, which frequently colocalize with the cell periphery and with chloroplasts. {ECO:0000269|PubMed:22025705}.
| null | null | null | null | null |
FUNCTION: Required for plastid separation and partitioning during cell division (PubMed:22025705). Not involved in plastid constriction or in the organization of cytoplasmic actin cables (PubMed:22025705). Contributes to polar growth of root hairs (PubMed:28096376). {ECO:0000269|PubMed:22025705, ECO:0000269|PubMed:28096376}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48814
|
BIK1_ARATH
|
MGSCFSSRVKADIFHNGKSSDLYGLSLSSRKSSSTVAAAQKTEGEILSSTPVKSFTFNELKLATRNFRPDSVIGEGGFGCVFKGWLDESTLTPTKPGTGLVIAVKKLNQEGFQGHREWLTEINYLGQLSHPNLVKLIGYCLEDEHRLLVYEFMQKGSLENHLFRRGAYFKPLPWFLRVNVALDAAKGLAFLHSDPVKVIYRDIKASNILLDADYNAKLSDFGLARDGPMGDLSYVSTRVMGTYGYAAPEYMSSGHLNARSDVYSFGVLLLEILSGKRALDHNRPAKEENLVDWARPYLTSKRKVLLIVDNRLDTQYLPEEAVRMASVAVQCLSFEPKSRPTMDQVVRALQQLQDNLGKPSQTNPVKDTKKLGFKTGTTKSSEKRFTQKPFGRHLV
|
2.7.11.1
| null |
defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; innate immune response [GO:0045087]; pattern recognition receptor signaling pathway [GO:0002221]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of defense response to bacterium [GO:1900424]; regulation of jasmonic acid biosynthetic process [GO:0080141]; regulation of salicylic acid biosynthetic process [GO:0080142]; regulation of stomatal movement [GO:0010119]; response to fungus [GO:0009620]; response to molecule of bacterial origin [GO:0002237]
|
cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; endosome [GO:0005768]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; kinase activity [GO:0016301]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF07714;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
|
PTM: Phosphorylated by SIK1 to be stabilized (PubMed:30212650). Phosphorylated by FLS2 and BAK1 (PubMed:20404519, Ref.20). Autophosphorylated (PubMed:22504181, PubMed:23431184, PubMed:24104392, PubMed:26021844). Autophosphorylation is reduced in presence of the Xanthomonas campestris effector XopAC/AvrAC (PubMed:22504181, Ref.20). Phosphorylated, especially by EFR at Ser-89 and Thr-90, in response to the microbe-associated molecular pattern (MAMP) flg22 (PubMed:20413097, PubMed:22504181, PubMed:25522736, PubMed:29649442, Ref.20). Phosphorylation in response to flg22 is abolished in presence of the Xanthomonas campestris effector XopAC/AvrAC (PubMed:22504181). Phosphorylated at Ser-233, Ser-236 and Thr-237 by PEPR1 (PubMed:23431184). Phosphorylated at Tyr-150, Tyr-243 and Tyr-250. Tyrosine phosphorylation is required for BIK1 function in plant innate immunity (PubMed:24532660). {ECO:0000269|PubMed:20404519, ECO:0000269|PubMed:20413097, ECO:0000269|PubMed:22504181, ECO:0000269|PubMed:23431184, ECO:0000269|PubMed:24104392, ECO:0000269|PubMed:24532660, ECO:0000269|PubMed:25522736, ECO:0000269|PubMed:26021844, ECO:0000269|PubMed:29649442, ECO:0000269|PubMed:30212650, ECO:0000269|Ref.20}.; PTM: Uridylylated at Ser-236 and Thr-237 by the Xanthomonas campestris effector XopAC/AvrAC. This conceals conserved phosphorylation sites in the activation loop, reducing BIK1 kinase activity and consequently inhibiting downstream signaling. {ECO:0000269|PubMed:22504181}.; PTM: Monoubiquitinated by ATL44/RHA3A and ATL45/RHA3B following phosphorylation upon the recognition of microbe-associated molecular patterns (MAMPs, e.g. flg22) by pattern recognition receptors (PRRs), then released from the FLS2/BAK1 complex and internalized dynamically into endocytic compartments followed by the activation of immune signaling. {ECO:0000269|Ref.20}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16339855, ECO:0000269|PubMed:26021844, ECO:0000269|PubMed:29649442, ECO:0000269|Ref.20}; Lipid-anchor {ECO:0000269|PubMed:16339855, ECO:0000269|PubMed:26021844}. Endosome membrane {ECO:0000269|Ref.20}; Lipid-anchor {ECO:0000269|PubMed:16339855, ECO:0000269|PubMed:26021844}. Nucleus {ECO:0000269|PubMed:29649442}. Note=Linked to the plasma membrane when inactivated, but moves to the nucleus upon pathogen-mediated activation by phosphorylation (PubMed:29649442). Internalized dynamically into endocytic compartments upon the recognition of microbe-associated molecular patterns (MAMPs, e.g. flg22), when monoubiquitinated after phosphorylation and subsequent dissociation of the FLS2/BIK1 complex (Ref.20). {ECO:0000269|PubMed:29649442, ECO:0000269|Ref.20}.
|
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; Evidence={ECO:0000269|PubMed:24104392}; 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; Evidence={ECO:0000269|PubMed:24104392};
| null | null | null | null |
FUNCTION: Plays a central role in immune responses (PubMed:20413097, PubMed:29649442). Required to activate the resistance responses to necrotrophic pathogens, including the regulation of defense hormone expression (e.g. jasmonic acid (JA) and salicylic acid (SA)) (PubMed:16339855, PubMed:29649442). Phosphorylates FLS2 and BAK1 (PubMed:20404519, PubMed:24104392). Involved in pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) signaling, including calcium signaling, and defense responses downstream of FLS2; upon PAMP recognition, first phosphorylated by FLS2 and SIK1 prior to being monoubiquitinated by ATL44/RHA3A and ATL45/RHA3B at the plasma membrane, then internalized dynamically into endocytic compartments together with FLS2 (PubMed:20413097, PubMed:25522736, PubMed:30212650, Ref.20). Acts additively with PBL1 in PTI defenses (PubMed:20413097). Acts as a positive regulator of the PAMP flg22-induced increase of cytosolic calcium. Binds directly and phosphorylates the NADPH oxidase RBOHD at specific sites in a calcium-independent manner to enhance reactive oxygen species (ROS) generation upon flg22 perception. ROS production in response to flg22 controls stomatal movement and restriction of bacterial entry into leaf tissues (PubMed:24629339). Seems not required for flg22-induced MAPK activation (Probable). Required for Pep1-induced defenses. Pep1 is an endogenous elicitor that potentiates PAMP-inducible plant responses. In association with PEPR1, acts downstream of the canonical ethylene signaling cascade to regulate ethylene responses (PubMed:23431184). Involved in ethylene signaling. Destabilizes EIN3, the key transcription activator in ethylene signaling, and represses EIN3-dependent transcription (PubMed:26021844). Acts as a negative regulator in brassinosteroid (BR) signaling. Functions in BR signaling by direct interaction with the BR receptor BRI1 cytosolic kinase domain (PubMed:23818580). Required during SCOOP small peptides (e.g. SCOOP10 and SCOOP12) perception and signaling; receptor-like cytosolic kinases (RLCK) activated by BAK1/SERK3 and SERK4 coreceptors when associated with MIK2 upon the perception of SCOOP peptides (PubMed:34535661). {ECO:0000269|PubMed:16339855, ECO:0000269|PubMed:20404519, ECO:0000269|PubMed:20413097, ECO:0000269|PubMed:23431184, ECO:0000269|PubMed:23818580, ECO:0000269|PubMed:24104392, ECO:0000269|PubMed:24629339, ECO:0000269|PubMed:25522736, ECO:0000269|PubMed:26021844, ECO:0000269|PubMed:29649442, ECO:0000269|PubMed:30212650, ECO:0000269|PubMed:34535661, ECO:0000269|Ref.20, ECO:0000305, ECO:0000305|PubMed:22504181}.; FUNCTION: (Microbial infection) Xanthomonas campestris effector AvrAC/XopAC-mediated uridylylation prevents activation by phosphorylation at the same residues, thus affecting immune responses and reducing defense responses toward X.campestris, mediating avrAC/XopAC virulence functions. {ECO:0000269|PubMed:26355215}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48847
|
LUH_ARATH
|
MAQSNWEADKMLDVYIYDYLVKKKLHNTAKSFMTEGKVSPDPVAIDAPGGFLFEWWSVFWDIFIARTNEKHSEAAAAYIEAQQGKAKEQQMQIQQLQMMRQAQMQRRDPNHPSLGGPMNAIGSEGMIGQSNASALAAKMYEERMKQPNPMNSETSQPHLDARMALLKSATNHHGQIVQGNHQGGVSAALQQIQSRTQQPTEIKTEVNLGTSPRQLPVDPSTVYGQGILQSKPGMGSAGLNPGVSGLPLKGWPLTGIEQMRPGLGGPQVQKSFLQNQSQFQLSPQQQQHQMLAQVQAQGNMTNSPMYGGDMDPRRFTGLPRGNLNPKDGQQNANDGSIGSPMQSSSSKHISMPPVQQSSSQQQDHLLSQQSQQNNRKRKGPSSSGPANSTGTGNTVGPSNSQPSTPSTHTPVDGVAIAGNMHHVNSMPKGPMMYGSDGIGGLASSANQLLQDDMDQFGDVGALEDNVESFLSQDDGDGGSLFGTLKRNSSVHTETSKPFSFNEVSCIRKSASKVICCSFSYDGKLLASAGHDKKVFIWNMETLQVESTPEEHAHIITDVRFRPNSTQLATSSFDKTIKIWDASDPGYFLRTISGHAAPVMSIDFHPKKTELLCSCDSNNDIRFWDINASCVRAVKGASTQVRFQPRTGQFLAAASENTVSIFDIENNNKRVNIFKGHSSNVHSVCWSPNGELVASVSEDAVKLWSLSSGDCIHELSNSGNKFHSVVFHPSYPDLLVIGGYQAIELWNTMENKCMTVAGHECVISALAQSPSTGVVASASHDKSVKIWK
| null | null |
cell differentiation [GO:0030154]; cellular response to external biotic stimulus [GO:0071217]; DNA damage response [GO:0006974]; embryo development ending in seed dormancy [GO:0009793]; flower development [GO:0009908]; galacturonan metabolic process [GO:0010393]; meristem maintenance [GO:0010073]; mucilage biosynthetic process [GO:0010192]; mucilage extrusion from seed coat [GO:0080001]; mucilage metabolic process involved in seed coat development [GO:0048359]; mucilage pectin biosynthetic process [GO:0048358]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of response to salt stress [GO:1901001]; plant-type cell wall modification [GO:0009827]; polarity specification of adaxial/abaxial axis [GO:0009944]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of cell wall pectin metabolic process [GO:1902066]; regulation of DNA-templated transcription [GO:0006355]; regulation of embryonic development [GO:0045995]; regulation of flower development [GO:0009909]; regulation of leaf development [GO:2000024]; regulation of response to osmotic stress [GO:0047484]; regulation of shoot apical meristem development [GO:1902183]; response to aluminum ion [GO:0010044]; response to auxin [GO:0009733]; response to bacterium [GO:0009617]; response to cycloheximide [GO:0046898]; response to fungus [GO:0009620]; response to hypoxia [GO:0001666]; response to nematode [GO:0009624]; response to oxidative stress [GO:0006979]; response to salt [GO:1902074]; response to silver ion [GO:0010272]; response to water deprivation [GO:0009414]; response to wounding [GO:0009611]
|
nucleus [GO:0005634]
|
transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]
|
PF08513;PF00400;
|
2.130.10.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21518777}.
| null | null | null | null | null |
FUNCTION: Transcription repressor subunit of the SEU-SLK1 and SEU-SLK2 transcriptional corepressor of abiotic stress (e.g. salt and osmotic stress) response genes, by means of an epigenetic process involving histone modification (e.g. H3K9 and H3K14 acetylation), probably by recruiting HDAC, to facilitate the condensation of chromatin thus preventing transcription at the target genes (PubMed:24564815). Can also act as a transcription activator (PubMed:21518777). Implicated in embryo and floral development (PubMed:18390806). Involved in post-synthesis cell wall modifications necessary for mucilage extrusion from seeds upon imbibition, probably by promoting the expression of genes required for mucilage maturation (e.g. MUM2) (PubMed:11706181, PubMed:21362134, PubMed:21402796, PubMed:21518777). Regulates the maintenance on leaf polarity and meristem activity as well as the initiation of embryonic shoot apical meristem (SAM) development (PubMed:19837869). {ECO:0000269|PubMed:11706181, ECO:0000269|PubMed:18390806, ECO:0000269|PubMed:19837869, ECO:0000269|PubMed:21362134, ECO:0000269|PubMed:21402796, ECO:0000269|PubMed:21518777, ECO:0000269|PubMed:24564815}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48849
|
RLP23_ARATH
|
MSKALLHLHFLSLFLLCCVCHSSIFTLNFHFTGIVACRPHQIQAFTKFTNEFDTRGCNNSDTFNGVWCDNSTGAVAVLQLRKCLSGTLKSNSSLFGFHQLRYVDLQNNNLTSSSLPSGFGNLKRLEGLFLSSNGFLGQVPSSFSNLTMLAQLDLSYNKLTGSFPLVRGLRKLIVLDLSYNHFSGTLNPNSSLFELHQLRYLNLAFNNFSSSLPSKFGNLHRLENLILSSNGFSGQVPSTISNLTRLTKLYLDQNKLTSSFPLVQNLTNLYELDLSYNKFFGVIPSSLLTLPFLAHLALRENNLAGSVEVSNSSTSSRLEIMYLGSNHFEGQILEPISKLINLKHLDLSFLNTSYPIDLKLFSSLKSLRSLDLSGNSISSASLSSDSYIPLTLEMLTLRHCDINEFPNILKTLKELVYIDISNNRMKGKIPEWLWSLPLLQSVTLGNNYFTGFQGSAEILVNSSVLLLYLDSNNFEGALPDLPLSIKGFGVASNSFTSEIPLSICNRSSLAAIDLSYNNFTGPIPPCLRNLELVYLRNNNLEGSIPDALCDGASLRTLDVSHNRLTGKLPRSFVNCSSLKFLSVINNRIEDTFPFWLKALPNLQVLTLRSNRFYGPISPPHQGPLGFPELRIFEISDNKFTGSLPPNYFVNWKASSRTMNQDGGLYMVYEEKLFDEGGYGYTDALDLQYKGLHMEQAKALTSYAAIDFSGNRLEGQIPESIGLLKALIAVNISNNAFTGHIPLSMANLENLESLDMSRNQLSGTIPNGLGSISFLAYINVSHNQLTGEIPQGTQITGQSKSSFEGNAGLCGLPLKESCFGTGAPPMYHQKQEDKEEEEEEEEEEEEVLNGRAVAIGYGSGLLLGLAIAQVIASYKPEWLVKIIGLNKRRKR
| null | null |
defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; defense response to oomycetes [GO:0002229]; detection of molecule of fungal origin [GO:0032491]; innate immune response-activating signaling pathway [GO:0002758]; pathogen-associated molecular pattern receptor signaling pathway [GO:0140426]; response to mannitol [GO:0010555]; response to molecule of bacterial origin [GO:0002237]; response to molecule of fungal origin [GO:0002238]; response to molecule of oomycetes origin [GO:0002240]
|
endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]
|
protein kinase binding [GO:0019901]
|
PF00560;PF13516;PF13855;
|
3.80.10.10;
|
RLP family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Involved in the perception of necrosis and ethylene-inducing peptide 1-like proteins (NLPs), that act as extracellular signals mediating immune activation. Component of the RLP23-SOBIR1-BAK1 complex that mediates NLP-triggered immunity. {ECO:0000269|PubMed:27251392}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48881
|
TPS1_BRANA
|
MQSLGGIRSWPATWRTTTASMTTTTTESVRKVAQVLTVAGSDSGAGAGIQADIKVCAARGVYCASVKTAVKAKNTRAVQSVHLLPPDSVSEQLKSVLSDFEVDVVKTGMLPSPEIVEVLLQNLSEYPVRALVVDPVMVSTSGHVLAGSSILSIFRERLLPLADIITPNVKEASALLGGVRIQTVAEMRSAAKSLHQMGPRFVLVKGGDLPDSSDSVDVYFDGNEFHELHSPRIATRNTHGTGCTLASCIAAELAKGSNMLSAVKVAKRFVDSALNYSKDIVIGSGMQGPFDHFLSLKDPQSYRQSTFKPDDLFLYAVTDSRMNKKWNRSIVDAVKAAIEGGATIIQLREKEAETREFLEEAKSCVDICRSNGVCLLINDRFDIAIALDADGVHVGQSDMPVDLVRSLLGPDKIIGVSCKTQEQAHQAWKDGADYIGSGGVFPTNTKANNRTIGLDGLREVCKASKLPVVAIGGIGISNAESVMRIGEPNLKGVAVVSALFDQECVLTQAKKLHKTLTESKREH
|
2.5.1.3; 2.7.1.49
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
|
phosphorylation [GO:0016310]; thiamine biosynthetic process [GO:0009228]; thiamine diphosphate biosynthetic process [GO:0009229]
|
chloroplast [GO:0009507]; cytosol [GO:0005829]
|
ATP binding [GO:0005524]; hydroxymethylpyrimidine kinase activity [GO:0008902]; metal ion binding [GO:0046872]; phosphomethylpyrimidine kinase activity [GO:0008972]; thiamine-phosphate diphosphorylase activity [GO:0004789]
|
PF08543;PF02581;
|
3.40.1190.20;3.20.20.70;
|
Thiamine-phosphate synthase family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3; Evidence={ECO:0000269|PubMed:9700068}; CATALYTIC ACTIVITY: Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3; Evidence={ECO:0000269|PubMed:9700068}; CATALYTIC ACTIVITY: Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl-5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine phosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:58296; EC=2.5.1.3; Evidence={ECO:0000269|PubMed:9700068}; CATALYTIC ACTIVITY: Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+); Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892, ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.1.49; Evidence={ECO:0000250|UniProtKB:P30137};
| null |
PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.; PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 2/3.
| null | null |
FUNCTION: Essential for thiamine biosynthesis. Bifunctional enzyme that catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP and condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). {ECO:0000269|PubMed:9700068}.
|
Brassica napus (Rape)
|
O48915
|
NDR1_ARATH
|
MNNQNEDTEGGRNCCTCCLSFIFTAGLTSLFLWLSLRADKPKCSIQNFFIPALGKDPNSRDNTTLNFMVRCDNPNKDKGIYYDDVHLNFSTINTTKINSSALVLVGNYTVPKFYQGHKKKAKKWGQVKPLNNQTVLRAVLPNGSAVFRLDLKTQVRFKIVFWKTKRYGVEVGADVEVNGDGVKAQKKGIKMKKSDSSFPLRSSFPISVLMNLLVFFAIR
| null | null |
defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; defense response to other organism [GO:0098542]; plant-type hypersensitive response [GO:0009626]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]; side of membrane [GO:0098552]
| null | null | null | null |
PTM: N-glycosylated. {ECO:0000269|PubMed:15447649}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15447649}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:15447649}.
| null | null | null | null | null |
FUNCTION: Involved in disease resistance. Required for resistance conferred by multiple R genes recognizing different bacterial and oomycete pathogen isolates like avirulent P.syringae or H.parasitica (downy mildew). Required for the establishment of hypersensitive response (HR) and systemic acquired resistance (SAR) after infection with the bacterial pathogen P.syringae DC3000 carrying avrRpt2. Required for resistance to the soilborne fungus V.longisporum. Interaction with RIN4 is required for the activation of the R gene RPS2 and RPS2-mediated resistance. {ECO:0000269|PubMed:11607554, ECO:0000269|PubMed:11706189, ECO:0000269|PubMed:15447649, ECO:0000269|PubMed:16941900, ECO:0000269|PubMed:17012600}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48917
|
SQD1_ARATH
|
MAHLLSASCPSVISLSSSSSKNSVKPFVSGQTFFNAQLLSRSSLKGLLFQEKKPRKSCVFRATAVPITQQAPPETSTNNSSSKPKRVMVIGGDGYCGWATALHLSKKNYEVCIVDNLVRRLFDHQLGLESLTPIASIHDRISRWKALTGKSIELYVGDICDFEFLAESFKSFEPDSVVHFGEQRSAPYSMIDRSRAVYTQHNNVIGTLNVLFAIKEFGEECHLVKLGTMGEYGTPNIDIEEGYITITHNGRTDTLPYPKQASSFYHLSKVHDSHNIAFTCKAWGIRATDLNQGVVYGVKTDETEMHEELRNRLDYDAVFGTALNRFCVQAAVGHPLTVYGKGGQTRGYLDIRDTVQCVEIAIANPAKAGEFRVFNQFTEQFSVNELASLVTKAGSKLGLDVKKMTVPNPRVEAEEHYYNAKHTKLMELGLEPHYLSDSLLDSLLNFAVQFKDRVDTKQIMPSVSWKKIGVKTKSMTT
|
3.13.1.1
|
COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540;
|
cellular response to phosphate starvation [GO:0016036]; glycolipid biosynthetic process [GO:0009247]; sulfolipid biosynthetic process [GO:0046506]
|
chloroplast [GO:0009507]; plasma membrane [GO:0005886]
|
sulfotransferase activity [GO:0008146]; UDPsulfoquinovose synthase activity [GO:0046507]; zinc ion binding [GO:0008270]
|
PF01370;
|
3.40.50.720;3.90.25.10;
|
NAD(P)-dependent epimerase/dehydratase family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:9465123}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + sulfite + UDP-alpha-D-glucose = H2O + UDP-alpha-D-6-sulfoquinovose; Xref=Rhea:RHEA:13197, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:58885, ChEBI:CHEBI:60009; EC=3.13.1.1;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=150 uM for UDP-glucose; KM=10 uM for sulfite;
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-9.5.;
| null |
FUNCTION: Involved in the biosynthesis of sulfolipids found in thylakoid membranes. Converts UDP-glucose and sulfite to the sulfolipid head group precursor UDP-sulfoquinovose. {ECO:0000269|PubMed:11073956}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48946
|
CESA1_ARATH
|
MEASAGLVAGSYRRNELVRIRHESDGGTKPLKNMNGQICQICGDDVGLAETGDVFVACNECAFPVCRPCYEYERKDGTQCCPQCKTRFRRHRGSPRVEGDEDEDDVDDIENEFNYAQGANKARHQRHGEEFSSSSRHESQPIPLLTHGHTVSGEIRTPDTQSVRTTSGPLGPSDRNAISSPYIDPRQPVPVRIVDPSKDLNSYGLGNVDWKERVEGWKLKQEKNMLQMTGKYHEGKGGEIEGTGSNGEELQMADDTRLPMSRVVPIPSSRLTPYRVVIILRLIILCFFLQYRTTHPVKNAYPLWLTSVICEIWFAFSWLLDQFPKWYPINRETYLDRLAIRYDRDGEPSQLVPVDVFVSTVDPLKEPPLVTANTVLSILSVDYPVDKVACYVSDDGSAMLTFESLSETAEFAKKWVPFCKKFNIEPRAPEFYFAQKIDYLKDKIQPSFVKERRAMKREYEEFKVRINALVAKAQKIPEEGWTMQDGTPWPGNNTRDHPGMIQVFLGHSGGLDTDGNELPRLIYVSREKRPGFQHHKKAGAMNALIRVSAVLTNGAYLLNVDCDHYFNNSKAIKEAMCFMMDPAIGKKCCYVQFPQRFDGIDLHDRYANRNIVFFDINMKGLDGIQGPVYVGTGCCFNRQALYGYDPVLTEEDLEPNIIVKSCCGSRKKGKSSKKYNYEKRRGINRSDSNAPLFNMEDIDEGFEGYDDERSILMSQRSVEKRFGQSPVFIAATFMEQGGIPPTTNPATLLKEAIHVISCGYEDKTEWGKEIGWIYGSVTEDILTGFKMHARGWISIYCNPPRPAFKGSAPINLSDRLNQVLRWALGSIEILLSRHCPIWYGYHGRLRLLERIAYINTIVYPITSIPLIAYCILPAFCLITDRFIIPEISNYASIWFILLFISIAVTGILELRWSGVSIEDWWRNEQFWVIGGTSAHLFAVFQGLLKVLAGIDTNFTVTSKATDEDGDFAELYIFKWTALLIPPTTVLLVNLIGIVAGVSYAVNSGYQSWGPLFGKLFFALWVIAHLYPFLKGLLGRQNRTPTIVIVWSVLLASIFSLLWVRINPFVDANPNANNFNGKGGVF
|
2.4.1.12
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9SWW6}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9SWW6}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q941L0};
|
cell wall organization [GO:0071555]; cellulose biosynthetic process [GO:0030244]; hyperosmotic salinity response [GO:0042538]; plant-type primary cell wall biogenesis [GO:0009833]
|
endosome [GO:0005768]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]
|
cellulose synthase (UDP-forming) activity [GO:0016760]; metal ion binding [GO:0046872]
|
PF03552;PF14569;
|
3.30.40.10;
|
Glycosyltransferase 2 family, Plant cellulose synthase subfamily
|
PTM: S-acylated. {ECO:0000269|PubMed:27387950}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378, ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12; Evidence={ECO:0000305|PubMed:11901167, ECO:0000305|PubMed:12481071};
| null |
PATHWAY: Glycan metabolism; plant cellulose biosynthesis.
| null | null |
FUNCTION: Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the primary cell wall formation. Required during embryogenesis for cell elongation, orientation of cell expansion and complex cell wall formations, such as interdigitated pattern of epidermal pavement cells, stomatal guard cells and trichomes. Plays a role in lateral roots formation, but seems not necessary for the development of tip-growing cells such as root hairs. The presence of each protein CESA1 and CESA6 is critical for cell expansion after germination. {ECO:0000269|PubMed:10987560, ECO:0000269|PubMed:11148287, ECO:0000269|PubMed:11732051, ECO:0000269|PubMed:11732056, ECO:0000269|PubMed:11901167, ECO:0000269|PubMed:12068120, ECO:0000269|PubMed:12481071, ECO:0000269|PubMed:17878302, ECO:0000269|PubMed:17878303, ECO:0000269|PubMed:9445479}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48947
|
CESA2_ARATH
|
MNTGGRLIAGSHNRNEFVLINADESARIRSVQELSGQTCQICGDEIELTVSSELFVACNECAFPVCRPCYEYERREGNQACPQCKTRYKRIKGSPRVDGDDEEEEDIDDLEYEFDHGMDPEHAAEAALSSRLNTGRGGLDSAPPGSQIPLLTYCDEDADMYSDRHALIVPPSTGYGNRVYPAPFTDSSAPPQARSMVPQKDIAEYGYGSVAWKDRMEVWKRRQGEKLQVIKHEGGNNGRGSNDDDELDDPDMPMMDEGRQPLSRKLPIRSSRINPYRMLILCRLAILGLFFHYRILHPVNDAYGLWLTSVICEIWFAVSWILDQFPKWYPIERETYLDRLSLRYEKEGKPSGLAPVDVFVSTVDPLKEPPLITANTVLSILAVDYPVDKVACYVSDDGAAMLTFEALSDTAEFARKWVPFCKKFNIEPRAPEWYFSQKMDYLKNKVHPAFVRERRAMKRDYEEFKVKINALVATAQKVPEEGWTMQDGTPWPGNNVRDHPGMIQVFLGHSGVRDTDGNELPRLVYVSREKRPGFDHHKKAGAMNSLIRVSAVLSNAPYLLNVDCDHYINNSKAIRESMCFMMDPQSGKKVCYVQFPQRFDGIDRHDRYSNRNVVFFDINMKGLDGIQGPIYVGTGCVFRRQALYGFDAPKKKKPPGKTCNCWPKWCCLCCGLRKKSKTKAKDKKTNTKETSKQIHALENVDEGVIVPVSNVEKRSEATQLKLEKKFGQSPVFVASAVLQNGGVPRNASPACLLREAIQVISCGYEDKTEWGKEIGWIYGSVTEDILTGFKMHCHGWRSVYCMPKRAAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHCPIWYGYGGGLKWLERFSYINSVVYPWTSLPLIVYCSLPAVCLLTGKFIVPEISNYAGILFMLMFISIAVTGILEMQWGGVGIDDWWRNEQFWVIGGASSHLFALFQGLLKVLAGVNTNFTVTSKAADDGAFSELYIFKWTTLLIPPTTLLIINIIGVIVGVSDAISNGYDSWGPLFGRLFFALWVIVHLYPFLKGMLGKQDKMPTIIVVWSILLASILTLLWVRVNPFVAKGGPVLEICGLNCGN
|
2.4.1.12
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q941L0}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9SWW6}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9SWW6};
|
cell wall organization [GO:0071555]; cellulose biosynthetic process [GO:0030244]; plant-type primary cell wall biogenesis [GO:0009833]
|
plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]
|
cellulose synthase (UDP-forming) activity [GO:0016760]; metal ion binding [GO:0046872]
|
PF03552;PF14569;
|
3.30.40.10;
|
Glycosyltransferase 2 family, Plant cellulose synthase subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378, ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12; Evidence={ECO:0000305};
| null |
PATHWAY: Glycan metabolism; plant cellulose biosynthesis.
| null | null |
FUNCTION: Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the primary cell wall formation. {ECO:0000269|PubMed:12068120, ECO:0000269|PubMed:17085513, ECO:0000269|PubMed:17878303}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O48963
|
PHOT1_ARATH
|
MEPTEKPSTKPSSRTLPRDTRGSLEVFNPSTQLTRPDNPVFRPEPPAWQNLSDPRGTSPQPRPQQEPAPSNPVRSDQEIAVTTSWMALKDPSPETISKKTITAEKPQKSAVAAEQRAAEWGLVLKTDTKTGKPQGVGVRNSGGTENDPNGKKTTSQRNSQNSCRSSGEMSDGDVPGGRSGIPRVSEDLKDALSTFQQTFVVSDATKPDYPIMYASAGFFNMTGYTSKEVVGRNCRFLQGSGTDADELAKIRETLAAGNNYCGRILNYKKDGTSFWNLLTIAPIKDESGKVLKFIGMQVEVSKHTEGAKEKALRPNGLPESLIRYDARQKDMATNSVTELVEAVKRPRALSESTNLHPFMTKSESDELPKKPARRMSENVVPSGRRNSGGGRRNSMQRINEIPEKKSRKSSLSFMGIKKKSESLDESIDDGFIEYGEEDDEISDRDERPESVDDKVRQKEMRKGIDLATTLERIEKNFVITDPRLPDNPIIFASDSFLELTEYSREEILGRNCRFLQGPETDLTTVKKIRNAIDNQTEVTVQLINYTKSGKKFWNIFHLQPMRDQKGEVQYFIGVQLDGSKHVEPVRNVIEETAVKEGEDLVKKTAVNIDEAVRELPDANMTPEDLWANHSKVVHCKPHRKDSPPWIAIQKVLESGEPIGLKHFKPVKPLGSGDTGSVHLVELVGTDQLFAMKAMDKAVMLNRNKVHRARAEREILDLLDHPFLPALYASFQTKTHICLITDYYPGGELFMLLDRQPRKVLKEDAVRFYAAQVVVALEYLHCQGIIYRDLKPENVLIQGNGDISLSDFDLSCLTSCKPQLLIPSIDEKKKKKQQKSQQTPIFMAEPMRASNSFVGTEEYIAPEIISGAGHTSAVDWWALGILMYEMLYGYTPFRGKTRQKTFTNVLQKDLKFPASIPASLQVKQLIFRLLQRDPKKRLGCFEGANEVKQHSFFKGINWALIRCTNPPELETPIFSGEAENGEKVVDPELEDLQTNVF
|
2.7.11.1
|
COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:18585389, ECO:0000269|PubMed:24316821}; Note=Binds 2 FMN per subunit. {ECO:0000269|PubMed:18585389, ECO:0000269|PubMed:24316821};
|
cellular response to blue light [GO:0071483]; chloroplast accumulation movement [GO:0009904]; chloroplast avoidance movement [GO:0009903]; circadian rhythm [GO:0007623]; negative regulation of anion channel activity by blue light [GO:0010362]; phototropism [GO:0009638]; protein autophosphorylation [GO:0046777]; regulation of proton transport [GO:0010155]; regulation of stomatal movement [GO:0010119]; response to blue light [GO:0009637]
|
cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; nucleus [GO:0005634]; plant-type vacuole [GO:0000325]
|
ATP binding [GO:0005524]; blue light photoreceptor activity [GO:0009882]; FMN binding [GO:0010181]; identical protein binding [GO:0042802]; kinase activity [GO:0016301]; mRNA binding [GO:0003729]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF13426;PF00069;
|
3.30.450.20;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family
|
PTM: Autophosphorylated at Ser-185, Ser-350 and Ser-410 in response to blue light irradiation. {ECO:0000269|PubMed:11537679, ECO:0000269|PubMed:16777956, ECO:0000269|PubMed:20031924, ECO:0000269|PubMed:28358053, ECO:0000269|PubMed:9831559, ECO:0000305}.; PTM: 2 molecules of FMN bind covalently to cysteines after exposure to blue light and are reversed in the dark. {ECO:0000269|PubMed:10411952}.
|
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cytoplasm.
|
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; Evidence={ECO:0000269|PubMed:16777956, ECO:0000269|PubMed:20031924, ECO:0000269|PubMed:23811955, ECO:0000269|PubMed:29101334}; 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; Evidence={ECO:0000303|PubMed:31904040};
| null | null | null | null |
FUNCTION: Protein kinase that acts as a blue light (BL) photoreceptor in a signal-transduction pathway for photo-induced movements (PubMed:14739272, PubMed:15821287, PubMed:29101334, PubMed:31904040). Triggers the phosphorylation of AHA1 and AHA2 C-terminal penultimate Thr in guard cells to activate them and induce stomatal opening in response to blue light (BL) (PubMed:15821287, PubMed:31904040). Phosphorylates also BLUS1, a kinase involved in stomatal opening (PubMed:23811955). Mediates the phosphorylation of CBC1 in stomata, but not of CBC2, in response to blue light (PubMed:29101334). Required for blue light mediated mRNA destabilization. Mediates calcium spiking of extracellular origin in response to a low rate of blue light. Also mediates rapid membrane depolarization and growth inhibition in response to blue light. Necessary for root phototropism. Involved in hypocotyl phototropism under a low rate but not under a high rate of blue light. Contributes to the chloroplast accumulation but seems not to be required for chloroplast translocation. Regulates stomata opening and photomorphogenesis response of leaf tissue. Confers sensitivity to drought. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening. {ECO:0000269|PubMed:10662859, ECO:0000269|PubMed:11439133, ECO:0000269|PubMed:12650626, ECO:0000269|PubMed:12821778, ECO:0000269|PubMed:14739272, ECO:0000269|PubMed:14982991, ECO:0000269|PubMed:15031408, ECO:0000269|PubMed:15821287, ECO:0000269|PubMed:16777956, ECO:0000269|PubMed:20031924, ECO:0000269|PubMed:23811955, ECO:0000269|PubMed:29101334, ECO:0000269|PubMed:31904040, ECO:0000303|PubMed:15821287, ECO:0000303|PubMed:31904040}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49006
|
PME3_ARATH
|
MAPSMKEIFSKDNFKKNKKLVLLSAAVALLFVAAVAGISAGASKANEKRTLSPSSHAVLRSSCSSTRYPELCISAVVTAGGVELTSQKDVIEASVNLTITAVEHNYFTVKKLIKKRKGLTPREKTALHDCLETIDETLDELHETVEDLHLYPTKKTLREHAGDLKTLISSAITNQETCLDGFSHDDADKQVRKALLKGQIHVEHMCSNALAMIKNMTDTDIANFEQKAKITSNNRKLKEENQETTVAVDIAGAGELDSEGWPTWLSAGDRRLLQGSGVKADATVAADGSGTFKTVAAAVAAAPENSNKRYVIHIKAGVYRENVEVAKKKKNIMFMGDGRTRTIITGSRNVVDGSTTFHSATVAAVGERFLARDITFQNTAGPSKHQAVALRVGSDFSAFYNCDMLAYQDTLYVHSNRQFFVKCLIAGTVDFIFGNAAVVLQDCDIHARRPNSGQKNMVTAQGRTDPNQNTGIVIQKCRIGATSDLQSVKGSFPTYLGRPWKEYSQTVIMQSAISDVIRPEGWSEWTGTFALNTLTYREYSNTGAGAGTANRVKWRGFKVITAAAEAQKYTAGQFIGGGGWLSSTGFPFSLGL
|
3.1.1.11
| null |
cell wall modification [GO:0042545]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; negative regulation of seed germination [GO:0010187]; pectin catabolic process [GO:0045490]; regulation of gene expression [GO:0010468]; regulation of unidimensional cell growth [GO:0051510]; response to bacterium [GO:0009617]; response to fungus [GO:0009620]; response to nematode [GO:0009624]; response to zinc ion [GO:0010043]; root development [GO:0048364]; root hair cell development [GO:0080147]
|
apoplast [GO:0048046]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plant-type cell wall [GO:0009505]
|
aspartyl esterase activity [GO:0045330]; mRNA binding [GO:0003729]; pectinesterase activity [GO:0030599]; pectinesterase inhibitor activity [GO:0046910]
|
PF01095;PF04043;
|
1.20.140.40;2.160.20.10;
|
PMEI family; Pectinesterase family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:15593128}. Secreted, cell wall {ECO:0000269|PubMed:26183897}. Note=Present in hypocotyl cell walls. {ECO:0000269|PubMed:26183897}.
|
CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol; Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11; Evidence={ECO:0000269|PubMed:26183897}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22381; Evidence={ECO:0000269|PubMed:26183897};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12 uM for HG96B82 {ECO:0000269|PubMed:26183897}; KM=5 uM for HG96B69 {ECO:0000269|PubMed:26183897}; KM=9 uM for HG96B20 {ECO:0000269|PubMed:26183897}; KM=6 uM for HG97B77P63 {ECO:0000269|PubMed:26183897}; KM=224 uM for HG96P64 {ECO:0000269|PubMed:26183897}; Vmax=0.07 umol/min/ug enzyme with HG96B82 as substrate {ECO:0000269|PubMed:26183897}; Vmax=0.05 umol/min/ug enzyme with HG96B69 as substrate {ECO:0000269|PubMed:26183897}; Vmax=0.1 umol/min/ug enzyme with HG96B20 as substrate {ECO:0000269|PubMed:26183897}; Vmax=0.05 umol/min/ug enzyme with HG97B77P63 as substrate {ECO:0000269|PubMed:26183897}; Vmax=0.02 umol/min/ug enzyme with HG96P64 as substrate {ECO:0000269|PubMed:26183897};
|
PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5. {ECO:0000305}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 on homogalacturonan (HG) substrates with a degree of methylesterification between 60 and 80% and a random distribution of methyl esters. {ECO:0000269|PubMed:26183897};
| null |
FUNCTION: Acts in the modification of cell walls via demethylesterification of cell wall pectin (PubMed:21171891, PubMed:26183897). Required for zinc Zn(2+) homeostasis and to monitor Zn(2+) influence on cell wall-controlled growth processes such as root cell elongation (PubMed:23826687). Monitors seed germination and favors root hairs production (PubMed:28375469). Prevents cruciferin seed storage proteins activity, but promotes the expression of genes involved in cell wall organization and remodeling as well as genes involved in lipid and protein metabolism, during post-germinative growth of seedlings (PubMed:28375469). Confers sensitivity to Zn(2+) when overexpressed (PubMed:23826687). Acts as a susceptibility factor required for the initial colonization of the host tissue by virulent pathogens including Botrytis cinerea and Pectobacterium carotovorum, probably by facilitating cell wall pectine degradation by pathogen pectic enzymes after its demethylesterification (PubMed:21171891). {ECO:0000269|PubMed:21171891, ECO:0000269|PubMed:23826687, ECO:0000269|PubMed:26183897, ECO:0000269|PubMed:28375469}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49048
|
VPS45_ARATH
|
MVLVTSVRDYINRMLQDISGMKVLILDSETVSNVSIVYSQSELLQKEVFLVEMIDSISVSKESMSHLKAVYFIRPTSDNIQKLRYQLANPRFGEYHLFFSNLLKDTQIHILADSDEQEVVQQVQEYYADFVSGDPYHFTLNMASNHLYMIPAVVDPSGLQRFSDRVVDGIAAVFLALKRRPVIRYQRTSDTAKRIAHETAKLMYQHESALFDFRRTESSPLLLVIDRRDDPVTPLLNQWTYQAMVHELIGLQDNKVDLKSIGSLPKDQQVEVVLSSEQDAFFKSNMYENFGDIGMNIKRMVDDFQQVAKSNQNIQTVEDMARFVDNYPEYKKMQGNVSKHVTLVTEMSKLVEARKLMTVSQTEQDLACNGGQGAAYEAVTDLLNNESVSDIDRLRLVMLYALRYEKENPVQLMQLFNKLASRSPKYKPGLVQFLLKQAGVEKRTGDLFGNRDLLNIARNMARGLKGVENVYTQHQPLLFQTMESITRGRLRDVDYPFVGDHFQQGRPQEVVIFMVGGTTYEESRSVALQNATNSGVRFILGGTAVLNSKRFLKDLEEAQRISRSGSHMV
| null | null |
auxin-activated signaling pathway [GO:0009734]; intracellular protein transport [GO:0006886]; pollen germination [GO:0009846]; positive regulation of cell growth [GO:0030307]; regulation of auxin polar transport [GO:2000012]; regulation of root morphogenesis [GO:2000067]; regulation of vesicle fusion [GO:0031338]; vesicle-mediated transport [GO:0016192]
|
early endosome [GO:0005769]; Golgi membrane [GO:0000139]; mitochondrion [GO:0005739]; plant-type vacuole membrane [GO:0009705]; SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802]
| null |
PF00995;
|
1.25.40.60;3.40.50.1910;3.40.50.2060;
|
STXBP/unc-18/SEC1 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:10888666}; Peripheral membrane protein {ECO:0000269|PubMed:10888666}. Early endosome {ECO:0000269|PubMed:23737757}. Note=Binds to trans-Golgi network membranes through interaction with other proteins. {ECO:0000269|PubMed:10888666}.
| null | null | null | null | null |
FUNCTION: Involved in the protein transport to the vacuole, probably at the level of vesicle fusion at the trans-Golgi network (TGN) and not in transport from the TGN to the prevacuolar compartment, by promoting the recycling of vacuolar sorting receptors back to the TGN (PubMed:19251905). Involved in early endosomal vesicle trafficking, particularly at the trans-Golgi-network/early endosome (TGN/EE) thus residing in early endocytic route (PubMed:23737757). Together with BIG5/BEN1 required for polar PIN-FORMED (PIN) proteins localization, for their dynamic repolarization, and consequently for auxin activity gradient formation and auxin-related developmental processes (e.g. embryonic patterning, organogenesis and vasculature venation patterning) (PubMed:23737757). Necessary for pollen germination and for cell expansion (PubMed:19251905). Binds syntaxins. {ECO:0000269|PubMed:19251905, ECO:0000269|PubMed:23737757}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49139
|
CMT1_ARATH
|
MAARNKQKKRAEPESDLCFAGKPMSVVESTIRWPHRYQSKKTKLQAPTKKPANKGGKKEDEEIIKQAKCHFDKALVDGVLINLNDDVYVTGLPGKLKFIAKVIELFEADDGVPYCRFRWYYRPEDTLIERFSHLVQPKRVFLSNDENDNPLTCIWSKVNIAKVPLPKITSRIEQRVIPPCDYYYDMKYEVPYLNFTSADDGSDASSSLSSDSALNCFENLHKDEKFLLDLYSGCGAMSTGFCMGASISGVKLITKWSVDINKFACDSLKLNHPETEVRNEAAEDFLALLKEWKRLCEKFSLVSSTEPVESISELEDEEVEENDDIDEASTGAELEPGEFEVEKFLGIMFGDPQGTGEKTLQLMVRWKGYNSSYDTWEPYSGLGNCKEKLKEYVIDGFKSHLLPLPGTVYTVCGGPPCQGISGYNRYRNNEAPLEDQKNQQLLVFLDIIDFLKPNYVLMENVVDLLRFSKGFLARHAVASFVAMNYQTRLGMMAAGSYGLPQLRNRVFLWAAQPSEKLPPYPLPTHEVAKKFNTPKEFKDLQVGRIQMEFLKLDNALTLADAISDLPPVTNYVANDVMDYNDAAPKTEFENFISLKRSETLLPAFGGDPTRRLFDHQPLVLGDDDLERVSYIPKQKGANYRDMPGVLVHNNKAEINPRFRAKLKSGKNVVPAYAISFIKGKSKKPFGRLWGDEIVNTVVTRAEPHNQCVIHPMQNRVLSVRENARLQGFPDCYKLCGTIKEKYIQVGNAVAVPVGVALGYAFGMASQGLTDDEPVIKLPFKYPECMQAKDQI
|
2.1.1.37
| null |
chromatin organization [GO:0006325]; DNA-mediated transformation [GO:0009294]; methylation [GO:0032259]
|
nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA binding [GO:0003677]
|
PF01426;PF00385;PF00145;
|
2.30.30.490;3.90.120.10;3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
|
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;
| null | null | null | null |
FUNCTION: May be involved in the CpXpG methylation and in gene silencing. {ECO:0000250}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49163
|
HM1_MAIZE
|
MAEKESNGVRVCVTGGAGFIGSWLVRKLLEKGYTVHATLRNTGDEAKAGLLRRLVPGAAERLRLFQADLFDAATFAPAIAGCQFVFLVATPFGLDSAGSQYKSTAEAVVDAVHAILRQCEESRTVKRVIHTASVAAASPLLEEEVPASGVGYRDFIDESCWTSLNVDYPLRSAHFDKYILSKLQSEQELLSYNNGESPAFEVVTLPLGLVAGDTVLGRAPETVESAVAPVSRSEPYFGLLRILQQLLGSLPLVHVDDVCDALVFCMERRPSVAGRFLCAAAYPTIHDVVAHYASKFPHLDILKETTEAVATVRPARDRLGELGFKYKYGMEEILDSSVACAARLGSLDASKLGLQKG
|
1.3.1.-
| null |
defense response to fungus [GO:0050832]; toxin catabolic process [GO:0009407]
| null |
aldo-keto reductase (NADP) activity [GO:0004033]; oxidoreductase activity [GO:0016491]
|
PF01370;
|
3.40.50.720;
|
NAD(P)-dependent epimerase/dehydratase family
| null | null | null | null | null | null | null |
FUNCTION: In tandem with Hm2, NADPH-dependent Helminthosporium carbonum (HC) toxin reductase (HCTR), which inactivates HC toxin, a cyclic tetrapeptide produced by the fungus Cochliobolus carbonum to permit infection and acting as an inhibitor of host histone deacetylases (HDACs), thus conferring resistance against C.carbonum race 1 in resistant cultivars (e.g. cv. B73 and cv. Wisconsin 22) (PubMed:1359642, PubMed:16839576, PubMed:9465077). Catalyzes the production of 8-hydroxy derivative of HC-toxin via the reduction of the 8-keto group of 2-amino-9,10-epoxy-8-oxo-decanoic acid, an amino acid of the HC-toxin (PubMed:16668492). {ECO:0000269|PubMed:1359642, ECO:0000269|PubMed:16668492, ECO:0000269|PubMed:9465077, ECO:0000303|PubMed:16839576}.
|
Zea mays (Maize)
|
O49196
|
APK2_ARATH
|
MEGLAIRASRPSVFCSIPGLGGDSHRKPPSDGFLKLPASSIPADSRKLVANSTSFHPISAVNVSAQASLTADFPALSETILKEGRNNGKEKAENIVWHESSICRCDRQQLLQQKGCVVWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEHRTENIRRIGEVAKLFADVGVICIASLISPYRRDRDACRSLLPDGDFVEVFMDVPLHVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPVNCEVVLKHTGDDESCSPRQMAENIISYLQNKGYLEG
|
2.7.1.25
| null |
cysteine biosynthetic process [GO:0019344]; hydrogen sulfide biosynthetic process [GO:0070814]; phosphorylation [GO:0016310]; sulfate assimilation [GO:0000103]
|
chloroplast [GO:0009507]; plastid [GO:0009536]
|
adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]
|
PF01583;
|
3.40.50.300;
|
APS kinase family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:19304933}.
|
CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339, ChEBI:CHEBI:456216; EC=2.7.1.25;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 uM for adenylyl sulfate {ECO:0000269|PubMed:19304933}; Vmax=10.6 mmol/min/mg enzyme {ECO:0000269|PubMed:19304933};
|
PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
| null | null |
FUNCTION: Catalyzes the synthesis of activated sulfate. Essential for plant reproduction and viability. Required for the production of glucosinolates. {ECO:0000269|PubMed:11488606, ECO:0000269|PubMed:19304933, ECO:0000269|PubMed:19903478, ECO:0000269|PubMed:23218016}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49203
|
NDK3_ARATH
|
MSSQICRSASKAAKSLLSSAKNARFFSEGRAIGAAAAVSASGKIPLYASNFARSSGSGVASKSWITGLLALPAAAYMIQDQEVLAAEMERTFIAIKPDGVQRGLISEIISRFERKGFKLVGIKVIVPSKDFAQKHYHDLKERPFFNGLCDFLSSGPVIAMVWEGDGVIRYGRKLIGATDPQKSEPGTIRGDLAVTVGRNIIHGSDGPETAKDEISLWFKPQELVSYTSNSEKWLYGDN
|
2.7.4.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
CTP biosynthetic process [GO:0006241]; GTP biosynthetic process [GO:0006183]; phosphorylation [GO:0016310]; UTP biosynthetic process [GO:0006228]
|
chloroplast thylakoid lumen [GO:0009543]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; cobalt ion binding [GO:0050897]; nucleoside diphosphate kinase activity [GO:0004550]; zinc ion binding [GO:0008270]
|
PF00334;
|
3.30.70.141;
|
NDK family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. Mitochondrion intermembrane space.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
| null | null | null | null |
FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Shows the highest specificity towards GDP (By similarity). {ECO:0000250}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49230
|
ETR1_BRAOL
|
MEVCNCIEPQWPADELLMKYQYISDFFIAVAYFSIPLELIYFVKKSAVFPYRWVLVQFGAFIVLCGATHLINLWTFTTHSRTVALVMTTAKVLTAVVSCATALMLVHIIPDLLSVKTRELFLKNKAAELDREMGLIRTQEETGRHVRMLTHEIRSTLDRHTILKTTLVELGRTLALEECALWMPTRTGLELQLSYTLRQQHPVEYTVPIQLPVINQVFGTSRAVKISPNSPVARLRPVSGKYLLGEVVAVRVPLLHLSNFQINDWPELSTKRYALMVLMLPSDSARQWHVHELELVEVVADQVAVALSHAAILEESMRARDLLMEQNVALDIARREAETAIRARNDFLAVMNHEMRTPMHAIIALSSLLQETELTPEQRLMVETVLKSSSLLATLMNDVLDLSRLEDGSLQLELGTFNLHTLFREVLNLIKPIAVVKKLPITLNLAPDLPEFVVGDEKRLMQIILNIVGNAVKFSKQGSISVTALVTKSDNRAPPDFFVVPTGSHFYLRVKVKDLGAGINPQDIPKLFTKFAQTQSLATRSSGGSGLGLAISKRFVNLMEGNIWIESEGVGKGCTAIFDVKLAISNESKQSGIPKVPANPQHVNFAGLKVLVMDENGVSRMVTKGLLVHLGCEVTTVSSNEECLRVVSHEHRVVFMDVCTPGVENYQIALRIHEKFTKRHQRPLLVALTGNTDKSTKEKCMSFGLDGVLLKPVSLDNMRNVLSDRLEHRVLYEAM
|
2.7.13.3
|
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; Note=Binds 1 copper ion per dimer. {ECO:0000250};
|
cell division [GO:0051301]; cytokinin metabolic process [GO:0009690]; defense response by callose deposition in cell wall [GO:0052544]; defense response to bacterium [GO:0042742]; detection of ethylene stimulus [GO:0009727]; hydrogen peroxide biosynthetic process [GO:0050665]; negative regulation of ethylene-activated signaling pathway [GO:0010105]; phloem or xylem histogenesis [GO:0010087]; regulation of seedling development [GO:1900140]; regulation of stomatal movement [GO:0010119]; response to abscisic acid [GO:0009737]; response to auxin [GO:0009733]; response to gibberellin [GO:0009739]; response to heat [GO:0009408]; response to insect [GO:0009625]; response to molecule of bacterial origin [GO:0002237]; response to salt stress [GO:0009651]; seed dormancy process [GO:0010162]
|
endoplasmic reticulum membrane [GO:0005789]
|
ATP binding [GO:0005524]; ethylene binding [GO:0051740]; ethylene receptor activity [GO:0038199]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phosphorelay sensor kinase activity [GO:0000155]
|
PF01590;PF02518;PF00512;PF00072;
|
1.10.287.130;3.30.450.40;3.40.50.2300;3.30.565.10;
|
Ethylene receptor family
|
PTM: Activation probably requires a transfer of a phosphate group between a His in the transmitter domain and an Asp of the receiver domain. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3;
| null | null | null | null |
FUNCTION: May act early in the ethylene signal transduction pathway, possibly as an ethylene receptor, or as a regulator of the pathway. {ECO:0000250}.
|
Brassica oleracea (Wild cabbage)
|
O49255
|
NAC29_ARATH
|
MEVTSQSTLPPGFRFHPTDEELIVYYLRNQTMSKPCPVSIIPEVDIYKFDPWQLPEKTEFGENEWYFFSPRERKYPNGVRPNRAAVSGYWKATGTDKAIHSGSSNVGVKKALVFYKGRPPKGIKTDWIMHEYRLHDSRKASTKRNGSMRLDEWVLCRIYKKRGASKLLNEQEGFMDEVLMEDETKVVVNEAERRTEEEIMMMTSMKLPRTCSLAHLLEMDYMGPVSHIDNFSQFDHLHQPDSESSWFGDLQFNQDEILNHHRQAMFKF
| null | null |
embryo development ending in seed dormancy [GO:0009793]; flower development [GO:0009908]; fruit ripening [GO:0009835]; leaf senescence [GO:0010150]; multidimensional cell growth [GO:0009825]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976]
|
PF02365;
|
2.170.150.80;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:16640597}.
| null | null | null | null | null |
FUNCTION: Transcription activator that binds to, and transactivates the promoter of the abscisic aldehyde oxidase AAO3. Promotes chlorophyll degradation in leaves by enhancing transcription of AAO3, which leads to increased levels of the senescence-inducing hormone abscisic acid (ABA) (PubMed:25516602). Involved in the control of dehydration in senescing leaves. Binds to the DNA sequence 5'-CACGTAAGT-3' of SAG113 promoter. SAG113 acts as a negative regulator of ABA signaling for stomatal closure in leaves, and controls water loss during leaf senescence (PubMed:22184656). Transcription factor of the NAC family involved in senescence. May function in the transition between active cell division and cell expansion (PubMed:16640597). Required for normal seed development and morphology (PubMed:18849494). {ECO:0000269|PubMed:16640597, ECO:0000269|PubMed:18849494, ECO:0000269|PubMed:22184656, ECO:0000269|PubMed:25516602}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49326
|
JAL21_ARATH
|
MVQKVEARGGEIGDVWDDGAYDGVRKVYVGQGEDGIAFVKFEYVNGSQEVVGDERGKKTLLGAEEFEVDPDDYIVYVEGYHEKVFGVTTKEIISTLTFKTYKGKTSPPFGIVSGTKFVLQGGKIVGFHGRSTDVLHSLGAYISSPATPKLRGKWIKVEQKGEGPGPRCSHDIAQVGNKIFSFGGELTPNQPIDKHLYVFDLETRTWSISPATGDVPNLSCLGVRMVSIGSSLYVFGGRDASRKYNGFYSFDTTKNEWKLLTPVEQGPTPRSFHSMTADENNVYVFGGVSATVRLKTLDAYNIVDHKWVQCSTPGGSCSVRGGAGLEVVQGKVWVVYGFNGCEVDDVHCYDPAQDKWTQVETFGEKPCARSVFASAVVGKHILVFGGEIAMDPKAHEGPGQLSGGTFALDTETLKWEKLDKLGEEEETPSIRGWSASTTGTIDGKKGLVMFGGKAQTNDRFGDLFFYGVDSA
|
4.8.1.5
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:19224919, ECO:0000269|PubMed:22954730};
|
embryo development ending in seed dormancy [GO:0009793]; glucosinolate catabolic process [GO:0019762]; nitrile biosynthetic process [GO:0080028]; seed dormancy process [GO:0010162]; seed germination [GO:0009845]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]
|
carbohydrate binding [GO:0030246]; enzyme regulator activity [GO:0030234]; lyase activity [GO:0016829]; metal ion binding [GO:0046872]
|
PF01419;PF01344;PF13415;
|
2.100.10.30;2.120.10.80;
|
Jacalin lectin family
| null | null |
CATALYTIC ACTIVITY: Reaction=a (Z)-N-(sulfonatooxy)alkanimidothioate = a nitrile + sulfate + sulfur; Xref=Rhea:RHEA:59956, ChEBI:CHEBI:16189, ChEBI:CHEBI:18379, ChEBI:CHEBI:26833, ChEBI:CHEBI:183089; EC=4.8.1.5; Evidence={ECO:0000269|PubMed:18987211, ECO:0000269|PubMed:19224919, ECO:0000269|PubMed:22954730}; CATALYTIC ACTIVITY: Reaction=(Z)-phenyl-N-(sulfonatooxy)methanimidothioate = phenylacetonitrile + sulfate + sulfur; Xref=Rhea:RHEA:69308, ChEBI:CHEBI:16189, ChEBI:CHEBI:25979, ChEBI:CHEBI:26833, ChEBI:CHEBI:183061; Evidence={ECO:0000269|PubMed:19224919}; CATALYTIC ACTIVITY: Reaction=(Z)-N-(sulfonatooxy)prop-2-enimidothioate = but-3-enenitrile + sulfate + sulfur; Xref=Rhea:RHEA:69276, ChEBI:CHEBI:16189, ChEBI:CHEBI:26833, ChEBI:CHEBI:183062, ChEBI:CHEBI:183063; Evidence={ECO:0000269|PubMed:19224919}; CATALYTIC ACTIVITY: Reaction=(Z)-(indol-3-yl)-N-(sulfonatooxy)methanimidothioate = (indol-3-yl)acetonitrile + sulfate + sulfur; Xref=Rhea:RHEA:76227, ChEBI:CHEBI:16189, ChEBI:CHEBI:17566, ChEBI:CHEBI:26833, ChEBI:CHEBI:195189; Evidence={ECO:0000269|PubMed:19224919, ECO:0000269|PubMed:22954730};
| null | null | null | null |
FUNCTION: Specifier protein responsible for constitutive and herbivore-induced simple nitrile formation, especially in seeds (PubMed:27990154). Promotes simple nitriles, but not epithionitrile or thiocyanate formation (PubMed:18987211, PubMed:19224919). Converts allylglucosinolate (allyl-GSL), 2-propenylglucosinolate (sinigrin), indol-3-ylmethylglucosinolate (glucobrassicin), benzylisothiocyanate and benzylglucosinolate (glucotropaeolin) to their corresponding simple nitriles in the presence of myrosinase (PubMed:18987211, PubMed:19224919, PubMed:22954730). Catalyzes mainly the conversion of benzylisothiocyanate when benzylglucosinolate is used as the initial substrate of myrosinase (PubMed:19224919, PubMed:22954730). Involved in the regulation of glucosinolate content in seeds, during stratification and germination (PubMed:31850033). {ECO:0000269|PubMed:18987211, ECO:0000269|PubMed:19224919, ECO:0000269|PubMed:22954730, ECO:0000269|PubMed:27990154, ECO:0000269|PubMed:31850033}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49339
|
PTI12_ARATH
|
MRRWICCGDKKGDSDLSNEEVHLKSPWQNSEANQKNQKPQAVVKPEAQKEALPIEVPPLSVDEVKEKTDNFGSKSLIGEGSYGRVYYATLNDGKAVALKKLDVAPEAETNTEFLNQVSMVSRLKHENLIQLVGYCVDENLRVLAYEFATMGSLHDILHGRKGVQGAQPGPTLDWLTRVKIAVEAARGLEYLHEKVQPPVIHRDIRSSNVLLFEDYQAKVADFNLSNQAPDNAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVTWATPRLSEDKVKQCVDPKLKGEYPPKSVAKLAAVAALCVQYESEFRPNMSIVVKALQPLLKPPAPAPAPVPES
|
2.7.10.2
| null |
defense response [GO:0006952]; phosphorylation [GO:0016310]
|
peroxisome [GO:0005777]; plasmodesma [GO:0009506]
|
ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein kinase binding [GO:0019901]
|
PF07714;
|
1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family
|
PTM: Autophosphorylated and phosphorylated by OXI1. {ECO:0000269|PubMed:17040918}.
| null |
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Probable tyrosine-protein kinase involved in oxidative burst-mediated signaling leading to specific genes expression. {ECO:0000269|PubMed:17040918}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49354
|
COQ3_ARATH
|
MLASVRVNQLQRLLLSARRLSSSPIIPPSRLLHQRLFSTSDTDASAASFSSSHPKIQTLEGKASNKSRSTSSTTSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHFSKDPSSAKPFEGLKFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIARLHADMDPVTSTIEYLCTTAEKLADEGRKFDAVLSLEVIEHVANPAEFCKSLSALTIPNGATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEEMSMILQRASVDVKEIAGFVYNPITGRWLLSDDISVNYIAYGTKRKDLGDI
|
2.1.1.114; 2.1.1.64
| null |
methylation [GO:0032259]; ubiquinone biosynthetic process [GO:0006744]
|
extrinsic component of mitochondrial inner membrane [GO:0031314]; mitochondrial envelope [GO:0005740]
|
2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity [GO:0008425]; 3,4-dihydroxy-5-polyprenylbenzoic acid O-methyltransferase activity [GO:0010420]; 3-demethylubiquinol-n 3-O-methyltransferase activity [GO:0061542]
|
PF08241;
|
3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, UbiG/COQ3 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03190, ECO:0000305|PubMed:25732537}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03190}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03190}.
|
CATALYTIC ACTIVITY: Reaction=3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44452, Rhea:RHEA-COMP:10930, Rhea:RHEA-COMP:10931, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64694, ChEBI:CHEBI:84443; EC=2.1.1.114; Evidence={ECO:0000255|HAMAP-Rule:MF_03190}; CATALYTIC ACTIVITY: Reaction=a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44380, Rhea:RHEA-COMP:9566, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:15378, ChEBI:CHEBI:17976, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:84422; EC=2.1.1.64; Evidence={ECO:0000255|HAMAP-Rule:MF_03190};
| null |
PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03190}.
| null | null |
FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. {ECO:0000255|HAMAP-Rule:MF_03190}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49394
|
C82C2_ARATH
|
MDTSLFSLFVPILVFVFIALFKKSKKPKHVKAPAPSGAWPIIGHLHLLSGKEQLLYRTLGKMADQYGPAMSLRLGSSETFVVSSFEVAKDCFTVNDKALASRPITAAAKHMGYDCAVFGFAPYSAFWREMRKIATLELLSNRRLQMLKHVRVSEISMVMQDLYSLWVKKGGSEPVMVDLKSWLEDMSLNMMVRMVAGKRYFGGGSLSPEDAEEARQCRKGVANFFHLVGIFTVSDAFPKLGWFDFQGHEKEMKQTGRELDVILERWIENHRQQRKVSGTKHNDSDFVDVMLSLAEQGKFSHLQHDAITSIKSTCLALILGGSETSPSTLTWAISLLLNNKDMLKKAQDEIDIHVGRDRNVEDSDIENLVYIQAIIKETLRLYPAGPLLGHREAIEDCTVAGYNVRRGTRMLVNVWKIQRDPRVYMEPNEFRPERFITGEAKEFDVRGQNFELMPFGSGRRSCPGSSLAMQVLHLGLARFLQSFDVKTVMDMPVDMTESPGLTIPKATPLEILISPRLKEGLYV
|
1.14.14.-; 1.14.14.165
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
|
cellular response to hypoxia [GO:0071456]; defense response [GO:0006952]
|
membrane [GO:0016020]
|
heme binding [GO:0020037]; indole-3-carbonyl nitrile 4-hydroxylase activity [GO:0106149]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=O2 + reduced [NADPH--hemoprotein reductase] + xanthotoxin = 5-hydroxyxanthotoxin + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:58064, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18358, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78326; Evidence={ECO:0000269|PubMed:18291319}; CATALYTIC ACTIVITY: Reaction=indole-3-carbonyl nitrile + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxy-indole-3-carbonyl nitrile + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:57864, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142138, ChEBI:CHEBI:142139; EC=1.14.14.165; Evidence={ECO:0000269|PubMed:26352477};
| null | null | null | null |
FUNCTION: Involved in the biosynthetic pathway to 4-hydroxyindole-3-carbonyl nitrile (4-OH-ICN), a cyanogenic metabolite required for inducible pathogen defense. Converts indole-3-carbonyl nitrile (ICN) into 4-OH-ICN (PubMed:26352477). Can hydroxylate xanthotoxin (8-methoxypsoralen) to form 5-hydroxyxanthotoxin (5-hydroxy-8-methoxypsoralen) in vivo and in vitro (PubMed:18291319). {ECO:0000269|PubMed:18291319, ECO:0000269|PubMed:26352477}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49397
|
ARR10_ARATH
|
MTMEQEIEVLDQFPVGMRVLAVDDDQTCLRILQTLLQRCQYHVTTTNQAQTALELLRENKNKFDLVISDVDMPDMDGFKLLELVGLEMDLPVIMLSAHSDPKYVMKGVKHGACDYLLKPVRIEELKNIWQHVVRKSKLKKNKSNVSNGSGNCDKANRKRKEQYEEEEEEERGNDNDDPTAQKKPRVLWTHELHNKFLAAVDHLGVERAVPKKILDLMNVDKLTRENVASHLQKFRVALKKVSDDAIQQANRAAIDSHFMQMNSQKGLGGFYHHHRGIPVGSGQFHGGTTMMRHYSSNRNLGRLNSLGAGMFQPVSSSFPRNHNDGGNILQGLPLEELQINNNINRAFPSFTSQQNSPMVAPSNLLLLEGNPQSSSLPSNPGFSPHFEISKRLEHWSNAALSTNIPQSDVHSKPDTLEWNAFCDSASPLVNPNLDTNPASLCRNTGFGSTNAAQTDFFYPLQMNQQPANNSGPVTEAQLFRSSNPNEGLLMGQQKLQSGLMASDAGSLDDIVNSLMTQEQSQSDFSEGDWDLDGLAHSEHAYEKLHFPFSLSA
| null | null |
callus formation [GO:1990110]; cellular response to cytokinin stimulus [GO:0071368]; cytokinin-activated signaling pathway [GO:0009736]; maintenance of shoot apical meristem identity [GO:0010492]; primary root development [GO:0080022]; regulation of anthocyanin metabolic process [GO:0031537]; regulation of chlorophyll biosynthetic process [GO:0010380]; regulation of cytokinin-activated signaling pathway [GO:0080036]; regulation of root meristem growth [GO:0010082]; regulation of seed growth [GO:0080113]; response to cytokinin [GO:0009735]; response to water deprivation [GO:0009414]; root development [GO:0048364]; shoot system development [GO:0048367]
|
nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; phosphorelay response regulator activity [GO:0000156]
|
PF00249;PF00072;
|
3.40.50.2300;1.10.10.60;
|
ARR family, Type-B subfamily
|
PTM: Two-component system major event consists of a His-to-Asp phosphorelay between a sensor histidine kinase (HK) and a response regulator (RR). In plants, the His-to-Asp phosphorelay involves an additional intermediate named Histidine-containing phosphotransfer protein (HPt). This multistep phosphorelay consists of a His-Asp-His-Asp sequential transfer of a phosphate group between first an His and an Asp of the HK protein, followed by the transfer to a conserved His of the HPt protein and finally the transfer to an Asp in the receiver domain of the RR protein.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:12215502}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]GATT-3'. Functions as a response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Could directly activate some type-A response regulators in response to cytokinins. {ECO:0000269|PubMed:11574878}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49403
|
HFA4A_ARATH
|
MDENNHGVSSSSLPPFLTKTYEMVDDSSSDSIVSWSQSNKSFIVWNPPEFSRDLLPRFFKHNNFSSFIRQLNTYGFRKADPEQWEFANDDFVRGQPHLMKNIHRRKPVHSHSLPNLQAQLNPLTDSERVRMNNQIERLTKEKEGLLEELHKQDEEREVFEMQVKELKERLQHMEKRQKTMVSFVSQVLEKPGLALNLSPCVPETNERKRRFPRIEFFPDEPMLEENKTCVVVREEGSTSPSSHTREHQVEQLESSIAIWENLVSDSCESMLQSRSMMTLDVDESSTFPESPPLSCIQLSVDSRLKSPPSPRIIDMNCEPDGSKEQNTVAAPPPPPVAGANDGFWQQFFSENPGSTEQREVQLERKDDKDKAGVRTEKCWWNSRNVNAITEQLGHLTSSERS
| null | null |
cellular response to heat [GO:0034605]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to reactive oxygen species [GO:0000302]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976]
|
PF00447;
|
1.10.10.10;
|
HSF family, Class A subfamily
|
PTM: Exhibits temperature-dependent phosphorylation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49429
|
MORF1_ARATH
|
MAMISHRLRRALLTATSYVNRSISSSITPASDFPSVSAAVLKRSVIGRSTEVATRAPARLFSTRQYKLYKEGDEITEDTVLFEGCDYNHWLITMDFSKEETPKSPEEMVAAYEETCAQGLGISVEEAKQRMYACSTTTYQGFQAIMTEQESEKFKDLPGVVFILPDSYIDPQNKEYGGDKYENGVITHRPPPIQSGRARPRPRFDRSGGGSGGPQNFQRNTQYGQQPPMQGGGGSYGPQQGYATPGQGQGTQAPPPFQGGYNQGPRSPPPPYQAGYNQGQGSPVPPYQAGYNQVQGSPVPPYQGTQSSYGQGGSGNYSQGPQGGYNQGGPRNYNPQGAGNFGPASGAGNLGPAPGAGNPGYGQGYSGPGQEQNQTFPQADQRNRDWNNNNPAGQPGSDQVRSRSIMNLASFFFDILIRH
| null | null |
chloroplast RNA modification [GO:1900865]; cytidine to uridine editing [GO:0016554]; mitochondrial mRNA modification [GO:0080156]; mitochondrial RNA modification [GO:1900864]; mRNA processing [GO:0006397]
|
chloroplast [GO:0009507]; mitochondrion [GO:0005739]
|
protein dimerization activity [GO:0046983]
| null |
3.30.70.80;
|
MORF family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25583991}.
| null | null | null | null | null |
FUNCTION: Involved in organellar RNA editing. Required for the processing of numerous RNA editing sites in mitochondria (PubMed:22411807, PubMed:23818871). Binds to the mitochondrial MEF19 and MEF21 factors, two pentatricopeptide repeat-containing proteins involved in RNA editing (PubMed:22411807). {ECO:0000269|PubMed:22411807, ECO:0000269|PubMed:23818871}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49432
|
QRT3_ARATH
|
MELRKSQVAMPVFLAIMSLMVSQVVFAEKDSGSMSPHDRALAEMQALKASLVRRNLPALVSPPPTPPQAVPGPRVYQVISYGADPTGKLDSTDAILKAMEEAFDGPNHGVLMQGINDLGGARIDLQGGSYLISRPLRFPSAGAGNLLISGGTLRASNDFPVDRYLIELKDESSKLQYIFEYITLRDLLIDCNYRGGAIAVINSLRTSIDNCYITRFGDTNGILVKSGHETYIRNSFLGQHITAGGDRGERSFSGTAINLMGNDNAVTDTVIFSARIGVMVSGQANLLSGVHCYNKATGFGGTGIYLRLPGLTQNRIVNSYLDYTGIVAEDPVQLQISGTFFLGDAFILLKSIAGYIRGVSIVDNMFSGSGHGVQIVQLDQRNTAFDDVGQVVVDRNSVNGMVEKSTVARGSVDGNGTSWTVDFNPVLLFPDLINHVQYTLVASEAGVFPLHALRNVSDNRVVVETNAPVTGTVYVTVNQGV
|
3.2.1.15
| null |
cell wall organization [GO:0071555]; metabolic process [GO:0008152]; microsporogenesis [GO:0009556]; pollen exine formation [GO:0010584]
|
extracellular region [GO:0005576]
|
polygalacturonase activity [GO:0004650]
| null |
2.160.20.10;
|
Glycosyl hydrolase 28 family
| null |
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:14551328}.
|
CATALYTIC ACTIVITY: Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
| null | null | null | null |
FUNCTION: Polygalacturonase required for degrading the pollen mother cell wall during microspore development. {ECO:0000269|PubMed:14551328}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49434
|
AAH_ARATH
|
MAVPHPSSSSSRSHPFLSHVYHTSFHHHHHHNHPSLVLFWCLVFSLLSPLALSSSSSSSSSSSDSSSSSSSHISLGIGETEGTKHDLHQAILRDEAVARLHELGQVSDAATHLERTFMSPASIRAIPLIRGWMEDAGLSTWVDYMGNVHGRVEPKNGSSQALLIGSHMDTVIDAGKYDGSLGIISAISALKVLKIDGRLGELKRPVEVIAFSDEEGVRFQSTFLGSAALAGIMPVSRLEVTDKSGISVQDALKENSIDITDENLMQLKYDPASVWGYVEVHIEQGPVLEWVGYPLGVVKGIAGQTRLKVTVKGSQGHAGTVPMSMRQDPMTGAAELIVLLESVCKNPKDYLSCNVQCNEDTVESLANSLVCTVGEISTWPSASNVIPGQVTFTVDLRTIDDVGRKAILHDLSTRMYQICDKRSLLCSIERKHDADAVMSDPQLSLQLKSAAQSALKKMTGEVQDEVPVLMSGAGHDAMAMAHLTKVGMLFVRCRGGISHSPAEHVLDDDVGAAGLAILEFLESQM
|
3.5.3.9
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:18065556}; Note=Binds 2 manganese ions per subunit. {ECO:0000250|UniProtKB:Q8VXY9};
|
purine nucleobase catabolic process [GO:0006145]; ureide catabolic process [GO:0010136]
|
endoplasmic reticulum [GO:0005783]
|
allantoate deiminase activity [GO:0047652]; metal ion binding [GO:0046872]
|
PF07687;PF01546;
|
3.30.70.360;3.40.630.10;
|
Peptidase M20A family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:18065556}.
|
CATALYTIC ACTIVITY: Reaction=allantoate + 2 H(+) + H2O = (S)-2-ureidoglycine + CO2 + NH4(+); Xref=Rhea:RHEA:27485, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17536, ChEBI:CHEBI:28938, ChEBI:CHEBI:59947; EC=3.5.3.9; Evidence={ECO:0000269|PubMed:16496096, ECO:0000269|PubMed:18065556};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 27.2 sec(-1) for allantoate. {ECO:0000269|PubMed:18065556};
| null | null | null |
FUNCTION: Involved in the catabolism of purine nucleotides. Can use allantoate as substrate, but not Nalpha-carbamoyl-L-Asp, Nalpha-carbamoyl-L-Ala or Nalpha-carbamoyl-Gly. The sequential activity of AAH, UGLYAH and UAH allows a complete purine breakdown without the intermediate generation of urea (PubMed:16496096, PubMed:18065556, PubMed:19935661, PubMed:23940254). Involved in the regulation of seed maturation and seed dormancy (PubMed:35861030). {ECO:0000269|PubMed:16496096, ECO:0000269|PubMed:18065556, ECO:0000269|PubMed:19935661, ECO:0000269|PubMed:23940254, ECO:0000269|PubMed:35861030}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49447
|
ADT3_ARATH
|
MDGSKHPSVFQKLHGQSYLINRLSPSVQARGYCVSGAYVNGGLQSLLQPTSHGVGSSLIPHGSFPVLAHAPSEKTGTGFLIDFLMGGVSAAVSKTAAAPIERVKLLIQNQDEMIKAGRLSEPYKGISDCFARTVKDEGMLALWRGNTANVIRYFPTQALNFAFKDYFKRLFNFKKEKDGYWKWFAGNLASGGAAGASSLLFVYSLDYARTRLANDAKAAKKGGQRQFNGMVDVYKKTIASDGIVGLYRGFNISCVGIVVYRGLYFGLYDSLKPVVLVDGLQDSFLASFLLGWGITIGAGLASYPIDTVRRRMMMTSGEAVKYKSSLQAFSQIVKNEGAKSLFKGAGANILRAVAGAGVLAGYDKLQLIVLGKKYGSGGG
| null | null |
mitochondrial ADP transmembrane transport [GO:0140021]; mitochondrial ATP transmembrane transport [GO:1990544]; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901029]; purine nucleotide transport [GO:0015865]
|
chloroplast envelope [GO:0009941]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
ATP:ADP antiporter activity [GO:0005471]
|
PF00153;
|
1.50.40.10;
|
Mitochondrial carrier (TC 2.A.29) family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:14671022}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P48962}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000; Evidence={ECO:0000250|UniProtKB:P48962};
| null | null | null | null |
FUNCTION: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity). {ECO:0000250|UniProtKB:G2QNH0, ECO:0000250|UniProtKB:P48962}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49472
|
INDH_ARATH
|
MATVALLRSLRRRELHAAHISAYKFSSASAGGRTTELRLHGVKDIIAVASGKGGVGKSSTAVNLAVALANKCELKIGLLDADVYGPSVPIMMNINQKPQVNQDMKMIPVENYGVKCMSMGLLVEKDAPLVWRGPMVMSALAKMTKGVDWGDLDILVVDMPPGTGDAQISISQNLKLSGAVIVSTPQDVALADANRGISMFDKVRVPILGLVENMSCFVCPHCNEPSFIFGKEGARRTAAKKGLKLIGEIPLEMSIREGSDEGVPVVVSSPGSIVSKAYQDLAQNVVKGLKELRENPDNEIQMKLNVPHSSHSS
| null |
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:Q6CE48}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q6CE48};
|
iron-sulfur cluster assembly [GO:0016226]; mitochondrial respiratory chain complex I assembly [GO:0032981]; mitochondrial translation [GO:0032543]
|
chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; ATP-dependent FeS chaperone activity [GO:0140663]; metal ion binding [GO:0046872]
|
PF10609;
|
3.40.50.300;
|
Mrp/NBP35 ATP-binding proteins family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:24179128}.
| null | null | null | null | null |
FUNCTION: Essential during early vegetative growth (PubMed:24179128). Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) (PubMed:24179128). Involved in mitochondrial translation activity (PubMed:24179128). May deliver of one or more Fe-S clusters to complex I subunits (By similarity). {ECO:0000250|UniProtKB:Q8TB37, ECO:0000269|PubMed:24179128}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49482
|
CADH5_ARATH
|
MGIMEAERKTTGWAARDPSGILSPYTYTLRETGPEDVNIRIICCGICHTDLHQTKNDLGMSNYPMVPGHEVVGEVVEVGSDVSKFTVGDIVGVGCLVGCCGGCSPCERDLEQYCPKKIWSYNDVYINGQPTQGGFAKATVVHQKFVVKIPEGMAVEQAAPLLCAGVTVYSPLSHFGLKQPGLRGGILGLGGVGHMGVKIAKAMGHHVTVISSSNKKREEALQDLGADDYVIGSDQAKMSELADSLDYVIDTVPVHHALEPYLSLLKLDGKLILMGVINNPLQFLTPLLMLGRKVITGSFIGSMKETEEMLEFCKEKGLSSIIEVVKMDYVNTAFERLEKNDVRYRFVVDVEGSNLDA
|
1.1.1.195
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16633561}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:16633561};
|
lignin biosynthetic process [GO:0009809]
|
cytosol [GO:0005829]
|
cinnamyl-alcohol dehydrogenase activity [GO:0045551]; coniferyl-alcohol dehydrogenase activity [GO:0050268]; sinapyl alcohol dehydrogenase activity [GO:0052747]; zinc ion binding [GO:0008270]
|
PF08240;PF00107;
|
3.90.180.10;3.40.50.720;
|
Zinc-containing alcohol dehydrogenase family
| null | null |
CATALYTIC ACTIVITY: Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) + NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731, ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.195; Evidence={ECO:0000269|PubMed:14745009}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10394; Evidence={ECO:0000269|PubMed:14745009}; CATALYTIC ACTIVITY: Reaction=(E)-coniferol + NADP(+) = (E)-coniferaldehyde + H(+) + NADPH; Xref=Rhea:RHEA:22444, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547, ChEBI:CHEBI:17745, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.195; Evidence={ECO:0000269|PubMed:14745009}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22446; Evidence={ECO:0000269|PubMed:14745009}; CATALYTIC ACTIVITY: Reaction=(E)-sinapyl alcohol + NADP(+) = (E)-sinapaldehyde + H(+) + NADPH; Xref=Rhea:RHEA:45704, ChEBI:CHEBI:15378, ChEBI:CHEBI:27949, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64557; EC=1.1.1.195; Evidence={ECO:0000269|PubMed:14745009}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45706; Evidence={ECO:0000269|PubMed:14745009}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumaroyl alcohol + NADP(+) = (E)-4-coumaraldehyde + H(+) + NADPH; Xref=Rhea:RHEA:45724, ChEBI:CHEBI:15378, ChEBI:CHEBI:28353, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64555; EC=1.1.1.195; Evidence={ECO:0000269|PubMed:14745009}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45726; Evidence={ECO:0000269|PubMed:14745009}; CATALYTIC ACTIVITY: Reaction=(E)-caffeyl alcohol + NADP(+) = (E)-caffeyl aldehyde + H(+) + NADPH; Xref=Rhea:RHEA:45728, ChEBI:CHEBI:15378, ChEBI:CHEBI:28323, ChEBI:CHEBI:31334, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:14745009}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45730; Evidence={ECO:0000269|PubMed:14745009};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for 4-coumaraldehyde (at pH 6.25-6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009}; KM=68 uM for caffeyl aldehyde (at pH 6.0-6.25 and 30-35 degrees Celsius) {ECO:0000269|PubMed:14745009}; KM=35 uM for coniferaldehyde (at pH 6.0-6.25 and 30-35 degrees Celsius) {ECO:0000269|PubMed:14745009}; KM=22 uM for 5-hydroxyconiferaldehyde (at pH 6.25-6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009}; KM=20 uM for sinapaldehyde (at pH 6.0-6.25 and 30-35 degrees Celsius) {ECO:0000269|PubMed:14745009}; Vmax=187.3 pmol/sec/ug enzyme with 4-coumaraldehyde as substrate (at pH 6.25-6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009}; Vmax=94.1 pmol/sec/ug enzyme with caffeyl aldehyde as substrate (at pH 6.0-6.25 and 30-35 degrees Celsius) {ECO:0000269|PubMed:14745009}; Vmax=157.4 pmol/sec/ug enzyme with coniferaldehyde as substrate (at pH 6.0-6.25 and 30-35 degrees Celsius) {ECO:0000269|PubMed:14745009}; Vmax=106.9 pmol/sec/ug enzyme with 5-hydroxyconiferaldehyde as substrate (at pH 6.25-6.5 and 30 degrees Celsius) {ECO:0000269|PubMed:14745009}; Vmax=177 pmol/sec/ug enzyme with sinapaldehyde as substrate (at pH 6.0-6.25 and 30-35 degrees Celsius) {ECO:0000269|PubMed:14745009};
|
PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000305|PubMed:14745009}.
| null | null |
FUNCTION: Involved in lignin biosynthesis in the floral stem. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols. {ECO:0000269|PubMed:12805615, ECO:0000269|PubMed:14745009, ECO:0000269|PubMed:15937231}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49484
|
ASK11_ARATH
|
MSSKMIVLMSSDGQSFEVEEAVAIQSQTIAHMVEDDCVADGIPLANVESKILVKVIEYCKKHHVDEANPISEEDLNNWDEKFMDLEQSTIFELILAANYLNIKSLLDLTCQTVADMIKGKTPEEIRSTFNIENDFTPEEEEAVRKENQWAFE
| null | null |
auxin-activated signaling pathway [GO:0009734]; jasmonic acid mediated signaling pathway [GO:0009867]; protein ubiquitination [GO:0016567]; response to auxin [GO:0009733]; response to jasmonic acid [GO:0009753]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; SCF ubiquitin ligase complex [GO:0019005]
|
cullin family protein binding [GO:0097602]
|
PF01466;PF03931;
| null |
SKP1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
| null | null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1 (By similarity). Plays a role during early flowers reproductive development. {ECO:0000250, ECO:0000269|PubMed:12970487}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49485
|
SERA1_ARATH
|
MSATAAASSSIAVATNSLRNVTLSSRSPLPSAISVAFPSRGRNTLQRRLVLVSCSTGDGSKPTILVAEKLGDAGIKLLEDVANVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESSHGRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKEPPAKDSKLVQHERVTVTPHLGASTMEAQEGVAIEIAEAVVGALNGELAATAVNAPMVSAEVLTELKPYVVLAEKLGRLAVQLVAGGSGVKNAKITYASARATDDLDTRLLRAMITKGIIEPISDVYVNLVNADFTAKQRGLRLSEERVLLDGSPESPLETITVQLSNVESKFASSLSESGEVKVEGKVKDGVPHLTKVGSFEVDVTLEGSIILCRQVDQPGMIGTVGSILGESNVNVNFMSVGRIAPRKQAIMAIGVDDIPSKETLKKIGEIPAVEEFVFLKL
|
1.1.1.95
| null |
embryo development ending in seed dormancy [GO:0009793]; L-serine biosynthetic process [GO:0006564]; megagametogenesis [GO:0009561]; pollen development [GO:0009555]; sulfur amino acid metabolic process [GO:0000096]
|
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; plastid [GO:0009536]
|
ATP binding [GO:0005524]; NAD binding [GO:0051287]; phosphoglycerate dehydrogenase activity [GO:0004617]
|
PF00389;PF02826;PF01842;PF19304;
|
3.30.70.260;3.40.50.720;
|
D-isomer specific 2-hydroxyacid dehydrogenase family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24058165, ECO:0000269|PubMed:24368794}.
|
CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95; Evidence={ECO:0000269|PubMed:24368794};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.308 mM for 3-phospho-D-glycerate (at pH 8.1) {ECO:0000269|PubMed:24368794}; KM=0.39 mM for NAD(+) (at pH 8.1) {ECO:0000269|PubMed:24368794}; KM=2.11 mM for 3-phospho-D-glycerate (at pH 7.2) {ECO:0000269|PubMed:24368794}; KM=0.377 mM for NAD(+) (at pH 7.2) {ECO:0000269|PubMed:24368794}; Vmax=165 umol/min/mg enzyme (at pH 8.1) {ECO:0000269|PubMed:24368794}; Vmax=109.1 umol/min/mg enzyme (at pH 7.2) {ECO:0000269|PubMed:24368794};
|
PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
| null | null |
FUNCTION: Involved in the plastidial phosphorylated pathway of serine biosynthesis (PPSB). Required for mature pollen development. {ECO:0000269|PubMed:24058165, ECO:0000269|PubMed:24368794}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49499
|
CAMT4_ARATH
|
MATTTTEATKTSSTNGEDQKQSQNLRHQEVGHKSLLQSDDLYQYILETSVYPREPESMKELREVTAKHPWNIMTTSADEGQFLNMLIKLVNAKNTMEIGVYTGYSLLATALALPEDGKILAMDVNRENYELGLPIIEKAGVAHKIDFREGPALPVLDEIVADEKNHGTYDFIFVDADKDNYINYHKRLIDLVKIGGVIGYDNTLWNGSVVAPPDAPMRKYVRYYRDFVLELNKALAADPRIEICMLPVGDGITICRRIS
|
2.1.1.104
|
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:Q40313}; Note=Binds 1 divalent metal cation per subunit. {ECO:0000250|UniProtKB:Q40313};
|
coumarin biosynthetic process [GO:0009805]; lignin biosynthetic process [GO:0009809]; methylation [GO:0032259]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
caffeoyl-CoA O-methyltransferase activity [GO:0042409]; metal ion binding [GO:0046872]
|
PF01596;
|
3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family, CCoAMT subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=(E)-caffeoyl-CoA + S-adenosyl-L-methionine = (E)-feruloyl-CoA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16925, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87136, ChEBI:CHEBI:87305; EC=2.1.1.104; Evidence={ECO:0000269|PubMed:18547395};
| null |
PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
| null | null |
FUNCTION: Methylates caffeoyl-CoA to feruloyl-CoA. Has a very low activity with caffeic acid and esculetin. Involved in scopoletin biosynthesis in roots. {ECO:0000269|PubMed:17594112, ECO:0000269|PubMed:18547395, ECO:0000269|PubMed:22258746}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49500
|
MBR2_ARATH
|
MQGPRSTGDSSTGINYADGEPICSTNSETTSNNILNPVDVQFPNNTTGSGRPTYASSSSHVVQNHNWWSFGESSSRLGPSDHLNSNGSKTDRQLLSDGYGFEEGQSGMLLPGESFLRGSSSSHMLSHVNLGKDMDIGSGLQTSGVVIRHNNCETSLGSSSQTAEERSSGPGSSLGGLGSSCKRKALEGAPSHSFPGESHGCFFQTENGAWNEGLAQYDASSSLSLSMPSQNSPNVNNQSGLPEPRFGLGGGRAVTASAFPSTRSTETISRPGRRLNPGQPPESVAFSFTQSGSSVRQQQQLPATSPFVDPLDARAIPVTGSSSSGDGQPSMIHLPALTRNIHQFAWSASSSSRANSMPEEGLSPWDAPRINSEQPVFTTPANETRNPVQDQFCWSFTRGNPSTSGDSPFVPRAGSSSGIHGLQPNPTWVTPHNQSRISEVAPWSLFPSIESESATHGASLPLLPTGPSVSSNEAAAPSGSSSRSHRSRQRRSGLLLERQNDHLHLRHLGRSLAADNDGRNRLISEIRQVLSAMRRGENLRFEDYMVFDPLIYQGMAEMHDRHRDMRLDVDNMSYEELLALGERIGDVSTGLSEEVILKVMKQHKHTSSAAGSHQDMEPCCVCQEEYAEGDDLGTLGCGHEFHTACVKQWLMLKNLCPICKTVALST
|
2.3.2.27
| null |
flower development [GO:0009908]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; vegetative to reproductive phase transition of meristem [GO:0010228]
| null |
metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]
|
PF13639;
|
3.30.40.10;
|
RING-type zinc finger family
| null | null |
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase that functions as a regulator of MED25 stability by targeting MED25 for degradation in a RING-H2-dependent way. Proteasome-dependent degradation of MED25 seems to activate its function as positive regulator of FLOWERING LOCUS T (FT) and is important to induce the expression of FT and consequently to promote flowering. May function downstream of HAL3 and be required for HAL3-regulated plant growth. Activation of MBR2 by HAL3 may lead to the degradation of cell cycle suppressors, resulting in enhancement of cell division and plant growth. {ECO:0000269|PubMed:19543273, ECO:0000269|PubMed:22992513}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49506
|
GLO5_ARATH
|
MEITNVMEYEKIAKEKLPKMVYDYYASGAEDQWTLQENRNAFSRILFRPRILIDVSKIDVSTTVLGFNISMPIMIAPTAMQKMAHPDGELATARATSAAGTIMTLSSWATCSVEEVASTGPGIRFFQLYVYKDRNVVIQLVKRAEEAGFKAIALTVDTPRLGRRESDIKNRFALPRGLTLKNFEGLDLGKIDKTNDSGLASYVAGQVDQSLSWKDIKWLQSITSLPILVKGVITAEDARIAVEYGAAGIIVSNHGARQLDYVPATIVALEEVVKAVEGRIPVFLDGGVRRGTDVFKALALGASGVFVGRPSLFSLAADGEAGVRKMLQMLRDEFELTMALSGCRSLREISRTHIKTDWDTPHYLSAKL
|
1.1.3.15
|
COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05414};
|
defense response to bacterium [GO:0042742]; fatty acid alpha-oxidation [GO:0001561]; hydrogen peroxide biosynthetic process [GO:0050665]; lactate oxidation [GO:0019516]; oxidative photosynthetic carbon pathway [GO:0009854]
|
peroxisome [GO:0005777]; plasma membrane [GO:0005886]
|
(S)-2-hydroxy-acid oxidase activity [GO:0003973]; FMN binding [GO:0010181]; L-lactate dehydrogenase activity [GO:0004459]
|
PF01070;
|
3.20.20.70;
|
FMN-dependent alpha-hydroxy acid dehydrogenase family
| null |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=glycolate + O2 = glyoxylate + H2O2; Xref=Rhea:RHEA:25311, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29805, ChEBI:CHEBI:36655; EC=1.1.3.15; Evidence={ECO:0000250|UniProtKB:Q9LRR9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312; Evidence={ECO:0000250|UniProtKB:Q9LRR9};
| null |
PATHWAY: Photosynthesis; photorespiration; glycine from 2-phosphoglycolate: step 2/3. {ECO:0000250|UniProtKB:Q9LRR9}.
| null | null |
FUNCTION: Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2. Is a key enzyme in photorespiration in green plants. {ECO:0000250|UniProtKB:Q9LRR9}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49519
|
CLE2_ARATH
|
MAKLSFTFCFLLFLLLSSIAAGSRPLEGARVGVKVRGLSPSIEATSPTVEDDQAAGSHGKSPERLSPGGPDPQHH
| null | null |
cell fate commitment [GO:0045165]; cell-cell signaling [GO:0007267]
|
apoplast [GO:0048046]
|
receptor serine/threonine kinase binding [GO:0033612]
| null | null |
CLV3/ESR signal peptide family
|
PTM: [CLE2p]: The O-glycosylation (arabinosylation) of the hydroxyproline Pro-70 enhances binding affinity of the CLE2p peptide for its receptor. {ECO:0000269|PubMed:19525968}.
|
SUBCELLULAR LOCATION: [CLE2p]: Secreted, extracellular space {ECO:0000269|PubMed:19525968}.
| null | null | null | null | null |
FUNCTION: [CLE2p]: Extracellular signal peptide that regulates cell fate. May act with CLV1 as a ligand-receptor pair in a signal transduction pathway, coordinating growth between adjacent meristematic regions. {ECO:0000269|PubMed:16489133, ECO:0000269|PubMed:19525968}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49523
|
DSEL_ARATH
|
MKRKKKEEEEEKLIVTREFAKRWRDLSGQNHWKGMLQPLDQDLREYIIHYGEMAQAGYDTFNINTESQFAGASIYSRKDFFAKVGLEIAHPYTKYKVTKFIYATSDIHVPESFLLFPISREGWSKESNWMGYVAVTDDQGTALLGRRDIVVSWRGSVQPLEWVEDFEFGLVNAIKIFGERNDQVQIHQGWYSIYMSQDERSPFTKTNARDQVLREVGRLLEKYKDEEVSITICGHSLGAALATLSATDIVANGYNRPKSRPDKSCPVTAFVFASPRVGDSDFRKLFSGLEDIRVLRTRNLPDVIPIYPPIGYSEVGDEFPIDTRKSPYMKSPGNLATFHCLEGYLHGVAGTQGTNKADLFRLDVERAIGLVNKSVDGLKDECMVPGKWRVLKNKGMAQQDDGSWELVDHEIDDNEDLDF
|
3.1.1.-
| null |
diacylglycerol catabolic process [GO:0046340]; lipid storage [GO:0019915]; monoacylglycerol catabolic process [GO:0052651]; negative regulation of seed germination [GO:0010187]
|
cytoplasm [GO:0005737]
|
acylglycerol lipase activity [GO:0047372]; phospholipase A1 activity [GO:0008970]
|
PF01764;
|
3.40.50.1820;
|
AB hydrolase superfamily, Lipase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21477884}.
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-6 with 1,3-DAG as substrate and at 30 degrees Celsius. {ECO:0000269|PubMed:21477884};
| null |
FUNCTION: Acylhydrolase that catalyzes the hydrolysis of 1,3-diacylglycerol (1,3-DAG) and 1-monoacylglycerol (1-MAG) at the sn-1 position. High activity toward 1,3-DAG and 1-MAG, but low activity toward 1,2-diacylglycerol (1,2-DAG) and 1-lysophosphatidylcholine (1-LPC), and no activity toward phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG), triacylglycerol (TAG) and 2-monoacylglycerol (2-MAG). May be involved in the negative regulation of seedling establishment by inhibiting the breakdown, beta-oxidation and mobilization of seed storage oils. {ECO:0000269|PubMed:21477884}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49543
|
MNIF1_ARATH
|
MASKVISATIRRTLTKPHGTFSRCRYLSTAAAATEVNYEDESIMMKGVRISGRPLYLDMQATTPIDPRVFDAMNASQIHEYGNPHSRTHLYGWEAENAVENARNQVAKLIEASPKEIVFVSGATEANNMAVKGVMHFYKDTKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKTDGLVDLEMLREAIRPDTGLVSIMAVNNEIGVVQPMEEIGMICKEHNVPFHTDAAQAIGKIPVDVKKWNVALMSMSAHKIYGPKGVGALYVRRRPRIRLEPLMNGGGQERGLRSGTGATQQIVGFGAACELAMKEMEYDEKWIKGLQERLLNGVREKLDGVVVNGSMDSRYVGNLNLSFAYVEGESLLMGLKEVAVSSGSACTSASLEPSYVLRALGVDEDMAHTSIRFGIGRFTTKEEIDKAVELTVKQVEKLREMSPLYEMVKEGIDIKNIQWSQH
|
2.8.1.7
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:22511606};
|
[2Fe-2S] cluster assembly [GO:0044571]; iron-sulfur cluster assembly [GO:0016226]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plastid [GO:0009536]
|
ATP binding [GO:0005524]; cysteine desulfurase activity [GO:0031071]; iron-sulfur cluster binding [GO:0051536]; pyridoxal phosphate binding [GO:0030170]; zinc ion binding [GO:0008270]
|
PF00266;
|
3.90.1150.10;3.40.640.10;
|
Class-V pyridoxal-phosphate-dependent aminotransferase family, NifS/IscS subfamily
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:17417719}.
|
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:17417719};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=21.2 nmol/min/mg enzyme with cysteine as substrate {ECO:0000269|PubMed:22511606};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000303|PubMed:17417719};
| null |
FUNCTION: Catalyzes the removal of elemental sulfur from cysteine to produce alanine. Supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. {ECO:0000269|PubMed:16437155, ECO:0000269|PubMed:17417719}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49545
|
BAME1_ARATH
|
MKLFLLLLFLLHISHTFTASRPISEFRALLSLKTSLTGAGDDKNSPLSSWKVSTSFCTWIGVTCDVSRRHVTSLDLSGLNLSGTLSPDVSHLRLLQNLSLAENLISGPIPPEISSLSGLRHLNLSNNVFNGSFPDEISSGLVNLRVLDVYNNNLTGDLPVSVTNLTQLRHLHLGGNYFAGKIPPSYGSWPVIEYLAVSGNELVGKIPPEIGNLTTLRELYIGYYNAFEDGLPPEIGNLSELVRFDGANCGLTGEIPPEIGKLQKLDTLFLQVNVFSGPLTWELGTLSSLKSMDLSNNMFTGEIPASFAELKNLTLLNLFRNKLHGEIPEFIGDLPELEVLQLWENNFTGSIPQKLGENGKLNLVDLSSNKLTGTLPPNMCSGNKLETLITLGNFLFGSIPDSLGKCESLTRIRMGENFLNGSIPKGLFGLPKLTQVELQDNYLSGELPVAGGVSVNLGQISLSNNQLSGPLPPAIGNFTGVQKLLLDGNKFQGPIPSEVGKLQQLSKIDFSHNLFSGRIAPEISRCKLLTFVDLSRNELSGEIPNEITAMKILNYLNLSRNHLVGSIPGSISSMQSLTSLDFSYNNLSGLVPGTGQFSYFNYTSFLGNPDLCGPYLGPCKDGVAKGGHQSHSKGPLSASMKLLLVLGLLVCSIAFAVVAIIKARSLKKASESRAWRLTAFQRLDFTCDDVLDSLKEDNIIGKGGAGIVYKGVMPNGDLVAVKRLAAMSRGSSHDHGFNAEIQTLGRIRHRHIVRLLGFCSNHETNLLVYEYMPNGSLGEVLHGKKGGHLHWDTRYKIALEAAKGLCYLHHDCSPLIVHRDVKSNNILLDSNFEAHVADFGLAKFLQDSGTSECMSAIAGSYGYIAPEYAYTLKVDEKSDVYSFGVVLLELVTGRKPVGEFGDGVDIVQWVRKMTDSNKDSVLKVLDPRLSSIPIHEVTHVFYVAMLCVEEQAVERPTMREVVQILTEIPKLPPSKDQPMTESAPESELSPKSGVQSPPDLLNL
|
2.7.11.1
| null |
cell differentiation [GO:0030154]; floral organ development [GO:0048437]; gametophyte development [GO:0048229]; phosphorylation [GO:0016310]; regulation of meristem growth [GO:0010075]; regulation of meristem structural organization [GO:0009934]
|
plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein self-association [GO:0043621]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; receptor serine/threonine kinase binding [GO:0033612]
|
PF00560;PF08263;PF00069;
|
3.80.10.10;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14506206, ECO:0000269|PubMed:20626648}; Single-pass type I membrane protein {ECO:0000269|PubMed:14506206, ECO:0000269|PubMed:20626648}.
|
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: Necessary for male gametophyte development, as well as ovule specification and function. Involved in cell-cell communication process required during early anther development, and regulating cell division and differentiation to organize cell layers. Required for the development of high-ordered vascular strands within the leaf and a correlated control of leaf shape, size and symmetry. May regulate the CLV1-dependent CLV3-mediated signaling in meristems maintenance. {ECO:0000269|PubMed:16367950, ECO:0000269|PubMed:16751349, ECO:0000269|PubMed:18780746}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49562
|
PDRP1_ARATH
|
MALLSAMKLQGRPPPISSNLNPNSKPAGSDSVSLNASEPGSERKPRKFSSQLNRWNRARTLRSGAKLDSTITNGSNNTTGPMRPIESSSRTDVSTLDSDVSSSSNGVSEADMTAAKSIYIVSDGTGWTAEHAVNAALGQFDYCLVDRGCPVNTHLFSGIEDGEKLMEIIKQAAREGAMVIYTLADPSMAEATMRACKLWKIPSLDILGPITESISSHLGTNPSGLSRGITNSSLNEDYFKRIEAIEFTIKHDDGALPENLEKADIVLVGVSRTGKTPLSTYLAQKGYKVSNVPIVNGVDLPKTLFEIDPRKVFGLMINPLVLQGIREARAKSLGLGSSFKTKYSELGSVKEELELAKKIFAENPTWPVIEVTESAIEETAAVVLRLYDERQSNRAMPRISKSY
|
2.7.11.32; 2.7.4.27
| null |
phosphorylation [GO:0016310]
|
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]
|
ATP binding [GO:0005524]; phosphoprotein phosphatase activity [GO:0004721]; phosphotransferase activity, phosphate group as acceptor [GO:0016776]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]
|
PF03618;
| null |
Pyruvate, phosphate/water dikinase regulatory protein family, PDRP subfamily
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:17996018}.
|
CATALYTIC ACTIVITY: Reaction=ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase]; Xref=Rhea:RHEA:43692, Rhea:RHEA-COMP:10650, Rhea:RHEA-COMP:10651, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:61977, ChEBI:CHEBI:83586, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.11.32; Evidence={ECO:0000269|PubMed:21883547}; CATALYTIC ACTIVITY: Reaction=H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-[pyruvate, phosphate dikinase] + phosphate = diphosphate + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase]; Xref=Rhea:RHEA:43696, Rhea:RHEA-COMP:10650, Rhea:RHEA-COMP:10651, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977, ChEBI:CHEBI:83586; EC=2.7.4.27; Evidence={ECO:0000269|PubMed:21883547};
| null | null | null | null |
FUNCTION: Bifunctional serine/threonine kinase and phosphorylase involved in the dark/light-mediated regulation of PPDK by catalyzing its phosphorylation/dephosphorylation. Dark/light-induced changes in stromal concentrations of the competing ADP and Pi substrates govern the direction of the reaction. In the dark, phosphorylates the catalytic intermediate of PPDK (PPDK-HisP), inactivating it. Light exposure induces the phosphorolysis reaction that reactivates PPDK. Unlike the kinase function which can utilize either Thr or Ser as target, the phosphorylase function has a strict substrate requirement for threonyl phosphate. {ECO:0000269|PubMed:17996018, ECO:0000269|PubMed:21883547}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49595
|
HMGB1_ARATH
|
MKTAKGKDKVKTTKEALKPVDDRKVGKRKAPAEKPTKRETRKEKKAKKDPNKPKRAPSAFFVFLEDFRVTFKKENPNVKAVSAVGKAGGQKWKSMSQAEKAPYEEKAAKRKAEYEKQMDAYNKNLEEGSDESEKSRSEINDEDEASGEEELLEKEAAGDDEEEEEEEDDDDDDDEEED
| null | null |
chromatin organization [GO:0006325]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; structural constituent of chromatin [GO:0030527]
|
PF00505;
|
1.10.30.10;
|
HMGB family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:17114349, ECO:0000269|PubMed:18822296}. Note=Displays a highly dynamic speckle distribution pattern in interphase chromatin but does not associate with mitotic chromosomes.
| null | null | null | null | null |
FUNCTION: Binds preferentially double-stranded DNA. Modulates general plant growth and stress tolerance. Confers sensitivity to salt and genotoxic (methyl methanesulfonate, MMS) stresses. {ECO:0000269|PubMed:17114349, ECO:0000269|PubMed:9461286}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49596
|
HMGB2_ARATH
|
MKGAKSKTETRSSKLSVTKKPAKGAGRGKAAAKDPNKPKRPASAFFVFMEDFRETFKKENPKNKSVATVGKAAGDKWKSLSDSEKAPYVAKAEKRKVEYEKNIKAYNKKLEEGPKEDEESDKSVSEVNDEDDAEDGSEEEEDDD
| null | null |
chromatin organization [GO:0006325]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; structural constituent of chromatin [GO:0030527]
|
PF00505;
|
1.10.30.10;
|
HMGB family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:20123078}. Cytoplasm, cytosol {ECO:0000269|PubMed:20123078}.
| null | null | null | null | null |
FUNCTION: Binds preferentially double-stranded DNA. Confers sensitivity to salt and drought stresses. {ECO:0000269|PubMed:17169924, ECO:0000269|PubMed:9461286}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49597
|
HMGB5_ARATH
|
MKDNQTEVESRSTDDRLKVRGNKVGKKTKDPNRPKKPPSPFFVFLDDFRKEFNLANPDNKSVGNVGRAAGKKWKTMTEEERAPFVAKSQSKKTEYAVTMQQYNMELANGNKTTGDDEKQEKAADD
| null | null |
chromatin organization [GO:0006325]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; structural constituent of chromatin [GO:0030527]
|
PF00505;
|
1.10.30.10;
|
HMGB family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:17114349}. Note=Displays a highly dynamic speckle distribution pattern in interphase chromatin.
| null | null | null | null | null |
FUNCTION: Binds preferentially double-stranded DNA. Confers resistance to salt and drought stresses. {ECO:0000269|PubMed:17169924, ECO:0000269|PubMed:9461286}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49623
|
DPNP2_ARATH
|
MSYEKELAAAKKAVTLAARLSQEVQKTLLQSQVWKKSDRSPVTAADYGSQAVVSLVLERELQPDKLSLVAEEETGDLRKNGSEAFLEDIAKLVKDTLASEESYTSSPLSTDDVLNAIDCGKSEGGCKGSHWVLDPIDGTRGFVRGEQYAVGLALLVEGKVVLGVMACPNLPLASAVCATDNSSQEDVGCLFFATTGSGTYVQSLKGNSLPQKVQVSSNENLDEAKFLESYHKPIPIHGTIAKKLGIKALPVRIDSQAKYAALSRGDAEIYLRFTLNGYRECIWDHAPGSIITTEAGGVVCDATGKSLDFSKGKYLAHKTGIIVTTKKLKPWILKAVRESIEEENLYF
|
3.1.3.57; 3.1.3.7
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10205895};
|
sulfate assimilation [GO:0000103]
| null |
3'(2'),5'-bisphosphate nucleotidase activity [GO:0008441]; inositol bisphosphate phosphatase activity [GO:0016312]; inositol-1,4-bisphosphate 1-phosphatase activity [GO:0004441]; metal ion binding [GO:0046872]
|
PF00459;
|
3.40.190.80;3.30.540.10;
|
Inositol monophosphatase superfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000269|PubMed:10205895}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10041; Evidence={ECO:0000305|PubMed:10205895}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + H2O = adenosine 5'-phosphosulfate + phosphate; Xref=Rhea:RHEA:77639, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339; EC=3.1.3.7; Evidence={ECO:0000269|PubMed:10205895}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77640; Evidence={ECO:0000305|PubMed:10205895}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate; Xref=Rhea:RHEA:15553, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, ChEBI:CHEBI:58469; EC=3.1.3.57; Evidence={ECO:0000269|PubMed:10205895}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15554; Evidence={ECO:0000305|PubMed:10205895};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for adenosine 3',5'-bisphosphate {ECO:0000269|PubMed:10205895}; KM=830 uM for 1D-myo-inositol 1,4-bisphosphate {ECO:0000269|PubMed:10205895};
|
PATHWAY: Signal transduction; phosphatidylinositol signaling pathway. {ECO:0000305}.
| null | null |
FUNCTION: Phosphatase that converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'-phosphoadenosine 5'-phosphate (3'-PAP) to AMP (PubMed:10205895). May regulate the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS (By similarity). Prevents both the toxicity of PAP on RNA processing enzymes as well as the product inhibition by PAP of sulfate conjugation. Is also able to hydrolyze inositol 1,4-bisphosphate (PubMed:10205895). {ECO:0000250|UniProtKB:Q42546, ECO:0000269|PubMed:10205895}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49627
|
ISU1_ARATH
|
MMLKQAAKKALGLTSRQSTPWSVGILRTYHENVIDHYDNPRNVGSFDKNDPNVGTGLVGAPACGDVMKLQIKVDEKTGQIVDARFKTFGCGSAIASSSVATEWVKGKAMEDVLTIKNTEIAKHLSLPPVKLHCSMLAEDAIKAAVKDYKEKRVKTNGAAAAGETTQA
| null |
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:17417719}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000269|PubMed:17417719};
|
intracellular iron ion homeostasis [GO:0006879]; iron-sulfur cluster assembly [GO:0016226]
|
cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
2 iron, 2 sulfur cluster binding [GO:0051537]; ferrous iron binding [GO:0008198]; structural molecule activity [GO:0005198]
|
PF01592;
|
3.90.1010.10;
|
NifU family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:15792798, ECO:0000269|PubMed:17417719, ECO:0000269|PubMed:19865480}. Cytoplasm, cytosol {ECO:0000269|PubMed:19865480}. Note=Localizes to the cytosol when interacting with HSCB. {ECO:0000269|PubMed:19865480}.
| null | null |
PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis. {ECO:0000250|UniProtKB:Q03020}.
| null | null |
FUNCTION: Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins (PubMed:15507320, PubMed:17417719). First, a [2Fe-2S] cluster is transiently assembled on the scaffold protein ISCU (ISU1, ISU2 or ISU3). In a second step, the cluster is released from ISCU, transferred to a glutaredoxin, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISCU depends on the function of the cysteine desulfurase complex NFS1-ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase and ferredoxin, which receive their electrons from NADH (By similarity). {ECO:0000250|UniProtKB:Q03020, ECO:0000269|PubMed:15507320, ECO:0000269|PubMed:17417719}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49686
|
PYR1_ARATH
|
MPSELTPEERSELKNSIAEFHTYQLDPGSCSSLHAQRIHAPPELVWSIVRRFDKPQTYKHFIKSCSVEQNFEMRVGCTRDVIVISGLPANTSTERLDILDDERRVTGFSIIGGEHRLTNYKSVTTVHRFEKENRIWTVVLESYVVDMPEGNSEDDTRMFADTVVKLNLQKLATVAEAMARNSGDGSGSQVT
| null | null |
abscisic acid-activated signaling pathway [GO:0009738]; positive regulation of response to water deprivation [GO:1902584]; regulation of protein serine/threonine phosphatase activity [GO:0080163]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; plant-type vacuole membrane [GO:0009705]; plasma membrane [GO:0005886]; protein phosphatase inhibitor complex [GO:0062049]
|
abscisic acid binding [GO:0010427]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein phosphatase inhibitor activity [GO:0004864]; signaling receptor activity [GO:0038023]; ubiquitin-like protein ligase binding [GO:0044389]
|
PF10604;
|
3.30.530.20;
|
PYR/PYL/RCAR abscisic acid intracellular receptor family
|
PTM: Ubiquitynated and degraded by the proteasome upon binding to the E3 ubiquitin-protein ligase RSL1 at the plasma membrane. {ECO:0000269|PubMed:25330042}.; PTM: Phosphorylated by CARK1 especially in response to abscisic acid (ABA); this phosphorylation promotes its stability and inhibitory ability to ABI1. {ECO:0000269|PubMed:29928509}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}. Cytoplasm, cytosol {ECO:0000269|PubMed:29928509}. Nucleus {ECO:0000269|PubMed:25465408}. Cell membrane {ECO:0000269|PubMed:25330042, ECO:0000269|PubMed:25465408}. Vacuole {ECO:0000269|PubMed:27495812}. Note=Localizes at the plasma membrane in the presence of a CAR protein (By similarity). Localized transiently in the vacuole when in complex with RSL1 (PubMed:27495812). {ECO:0000250|UniProtKB:O80920, ECO:0000269|PubMed:27495812}.
| null | null | null | null | null |
FUNCTION: Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA (PubMed:19407142, PubMed:19624469, PubMed:19769575, PubMed:21658606, PubMed:23844015). Can be activated by both (-)-ABA and (+)-ABA (PubMed:23844015). Promotes drought tolerance (PubMed:29970817). {ECO:0000269|PubMed:19407142, ECO:0000269|PubMed:19624469, ECO:0000269|PubMed:19769575, ECO:0000269|PubMed:21658606, ECO:0000269|PubMed:23844015, ECO:0000269|PubMed:29970817}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49687
|
MYC4_ARATH
|
MSPTNVQVTDYHLNQSKTDTTNLWSTDDDASVMEAFIGGGSDHSSLFPPLPPPPLPQVNEDNLQQRLQALIEGANENWTYAVFWQSSHGFAGEDNNNNNTVLLGWGDGYYKGEEEKSRKKKSNPASAAEQEHRKRVIRELNSLISGGVGGGDEAGDEEVTDTEWFFLVSMTQSFVKGTGLPGQAFSNSDTIWLSGSNALAGSSCERARQGQIYGLQTMVCVATENGVVELGSSEIIHQSSDLVDKVDTFFNFNNGGGEFGSWAFNLNPDQGENDPGLWISEPNGVDSGLVAAPVMNNGGNDSTSNSDSQPISKLCNGSSVENPNPKVLKSCEMVNFKNGIENGQEEDSSNKKRSPVSNNEEGMLSFTSVLPCDSNHSDLEASVAKEAESNRVVVEPEKKPRKRGRKPANGREEPLNHVEAERQRREKLNQRFYSLRAVVPNVSKMDKASLLGDAISYISELKSKLQKAESDKEELQKQIDVMNKEAGNAKSSVKDRKCLNQESSVLIEMEVDVKIIGWDAMIRIQCSKRNHPGAKFMEALKELDLEVNHASLSVVNDLMIQQATVKMGNQFFTQDQLKVALTEKVGECP
| null | null |
anthocyanin-containing compound biosynthetic process [GO:0009718]; defense response [GO:0006952]; extracellular ATP signaling [GO:0106167]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355]; regulation of secondary cell wall biogenesis [GO:2000652]; stomatal complex development [GO:0010374]
|
nucleus [GO:0005634]
|
bHLH transcription factor binding [GO:0043425]; DNA-binding transcription factor activity [GO:0003700]; protein dimerization activity [GO:0046983]; transcription cis-regulatory region binding [GO:0000976]
|
PF14215;PF00010;
|
4.10.280.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:21321051, ECO:0000269|PubMed:21335373}.
| null | null | null | null | null |
FUNCTION: Transcription factor involved in jasmonic acid (JA) gene regulation. With MYC2 and MYC3, controls additively subsets of JA-dependent responses. Can form complexes with all known glucosinolate-related MYBs to regulate glucosinolate biosynthesis. Binds to the G-box (5'-CACGTG-3') of promoters. Activates multiple TIFY/JAZ promoters. {ECO:0000269|PubMed:21321051, ECO:0000269|PubMed:21335373, ECO:0000269|PubMed:23943862}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49696
|
ALMTC_ARATH
|
MSNKVHVGSLEMEEGLSKTKWMVLEPSEKIKKIPKRLWNVGKEDPRRVIHALKVGLSLTLVSLLYLMEPLFKGIGSNAIWAVMTVVVVLEFSAGATLCKGLNRGLGTLIAGSLAFFIEFVANDSGKVLRAIFIGTAVFIIGAAATYIRFIPYIKKNYDYGVVIFLLTFNLITVSSYRVDSVINIAHDRFYTIAVGCGICLFMSLLVFPIWSGEDLHKTTVGKLQGLSRSIEACVDEYFEEKEKEKTDSKDRIYEGYQAVLDSKSTDETLALYANWEPRHTLRCHRFPCQQYVKVGAVLRQFGYTVVALHGCLQTEIQTPRSVRALFKDPCVRLAGEVCKALTELADSISNHRHCSPEILSDHLHVALQDLNSAIKSQPKLFLGSNLHRHNNKHQNGSISNNKHHQRNSSNSGKDLNGDVSLQNTETGTRKITETGSRQGQNGAVSLSSFRTDTSALMEYRRSFKNSNSEMSAAGERRMLRPQLSKIAVMTSLEFSEALPFAAFASLLVEMVARLDNVIEEVEELGRIASFKEYDNKRDQTADDVRCENPANVTISVGAAE
| null | null |
malate transport [GO:0015743]; stomatal movement [GO:0010118]; sulfate transport [GO:0008272]
|
endomembrane system [GO:0012505]; plant-type vacuole membrane [GO:0009705]; plasma membrane [GO:0005886]
|
monoatomic anion transmembrane transporter activity [GO:0008509]
|
PF11744;
| null |
Aromatic acid exporter (TC 2.A.85) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20154005, ECO:0000269|PubMed:20626656}; Multi-pass membrane protein {ECO:0000269|PubMed:20154005, ECO:0000269|PubMed:20626656}. Note=PubMed:20626656 indicates also a not confirmed endomembrane localization.
| null | null | null | null | null |
FUNCTION: Malate-sensitive anion transporter permeable to chloride, nitrate, sulfate and malate. Involved in dark-, CO(2)-, abscisic acid- and water-deficient-induced stomatal closure. Belongs to the R-type anion channels. {ECO:0000269|PubMed:20154005, ECO:0000269|PubMed:20626656}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49717
|
CDPKF_ARATH
|
MGCFSSKHRNTESDIINGSVQSSIPTNQPENHVSRDVLKPQKPPSPQIPTTTQSNHHHQQESKPVNQQIEKKHVLTQPLKPIVFRETETILGKPFEEIRKLYTLGKELGRGQFGITYTCKENSTGNTYACKSILKRKLTRKQDIDDVKREIQIMQYLSGQENIVEIKGAYEDRQSIHLVMELCGGSELFDRIIAQGHYSEKAAAGVIRSVLNVVQICHFMGVIHRDLKPENFLLASTDENAMLKATDFGLSVFIEEGKVYRDIVGSAYYVAPEVLRRSYGKEIDIWSAGIILYILLCGVPPFWSETEKGIFNEIIKGEIDFDSQPWPSISESAKDLVRKLLTKDPKQRISAAQALEHPWIRGGEAPDKPIDSAVLSRMKQFRAMNKLKKLALKVIAESLSEEEIKGLKTMFANMDTDKSGTITYEELKNGLAKLGSKLTEAEVKQLMEAADVDGNGTIDYIEFISATMHRYRFDRDEHVFKAFQYFDKDNSGFITMDELESAMKEYGMGDEASIKEVIAEVDTDNDGRINYEEFCAMMRSGITLPQQGKILPVQ
|
2.7.11.1
| null |
intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein serine kinase activity [GO:0106310]
|
PF13499;PF00069;
|
1.10.238.10;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
|
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: May play a role in signal transduction pathways that involve calcium as a second messenger.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49782
|
MYB51_ARATH
|
MVRTPCCKAELGLKKGAWTPEEDQKLLSYLNRHGEGGWRTLPEKAGLKRCGKSCRLRWANYLRPDIKRGEFTEDEERSIISLHALHGNKWSAIARGLPGRTDNEIKNYWNTHIKKRLIKKGIDPVTHKGITSGTDKSENLPEKQNVNLTTSDHDLDNDKAKKNNKNFGLSSASFLNKVANRFGKRINQSVLSEIIGSGGPLASTSHTTNTTTTSVSVDSESVKSTSSSFAPTSNLLCHGTVATTPVSSNFDVDGNVNLTCSSSTFSDSSVNNPLMYCDNFVGNNNVDDEDTIGFSTFLNDEDFMMLEESCVENTAFMKELTRFLHEDENDVVDVTPVYERQDLFDEIDNYFG
| null | null |
defense response by callose deposition in cell wall [GO:0052544]; defense response to bacterium [GO:0042742]; indole glucosinolate biosynthetic process [GO:0009759]; induced systemic resistance [GO:0009682]; response to bacterium [GO:0009617]; response to insect [GO:0009625]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976]
|
PF00249;
|
1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:17461791}.
| null | null | null | null | null |
FUNCTION: Transcription factor positively regulating indolic glucosinolate biosynthetic pathway genes. {ECO:0000269|PubMed:17461791, ECO:0000269|PubMed:23580754, ECO:0000269|PubMed:23943862}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49815
|
BCH1_CAPAN
|
MAAEISISASSRAICLQRNPFPAPKYFATAPPLLFFSPLTCNLDAILRSRRKPRLAACFVLKDDKLYTAQSGKQSDTEAIGDEIEVETNEEKSLAVRLAEKFARKKSERFTYLVAAVMSSLGITSMAVISVYYRFSWQMEGGEMPFSEMFCTFALAFGAAIGMEYWARWAHRALWHASLWHMHESHHRPREGPFELNDIFAIINAVPAIALLSFGFNHKGLIPGLCFGAGLGITVFGMAYMFVHDGLVHKRFPVGPIANVPYFQRVAAAHQLHHSDKFDGVPYGLFLGPKELEEVGVLEELEKEVNRRIKSSKRL
|
1.14.15.24
| null |
carotene metabolic process [GO:0016119]; xanthophyll biosynthetic process [GO:0016123]
|
chloroplast membrane [GO:0031969]
|
beta-carotene 3-hydroxylase activity [GO:0052611]; beta-cryptoxanthin hydroxylase activity [GO:0052610]; carotene beta-ring hydroxylase activity [GO:0010291]; hydrolase activity [GO:0016787]; iron ion binding [GO:0005506]
|
PF04116;
| null |
Sterol desaturase family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=all-trans-beta-carotene + 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-[ferredoxin] = all-trans-zeaxanthin + 2 H2O + 4 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:30331, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17579, ChEBI:CHEBI:27547, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.14.15.24; Evidence={ECO:0000269|PubMed:9555077}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30332; Evidence={ECO:0000269|PubMed:9555077}; CATALYTIC ACTIVITY: Reaction=all-trans-beta-carotene + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = beta-cryptoxanthin + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:30323, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:10362, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17579, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; Evidence={ECO:0000269|PubMed:9555077}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30324; Evidence={ECO:0000269|PubMed:9555077}; CATALYTIC ACTIVITY: Reaction=beta-cryptoxanthin + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = all-trans-zeaxanthin + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:30327, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:10362, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:27547, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; Evidence={ECO:0000269|PubMed:9555077}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30328; Evidence={ECO:0000269|PubMed:9555077};
| null | null | null | null |
FUNCTION: Nonheme diiron monooxygenase involved in the biosynthesis of xanthophylls. Specific for beta-ring hydroxylations of beta-carotene. Produces beta-cryptoxanthin and zeaxanthin. Uses ferredoxin as an electron donor. {ECO:0000269|PubMed:9555077}.
|
Capsicum annuum (Capsicum pepper)
|
O49839
|
PBL2_ARATH
|
MGNCLDSSAKVDNSNHSPHANSASSGSKVSSKTSRSTGPSGLSTTSYSTDSSFGPLPTLRTEGEILSSPNLKAFTFNELKNATKNFRQDNLLGEGGFGCVFKGWIDQTSLTASRPGSGIVVAVKQLKPEGFQGHKEWLTEVNYLGQLSHPNLVLLVGYCAEGENRLLVYEFMPKGSLENHLFRRGAQPLTWAIRMKVAVGAAKGLTFLHEAKSQVIYRDFKAANILLDADFNAKLSDFGLAKAGPTGDNTHVSTKVIGTHGYAAPEYVATGRLTAKSDVYSFGVVLLELISGRRAMDNSNGGNEYSLVDWATPYLGDKRKLFRIMDTKLGGQYPQKGAFTAANLALQCLNPDAKLRPKMSEVLVTLEQLESVAKPGTKHTQMESPRFHHSSVMQKSPVRYSHDRPLLHMTPGASPLPSYTQSPRVR
|
2.7.11.1
| null |
defense response [GO:0006952]; phosphorylation [GO:0016310]; positive regulation of defense response to bacterium [GO:1900426]
|
nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; Tat protein binding [GO:0030957]
|
PF07714;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
|
PTM: Uridylylated at Ser-253 and Thr-254 by Xanthomonas campestris effector AvrAC/XopAC; this uridylylation is necessary for specific recruitment to RKS1 and to trigger immunity. {ECO:0000269|PubMed:26355215}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21219905}; Lipid-anchor {ECO:0000305|PubMed:21219905}. Nucleus {ECO:0000269|PubMed:21219905}. Note=Predominantly localized at the plasma membrane. {ECO:0000269|PubMed:21219905}.
|
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; Evidence={ECO:0000305}; 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; Evidence={ECO:0000305};
| null | null | null | null |
FUNCTION: Involved in disease resistance signaling (PubMed:20413097, PubMed:23951354, PubMed:26355215). Contributes to pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) signaling and defense responses downstream of FLS2 (PubMed:20413097). Acts as a BIK1 decoy and enables Xanthomonas campestris AvrAC/XopAC detection; X.campestris effector AvrAC/XopAC-mediated uridylylation promotes the formation of a complex with RKS1 and RPP13L4/ZAR1 which, in turn, activates effector-triggered immunity (ETI) against X.campestris (PubMed:23951354, PubMed:26355215, PubMed:30948526). Promotes, when uridylylated by AvrAC/XopAC, the release of ADP from the inactive RKS1-ZAR1 complex, thus activating the resistosome (PubMed:30948526). {ECO:0000269|PubMed:20413097, ECO:0000269|PubMed:23951354, ECO:0000269|PubMed:26355215, ECO:0000269|PubMed:30948526}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O49840
|
PBL3_ARATH
|
MGNCLDSSAKVDSSSHSPHANSASLSSRVSSKTSRSTVPSSLSINSYSSVESLPTPRTEGEILSSPNLKAFTFNELKNATRNFRPDSLLGEGGFGYVFKGWIDGTTLTASKPGSGIVVAVKKLKTEGYQGHKEWLTEVNYLGQLSHPNLVKLVGYCVEGENRLLVYEFMPKGSLENHLFRRGAQPLTWAIRMKVAIGAAKGLTFLHDAKSQVIYRDFKAANILLDAEFNSKLSDFGLAKAGPTGDKTHVSTQVMGTHGYAAPEYVATGRLTAKSDVYSFGVVLLELLSGRRAVDKSKVGMEQSLVDWATPYLGDKRKLFRIMDTRLGGQYPQKGAYTAASLALQCLNPDAKLRPKMSEVLAKLDQLESTKPGTGVGNRQAQIDSPRGSNGSIVQKSPRRYSYDRPLLHITPGASPLPTHNHSPRVR
|
2.7.11.1
| null |
defense response [GO:0006952]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF07714;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21219905}; Lipid-anchor {ECO:0000305|PubMed:21219905}. Nucleus {ECO:0000269|PubMed:21219905}. Note=Predominantly localized at the plasma membrane. {ECO:0000269|PubMed:21219905}.
|
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; Evidence={ECO:0000305}; 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; Evidence={ECO:0000305};
| null | null | null | null |
FUNCTION: May be involved in plant defense signaling. {ECO:0000250|UniProtKB:O48814}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O50008
|
METE1_ARATH
|
MASHIVGYPRMGPKRELKFALESFWDGKSTAEDLQKVSADLRSSIWKQMSAAGTKFIPSNTFAHYDQVLDTTAMLGAVPPRYGYTGGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYLLLSKAAKGVDKSFELLSLLPKILPIYKEVITELKAAGATWIQLDEPVLVMDLEGQKLQAFTGAYAELESTLSGLNVLVETYFADIPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLVKAGFPEGKYLFAGVVDGRNIWANDFAASLSTLQALEGIVGKDKLVVSTSCSLLHTAVDLINETKLDDEIKSWLAFAAQKVVEVNALAKALAGQKDEALFSANAAALASRRSSPRVTNEGVQKAAAALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKVSEEDYVKAIKEEIKKVVDLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPVIYGDVSRPKAMTVFWSAMAQSMTSRPMKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKGGIGVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQDSTQIHTHMCYSHFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSSEEIADRVNKMLAVLEQNILWVNPDCGLKTRKYTEVKPALKNMVDAAKLIRSQLASAK
|
2.1.1.14
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:15326182}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:15326182};
|
'de novo' L-methionine biosynthetic process [GO:0071266]; DNA methylation-dependent heterochromatin formation [GO:0006346]; methionine biosynthetic process [GO:0009086]; methylation [GO:0032259]; response to zinc ion [GO:0010043]
|
apoplast [GO:0048046]; chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; peroxisome [GO:0005777]; plant-type vacuole [GO:0000325]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]
|
5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity [GO:0003871]; copper ion binding [GO:0005507]; methionine synthase activity [GO:0008705]; mRNA binding [GO:0003729]; zinc ion binding [GO:0008270]
|
PF08267;PF01717;
|
3.20.20.210;
|
Vitamin-B12 independent methionine synthase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15024005}.
|
CATALYTIC ACTIVITY: Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196, ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199, ChEBI:CHEBI:58207; EC=2.1.1.14; Evidence={ECO:0000269|PubMed:15024005};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 uM for 5-methyltetrahydrofolate {ECO:0000269|PubMed:15024005}; Vmax=26.5 nmol/min/mg enzyme toward 5-methyltetrahydrofolate {ECO:0000269|PubMed:15024005};
|
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1. {ECO:0000269|PubMed:15024005}.
| null | null |
FUNCTION: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation. {ECO:0000269|PubMed:15024005}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O50055
|
COL1_ARATH
|
MLKVESNWAQACDTCRSAACTVYCRADSAYLCSSCDAQVHAANRLASRHERVRVCQSCERAPAAFFCKADAASLCTTCDSEIHSANPLARRHQRVPILPISEYSYSSTATNHSCETTVTDPENRLVLGQEEEDEDEAEAASWLLPNSGKNSGNNNGFSIGDEFLNLVDYSSSDKQFTDQSNQYQLDCNVPQRSYGEDGVVPLQIEVSKGMYQEQQNFQLSINCGSWGALRSSNGSLSHMVNVSSMDLGVVPESTTSDATVSNPRSPKAVTDQPPYPPAQMLSPRDREARVLRYREKKKMRKFEKTIRYASRKAYAEKRPRIKGRFAKKKDVDEEANQAFSTMITFDTGYGIVPSF
| null | null |
regulation of flower development [GO:0009909]
|
nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270]
|
PF06203;PF00643;
| null |
CONSTANS family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Putative transcription factor that may be involved in the light input to the circadian clock but does not affect flowering time.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O50061
|
RK4_ARATH
|
MASSATAPNSLSFFSSSLFLSSSHQIPKTYISVSKLGSGRVSKPLSVSSQLATLPILSFEGEKVGETYLDLKAAPEDTARAVVHRAIVTDLNNKRRGTASTLTRGEVRGGGIKPYSQKKTGHARRGSQRTPLRPGGGVVFGPRPKDWSIKINRKEKKLAISTALSSAASAEGGAIVVEEFGEKFEKPKTKDFLAAMQRWGLDPKEKAMFLMIDVDENVAKSSRNIGTLRMLTPRTLNLFDILNADKLVLTPAAVEFLNARYGVDAVEEEDDDEDETEGSEEA
| null | null |
translation [GO:0006412]
|
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; chloroplast thylakoid membrane [GO:0009535]; cytosolic ribosome [GO:0022626]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plastid large ribosomal subunit [GO:0000311]; plastid ribosome [GO:0009547]; thylakoid [GO:0009579]
|
mRNA binding [GO:0003729]; poly(U) RNA binding [GO:0008266]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]
|
PF00573;
|
3.40.1370.10;
|
Universal ribosomal protein uL4 family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast.
| null | null | null | null | null |
FUNCTION: This protein binds directly and specifically to 23S rRNA (By similarity). May play a role in plastid transcriptional regulation. {ECO:0000250}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O50078
|
ACEA_HYPME
|
MAHKKTYSQLRSELLARYPVGLTKGGVSIDDIVQLRLQSPYESHLDVARAMASVMRADMAAYDRDTGKFTQSLGCWSGFHAQQMIKAVKRLRGTTKGAYVYLSGWMVAGLRNRWGHLPDQSMHEKTSVVDLIEEIYVSLRQADEVALNDLFNELKDARAKGATNKACEEIISRIDGFESHVVPIIADIDAGFGNEHATYLLAKEMIKAGACCLQIENQVSDAKQCGHQDGKVTVPREDFIEKLRACRLAFEELGVDDGVIVARTDSLGASLTQKIPVSQQAGDFASSYIKWLKTEPITDANPLSEGELAIWQSGNFARPIRMPNGLFSFREGTGRARVIEDCIASLKDGDADLIWIETDTPNVDEIASMVAEIRKQVPDAKLVYNNSPSFNWTLNLRKQVRAQWISEGKIAEADYPDGTALMSAQYDTSELGREADDRLRQFQVDISARAGVFHNLITLPTFHLTAKSTDELSHGYFGEDRMLAYVATVQREEIRRSISAVRHQHEVGSDLGDTFKEMVSGDRALKAGGAHNTMNQFAAE
|
4.1.3.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9395332}; Note=Can also use Mn(2+). {ECO:0000269|PubMed:9395332};
|
glyoxylate cycle [GO:0006097]; tricarboxylic acid cycle [GO:0006099]
|
glyoxysome [GO:0009514]
|
isocitrate lyase activity [GO:0004451]; magnesium ion binding [GO:0000287]; transition metal ion binding [GO:0046914]
|
PF00463;
|
3.20.20.60;
|
Isocitrate lyase/PEP mutase superfamily, Isocitrate lyase family
| null | null |
CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate = glyoxylate + succinate; Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031, ChEBI:CHEBI:36655; EC=4.1.3.1; Evidence={ECO:0000269|PubMed:9395332};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.51 mM for D-isocitrate {ECO:0000269|PubMed:9395332};
|
PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 1/2. {ECO:0000305|PubMed:9395332}.; PATHWAY: One-carbon metabolism; formaldehyde assimilation via serine pathway. {ECO:0000305|PubMed:9395332}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. The enzyme is stable when incubated for 15 minutes at 30 degrees Celsius at pH 7.5-9. {ECO:0000269|PubMed:9395332};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. Loss of activity is 0%, 16%, 30%, 82% and 100% when incubated at 25, 30, 40, 50 and 60 degrees Celsius for 30 minutes, respectively. {ECO:0000269|PubMed:9395332};
|
FUNCTION: Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates. May be involved in the assimilation of one-carbon compounds via the isocitrate lyase-positive serine pathway. {ECO:0000269|PubMed:9395332}.
|
Hyphomicrobium methylovorum
|
O50083
|
RPIA_PYRHO
|
MNVEEMKKIAAKEALKFIEDDMVIGLGTGSTTAYFIKLLGEKLKRGEISDIVGVPTSYQAKLLAIEHDIPIASLDQVDAIDVAVDGADEVDPNLNLIKGRGAALTMEKIIEYRAGTFIVLVDERKLVDYLCQKMPVPIEVIPQAWKAIIEELSIFNAKAELRMGVNKDGPVITDNGNFIIDAKFPRIDDPLDMEIELNTIPGVIENGIFADIADIVIVGTREGVKKLER
|
5.3.1.6
| null |
D-ribose metabolic process [GO:0006014]; pentose-phosphate shunt, non-oxidative branch [GO:0009052]
|
cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]
|
ribose-5-phosphate isomerase activity [GO:0004751]
|
PF06026;
|
3.30.70.260;3.40.50.1360;
|
Ribose 5-phosphate isomerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate; Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273; EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170, ECO:0000269|PubMed:12057201};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.17 mM for ribose 5-P {ECO:0000269|PubMed:12057201};
|
PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00170}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 (at 50 degrees Celsius). {ECO:0000269|PubMed:12057201};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is over 95 degrees Celsius. {ECO:0000269|PubMed:12057201};
|
FUNCTION: Involved in the first step of the non-oxidative branch of the pentose phosphate pathway. It catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. {ECO:0000269|PubMed:12057201}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O50131
|
ORNAT_PYRHO
|
MELKPNVKEIPGPKARKVIEEHHKYMATTTNDPNEYFLVIERAEGVYWIDVDGNVLLDFSSGIGVMNVGLRNPKVIEAIKKQLDLVLHAAGTDYYNPYQVELAKKLVEIAPGDIERKVFLSNSGTEANEAALKIAKWSTNRKMFIAFIGAFHGRTHGTMSLTASKPVQRSRMFPTMPGVVHVPYPNPYRNPWGIDGYENPDELINRVIDYIEEYLFEHYVPAEEVAGIFFEPIQGEGGYVVPPKNFFKELKKLADKHGILLIDDEVQMGMGRTGRMWAIEHFDIVPDIVTVAKALGGGIPIGATIFRADLDFGVSGVHSNTFGGNTVAAAAALAVIEELQNGLIENAQKLEPLFRERLEEMKEKYEIIGDVRGLGLAWGVEFVKDRKTKEYATKERGEIVVEALKRGLALLGCGKSAIRLIPPLIISEEEAKMGLDIFEEAIKVVSERHGYKIH
|
2.6.1.13
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:35337912};
| null | null |
identical protein binding [GO:0042802]; pyridoxal phosphate binding [GO:0030170]; transaminase activity [GO:0008483]
|
PF00202;
|
3.90.1150.10;3.40.640.10;
|
Class-III pyridoxal-phosphate-dependent aminotransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-ornithine = L-glutamate + L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:25160, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:46911, ChEBI:CHEBI:58066; EC=2.6.1.13; Evidence={ECO:0000269|PubMed:35337912}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-lysine = (S)-2-amino-6-oxohexanoate + L-glutamate; Xref=Rhea:RHEA:21200, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:32551, ChEBI:CHEBI:58321; Evidence={ECO:0000269|PubMed:35337912};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.106 mM for L-ornithine (in the presence of 10 mM 2-oxoglutarate) {ECO:0000269|PubMed:35337912}; KM=0.211 mM for L-lysine (in the presence of 10 mM 2-oxoglutarate) {ECO:0000269|PubMed:35337912}; KM=0.446 mM for D-ornithine (in the presence of 5 mM 2-oxoglutarate) {ECO:0000269|PubMed:35337912}; KM=5.22 mM for D-lysine (in the presence of 20 mM 2-oxoglutarate) {ECO:0000269|PubMed:35337912}; KM=0.802 mM for 2-oxoglutarate (in the presence of 1 mM L-ornithine) {ECO:0000269|PubMed:35337912}; KM=0.624 mM for 2-oxoglutarate (in the presence of 2 mM L-lysine) {ECO:0000269|PubMed:35337912}; KM=0.182 mM for 2-oxoglutarate (in the presence of 5 mM D-ornithine) {ECO:0000269|PubMed:35337912}; KM=1.23 mM for 2-oxoglutarate (in the presence of 20 mM D-lysine) {ECO:0000269|PubMed:35337912}; Note=kcat is 4.32 sec(-1) with L-ornithine as substrate. kcat is 1.61 sec(-1) with L-lysine as substrate. kcat is 0.493 sec(-1) with D-ornithine as substrate. kcat is 3.25 sec(-1) with D-lysine as substrate. kcat is 3.51 sec(-1) with 2-oxoglutarate as substrate in the presence of L-ornithine. kcat is 1.41 sec(-1) with 2-oxoglutarate as substrate in the presence of L-lysine. kcat is 0.462 sec(-1) with 2-oxoglutarate as substrate in the presence of D-ornithine. kcat is 3.02 sec(-1) with 2-oxoglutarate as substrate in the presence of D-lysine. {ECO:0000269|PubMed:35337912};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:35337912};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is higher than 90 degrees Celsius. {ECO:0000269|PubMed:35337912};
|
FUNCTION: Catalyzes the conversion of L-ornithine and 2-oxoglutarate to L-glutamate semialdehyde and L-glutamate (PubMed:35337912). L-ornithine is the best substrate, but the enzyme also shows good activity toward L-lysine, and low activity toward D-ornithine, D-lysine, 5-aminovalerate, 6-aminohexanoate and GABA (PubMed:35337912). The enzyme activity is specific for 2-oxoglutarate (PubMed:35337912). {ECO:0000269|PubMed:35337912}.
|
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
|
O50146
|
LYSY_THET2
|
MDKKTLSIVGASGYAGGEFLRLALSHPYLEVKQVTSRRFAGEPVHFVHPNLRGRTNLKFIPPEKLEPADILVLALPHGVFAREFDRYSALAPILIDLSADFRLKDPELYRRYYGEHPRPDLLGCFVYAVPELYREALKGADWIAGAGCNATATLLGLYPLLKAGVLKPTPIFVTLLISTSAAGAEASPASHHPERAGSIRVYKPTGHRHTAEVVENLPGRPEVHLTAIATDRVRGILMTAQCFVQDGWSERDVWQAYREAYAGEPFIRLVKQKKGVHRYPDPRFVQGTNYADIGFELEEDTGRLVVMTAIDNLVKGTAGHALQALNVRMGWPETLGLDFPGLHP
|
1.2.1.103
| null |
arginine biosynthetic process [GO:0006526]; lysine biosynthetic process via aminoadipic acid [GO:0019878]
|
cytoplasm [GO:0005737]
|
N-acetyl-gamma-aminoadipyl-phosphate reductase activity [GO:0043870]; N-acetyl-gamma-glutamyl-phosphate reductase activity [GO:0003942]; NAD binding [GO:0051287]; NADP+ binding [GO:0070401]; protein dimerization activity [GO:0046983]
|
PF01118;PF02774;
|
3.40.50.720;
|
NAGSA dehydrogenase family, Type 1 subfamily, LysY sub-subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02083}.
|
CATALYTIC ACTIVITY: Reaction=[amino-group carrier protein]-C-terminal-N-(1-carboxy-5-oxopentan-1-yl)-L-glutamine + NADP(+) + phosphate = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + H(+) + NADPH; Xref=Rhea:RHEA:41948, Rhea:RHEA-COMP:9712, Rhea:RHEA-COMP:9714, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78499, ChEBI:CHEBI:78501; EC=1.2.1.103; Evidence={ECO:0000255|HAMAP-Rule:MF_02083, ECO:0000269|PubMed:26966182, ECO:0000305|PubMed:19620981};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.8 uM for [LysW]-aminoadipate 6-semialdehyde {ECO:0000269|PubMed:26966182}; KM=14 uM for NADP(+) {ECO:0000269|PubMed:26966182}; KM=12000 uM for phosphate {ECO:0000269|PubMed:26966182}; Note=kcat is 0.96 sec(-1). {ECO:0000269|PubMed:26966182};
|
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 3/5. {ECO:0000255|HAMAP-Rule:MF_02083, ECO:0000269|PubMed:19620981}.
| null | null |
FUNCTION: Catalyzes the NADPH-dependent reduction of [LysW]-aminoadipate 6-phosphate to yield [LysW]-aminoadipate 6-semialdehyde. {ECO:0000255|HAMAP-Rule:MF_02083, ECO:0000269|PubMed:26966182, ECO:0000305|PubMed:19620981}.
|
Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
|
O50147
|
LYSZ_THET2
|
MIVVKVGGAEGINYEAVAKDAASLWKEGVKLLLVHGGSAETNKVAEALGHPPRFLTHPGGQVSRLTDRKTLEIFEMVYCGLVNKRLVELLQKEGANAIGLSGLDGRLFVGRRKTAVKYVENGKVKVHRGDYTGTVEEVNKALLDLLLQAGYLPVLTPPALSYENEAINTDGDQIAALLATLYGAEALVYLSNVPGLLARYPDEASLVREIPVERIEDPEYLALAQGRMKRKVMGAVEAVRGGVKRVVFADARVENPIRRALSGEGTVVR
|
2.7.2.17
| null |
arginine biosynthetic process [GO:0006526]; lysine biosynthetic process via aminoadipic acid [GO:0019878]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]
|
acetylglutamate kinase activity [GO:0003991]; ATP binding [GO:0005524]; N2-acetyl-L-aminoadipate kinase activity [GO:0043744]
|
PF00696;
|
3.40.1160.10;
|
Acetylglutamate kinase family, LysZ subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02082}.
|
CATALYTIC ACTIVITY: Reaction=[amino-group carrier protein]-C-terminal-N-(1,4-dicarboxybutan-1-yl)-L-glutamine + ATP = [amino-group carrier protein]-C-terminal-N-(1-carboxy-5-phosphooxy-5-oxopentan-1-yl)-L-glutamine + ADP; Xref=Rhea:RHEA:41944, Rhea:RHEA-COMP:9694, Rhea:RHEA-COMP:9712, ChEBI:CHEBI:30616, ChEBI:CHEBI:78499, ChEBI:CHEBI:78503, ChEBI:CHEBI:456216; EC=2.7.2.17; Evidence={ECO:0000255|HAMAP-Rule:MF_02082, ECO:0000269|PubMed:25392000};
| null |
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 2/5. {ECO:0000255|HAMAP-Rule:MF_02082, ECO:0000269|PubMed:10613839, ECO:0000269|PubMed:19620981, ECO:0000305|PubMed:25392000}.
| null | null |
FUNCTION: Catalyzes the phosphorylation of LysW-gamma-alpha-aminoadipate. Does not phosphorylate N-acetyl-glutamate. {ECO:0000269|PubMed:25392000}.
|
Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
|
O50202
|
ARC_RHOER
|
MSSTENPDSVAAAEELHALRVEAQVLRRQLAQSPEQVRELESKVDSLSIRNSKLMDTLKEARQQLIALREEVDRLGQPPSGYGVLLSVHEDKTVDVFTSGRKMRLTCSPNIDTDTLALGQTVRLNEALTIVEAGTYEQVGEISTLREVLDDGLRALVVGHADEERIVWLAAPLAAVFADPEADIIAYDADSPTRKLRPGDSLLVDTKAGYAFERIPKAEVEDLVLEEVPDVHYDDIGGLGRQIEQIRDAVELPFLHKDLFHEYSLRPPKGVLLYGPPGCGKTLIAKAVANSLAKKIAEARGQDSKDAKSYFLNIKGPELLNKFVGETERHIRMIFQRAREKASEGTPVIVFFDEMDSIFRTRGSGVSSDVETTVVPQLLSEIDGVEGLENVIVIGASNREDMIDPAILRPGRLDVKIKIERPDAESAQDIFSKYLVDGLPINADDLAEFGGDRTACLKAMIVRVVDRMYAESEENRFLEVTYANGDKEVLFFKDFNSGAMIQNIVDRAKKYAIKSVLDTGAPGLRVQHLFDSIVDEFAENEDLPNTTNPDDWARISGKKGERIVYIRTLVTGKNASASRAIDTESNTGQYL
| null | null |
modification-dependent protein catabolic process [GO:0019941]; proteasomal protein catabolic process [GO:0010498]; retrograde protein transport, ER to cytosol [GO:0030970]
|
cytosol [GO:0005829]; proteasome complex [GO:0000502]; proteasome-activating nucleotidase complex [GO:0022623]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; CTPase activity [GO:0043273]; polyubiquitin modification-dependent protein binding [GO:0031593]
|
PF00004;PF16450;PF17758;
|
1.10.8.60;1.20.5.170;2.40.50.140;3.40.50.300;
|
AAA ATPase family
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=200 uM for ATP {ECO:0000269|PubMed:9514743}; Vmax=268 pmol/min/ug enzyme {ECO:0000269|PubMed:9514743}; Note=Is also able to cleave CTP at half the rate of ATP hydrolysis, but GTP or UTP are not substrates.;
|
PATHWAY: Protein degradation; proteasomal Pup-dependent pathway. {ECO:0000255|HAMAP-Rule:MF_02112}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. {ECO:0000269|PubMed:9514743};
| null |
FUNCTION: ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. {ECO:0000255|HAMAP-Rule:MF_02112, ECO:0000269|PubMed:19481487, ECO:0000269|PubMed:9514743}.
|
Rhodococcus erythropolis (Arthrobacter picolinophilus)
|
O50274
|
CYSNC_PSEAE
|
MSHQSDLISEDILAYLGQHERKELLRFLTCGNVDDGKSTLIGRLLHDSKMIYEDHLEAITRDSKKVGTTGDDVDLALLVDGLQAEREQGITIDVAYRYFSTAKRKFIIADTPGHEQYTRNMATGASTCDLAIILIDARYGVQTQTRRHSFIASLLGIRHIVVAINKMDLKDFDQGVFEQIKADYLAFAEKIGLKTSSLHFVPMSALKGDNVVNKSERSPWYAGQSLMEILETVEIAADRNLDDMRFPVQYVNRPNLNFRGFAGTLASGVVRKGDEVVALPSGKGSKVKSIVTFEGELEQAGPGQAVTLTLEDEIDVSRGDMLVHADNRPLVTDGFDAMLVWMAEEPMLPGKKYDIKRATSYVPGSIPSIVHKVDVNTLERTPGSELKLNEIARVKVSLDAPIALDGYEQNRTTGAFIVIDRLTNGTVGAGMIVSAPPAAHGSSAHHGSNAHVTREERAGRFGQQPATVLFSGLSGAGKSTLAYAVERKLFDMGRAVYVLDGQNLRHDLNKGLPQDRAGRTENWLRTAHVAKQFNEAGLISLCAFVAPSAEGREQARALIGAERLITVYVQASPQVCRERDPQGLYAAGEDNIPGESFPYDVPLDADLVIDTQALSVEDGVKQVLDLLRERQAI
|
2.7.1.25; 2.7.7.4
| null |
cellular response to sulfate starvation [GO:0009970]; hydrogen sulfide biosynthetic process [GO:0070814]; phosphorylation [GO:0016310]; sulfate assimilation [GO:0000103]; sulfur compound metabolic process [GO:0006790]
| null |
adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; sulfate adenylyltransferase (ATP) activity [GO:0004781]; translation elongation factor activity [GO:0003746]
|
PF01583;PF00009;
|
3.40.50.300;2.40.30.10;
|
APS kinase family; TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, CysN/NodQ subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58243; EC=2.7.7.4; CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339, ChEBI:CHEBI:456216; EC=2.7.1.25;
| null |
PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.; PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
| null | null |
FUNCTION: With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD. {ECO:0000250}.; FUNCTION: APS kinase catalyzes the synthesis of activated sulfate. {ECO:0000250}.
|
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
|
O50406
|
DITCY_MYCTU
|
METFRTLLAKAALGNGISSTAYDTAWVAKLGQLDDELSDLALNWLCERQLPDGSWGAEFPFCYEDRLLSTLAAMISLTSNKHRRRRAAQVEKGLLALKNLTSGAFEGPQLDIKDATVGFELIAPTLMAEAARLGLAICHEESILGELVGVREQKLRKLGGSKINKHITAAFSVELAGQDGVGMLDVDNLQETNGSVKYSPSASAYFALHVKPGDKRALAYISSIIQAGDGGAPAFYQAEIFEIVWSLWNLSRTDIDLSDPEIVRTYLPYLDHVEQHWVRGRGVGWTGNSTLEDCDTTSVAYDVLSKFGRSPDIGAVLQFEDADWFRTYFHEVGPSISTNVHVLGALKQAGYDKCHPRVRKVLEFIRSSKEPGRFCWRDKWHRSAYYTTAHLICAASNYDDALCSDAIGWILNTQRPDGSWGFFDGQATAEETAYCIQALAHWQRHSGTSLSAQISRAGGWLSQHCEPPYAPLWIAKTLYCSATVVKAAILSALRLVDESNQ
|
5.5.1.16
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19618417};
|
cellular response to magnesium starvation [GO:0010350]; geranylgeranyl diphosphate metabolic process [GO:0033385]; gibberellin biosynthetic process [GO:0009686]; response to host immune response [GO:0052572]; tuberculosinol biosynthetic process [GO:0035440]
| null |
halimadienyl-diphosphate synthase activity [GO:0035439]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]
|
PF00432;PF13243;
|
1.50.10.160;1.50.10.20;
|
Terpene synthase family
| null | null |
CATALYTIC ACTIVITY: Reaction=geranylgeranyl diphosphate = tuberculosinyl diphosphate; Xref=Rhea:RHEA:25621, ChEBI:CHEBI:57533, ChEBI:CHEBI:58822; EC=5.5.1.16; Evidence={ECO:0000269|PubMed:15719101, ECO:0000269|PubMed:19618417};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.7 uM for GGPP (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:19618417}; Vmax=186 nmol/min/mg enzyme (at 30 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:19618417};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. Enzyme activity is not detected at pH values above 9.0. {ECO:0000269|PubMed:19618417};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:19618417};
|
FUNCTION: Catalyzes the formation of tuberculosinyl diphosphate from geranylgeranyl diphosphate (GGPP). It could also react with (14R/S)-14,15-oxidoGGPP to generate 3alpha- and 3beta-hydroxytuberculosinyl diphosphate. {ECO:0000269|PubMed:15719101, ECO:0000269|PubMed:19618417}.
|
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
O50580
|
DT3E_PSECI
|
MNKVGMFYTYWSTEWMVDFPATAKRIAGLGFDLMEISLGEFHNLSDAKKRELKAVADDLGLTVMCCIGLKSEYDFASPDKSVRDAGTEYVKRLLDDCHLLGAPVFAGLTFCAWPQSPPLDMKDKRPYVDRAIESVRRVIKVAEDYGIIYALEVVNRFEQWLCNDAKEAIAFADAVDSPACKVQLDTFHMNIEETSFRDAILACKGKMGHFHLGEANRLPPGEGRLPWDEIFGALKEIGYDGTIVMEPFMRKGGSVSRAVGVWRDMSNGATDEEMDERARRSLQFVRDKLA
|
5.1.3.31
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17936787, ECO:0000269|PubMed:25655925, ECO:0000269|Ref.2};
| null | null |
isomerase activity [GO:0016853]; metal ion binding [GO:0046872]
|
PF01261;
|
3.20.20.150;
|
Hyi family
| null | null |
CATALYTIC ACTIVITY: Reaction=keto-D-tagatose = keto-D-sorbose; Xref=Rhea:RHEA:43048, ChEBI:CHEBI:13022, ChEBI:CHEBI:47693; EC=5.1.3.31; Evidence={ECO:0000269|PubMed:25655925, ECO:0000269|Ref.2}; CATALYTIC ACTIVITY: Reaction=D-allulose = keto-D-fructose; Xref=Rhea:RHEA:42360, ChEBI:CHEBI:27605, ChEBI:CHEBI:48095; EC=5.1.3.31; Evidence={ECO:0000269|PubMed:25655925, ECO:0000269|Ref.2}; CATALYTIC ACTIVITY: Reaction=D-ribulose = D-xylulose; Xref=Rhea:RHEA:51544, ChEBI:CHEBI:17140, ChEBI:CHEBI:17173; EC=5.1.3.31; Evidence={ECO:0000269|Ref.2};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=55 mM for D-tagatose {ECO:0000269|Ref.2}; Vmax=30 umol/min/mg enzyme with D-tagatose as substrate {ECO:0000269|Ref.2};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 7 and 9 at 30 degrees Celsius. The enzyme is stable from 7 to 11 at 30 degrees Celsius. {ECO:0000269|Ref.2};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is around 60 degrees Celsius. The enzyme is stable up to 60 degrees Celsius for 10 minutes. {ECO:0000269|Ref.2};
|
FUNCTION: Catalyzes the epimerization of various ketoses at the C(3) position. It is able to interconvert D-tagatose and D-ribulose to D-sorbose and D-xylulose, respectively. The enzyme is also able to accept other ketopentoses such as D-psicose with lower efficiency. {ECO:0000269|PubMed:17936787, ECO:0000269|PubMed:25655925, ECO:0000269|Ref.2}.
|
Pseudomonas cichorii
|
O50657
|
DCLO_SELRU
|
MKNFRLSEKEVKTLAKRIPTPFLVASLDKVEENYQFMRRHLPRAGVFYAMKANPTPEILSLLAGLGSHFDVASAGEMEILHELGVDGSQMIYANPVKDARGLKAAADYNVRRFTFDDPSEIDKMAKAVPGADVLVRIAVRNNKALVDLNTKFGAPVEEALDLLKAAQDAGLHAMGICFHVGSQSLSTAAYEEALLVARRLFDEAEEMGMHLTDLDIGGGFPVPDAKGLNVDLAAMMEAINKQIDRLFPDTAVWTEPGRYMCGTAVNLVTSVIGTKTRGEQPWYILDEGIYGCFSGIMYDHWTYPLHCFGKGNKKPSTFGGPSCDGIDVLYRDFMAPELKIGDKVLVTEMGSYTSVSATRFNGFYLAPTIIFEDQPEYAARLTEDDDVKKKAAV
|
4.1.1.17; 4.1.1.18
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
|
putrescine biosynthetic process from ornithine [GO:0033387]; spermidine biosynthetic process [GO:0008295]
|
cytoplasm [GO:0005737]
|
lysine decarboxylase activity [GO:0008923]; ornithine decarboxylase activity [GO:0004586]
|
PF02784;PF00278;
|
3.20.20.10;
|
Orn/Lys/Arg decarboxylase class-II family
| null | null |
CATALYTIC ACTIVITY: Reaction=H(+) + L-lysine = cadaverine + CO2; Xref=Rhea:RHEA:22352, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:58384; EC=4.1.1.18; CATALYTIC ACTIVITY: Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911, ChEBI:CHEBI:326268; EC=4.1.1.17;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for L-lysine; KM=0.96 mM for L-ornithine;
|
PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
| null | null |
FUNCTION: Decarboxylates both L-lysine and L-ornithine with similar catalytic efficiency.
|
Selenomonas ruminantium
|
O51312
|
ENO_BORBU
|
MGFHIYEIKARQIIDSRGNPTVEADVILEDGTYGRAAVPSGASTGINEAVELRDGDKSVYMGKGVLKAIENIKNIIAPELEGMSALNQVAIDRKMLELDGTPTKEKLGANAILAVSMATAKAAAKYLGLRPYQYLGAYKANILPTPMCNIINGGAHSDNSVDFQEFMIMPIGAKTFSEAIRMAAEVFHTLKGILSGKGYATSVGDEGGFAPNLKSNEEACEVIIEAIKKAGYEPGKDIAIALDPATSELYDPKTKKYVLKWSTKEKLTSEQMVEYWAKWVEKYPIISIEDGMAEEDWDGWKKLTDKIGNKIQLVGDDLFVTNTSFLKKGIEMGVANSILIKVNQIGTLTETFEAVEMAKKAGYTAIVSHRSGETEDTTIADLVVALGTGQIKTGSLSRTDRIAKYNQLIRIEEELETTAEYHGKSVFYSIKQK
|
4.2.1.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00318}; Note=Binds a second Mg(2+) ion via substrate during catalysis. {ECO:0000255|HAMAP-Rule:MF_00318};
|
evasion of host immune response [GO:0042783]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; symbiont entry into host [GO:0044409]
|
cell surface [GO:0009986]; cytosol [GO:0005829]; external side of cell outer membrane [GO:0031240]; extracellular region [GO:0005576]; membrane [GO:0016020]; phosphopyruvate hydratase complex [GO:0000015]
|
magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]
|
PF00113;PF03952;
|
3.20.20.120;3.30.390.10;
|
Enolase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. {ECO:0000255|HAMAP-Rule:MF_00318}.
|
CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00318};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00318}.
| null | null |
FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP). It is essential for the degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318}.
|
Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
|
O51934
|
RGYR_THEMA
|
MAVNSKYHHSCINCGGLNTDERNERGLPCEVCLPEDSPSDIYRALLERKTLKEYRFYHEFWNEYEDFRSFFKKKFGKDLTGYQRLWAKRIVQGKSFTMVAPTGVGKTTFGMMTALWLARKGKKSALVFPTVTLVKQTLERLQKLADEKVKIFGFYSSMKKEEKEKFEKSFEEDDYHILVFSTQFVSKNREKLSQKRFDFVFVDDVDAVLKASRNIDTLLMMVGIPEEIIRKAFSTIKQGKIYERPKNLKPGILVVSSATAKPRGIRPLLFRDLLNFTVGRLVSVARNITHVRISSRSKEKLVELLEIFRDGILIFAQTEEEGKELYEYLKRFKFNVGETWSEFEKNFEDFKVGKINILIGVQAYYGKLTRGVDLPERIKYVIFWGTPSMRFSLELDKAPRFVLARVLKEMGLIKAQENPDVEELRKIAKEHLTQKEFVEKVKEMFRGVVVKDEDLELIIPDVYTYIQASGRSSRILNGVLVKGVSVIFEEDEEIFESLKTRLLLIAEEEIIEEAEANWKELVHEVEESRRRSERELTDTSRSLLIIVESPTKAETLSRFLGRASSRKERNIIVHEAVTGEGVILFTATRGHVYDLVTKGGIHGVEEENGKFVPVYNSLKRCRDCGYQFTEDRDECPVCSSKNIDDKTETLRALREISLEADEILVATDPDVEGEKISWDVTQYLLPSTRSLRRIEMHEITRYGFKKARESVRFVDFNLVKAQIVRRVQDRWIGFELSGKLQKRFGRSNLSAGRVQSTVLGWIVEREEEYKKSEKDFTLLVLENGVNLEVEGKIADDVVTVVELQEAEEEKNPLPPYTTSSALSEISQKLRLGVQEVMDILQDLFEKGFITYHRTDSTRISLEGQNVARTYLRKIGKEDIFMGRSWSTEGAHEAIRPVKPIDARELEEMIEEGLIADLTKKHLRVYELIFNRFLASQSAAVKVKKQIVTVDVDGKRMGIEQIVEILRDGWNLFVPLTVSPRFEHRTYKIKEKKFYKKHTVPLFTQASIVEEMKKRGIGRPSTYAKIVEVLFRRGYVYEDKYKRVRPTRFGVMVYSYLKERYEKYVTEETTRRLEEIMDKVERGEEDYQATLRLLYEEIKSLMEEG
|
5.6.2.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01125, ECO:0000269|PubMed:23209025, ECO:0000312|PDB:7FSE, ECO:0000312|PDB:7FSF, ECO:0000312|PDB:8OFB, ECO:0007744|PDB:4DDT, ECO:0007744|PDB:4DDU, ECO:0007744|PDB:4DDV, ECO:0007744|PDB:4DDW, ECO:0007744|PDB:4DDX}; Note=Binds 2 zinc ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01125, ECO:0000269|PubMed:23209025, ECO:0000312|PDB:7FSE, ECO:0000312|PDB:7FSF, ECO:0000312|PDB:8OFB, ECO:0007744|PDB:4DDT, ECO:0007744|PDB:4DDU, ECO:0007744|PDB:4DDV, ECO:0007744|PDB:4DDW, ECO:0007744|PDB:4DDX}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01125, ECO:0000269|PubMed:9440516};
|
DNA topological change [GO:0006265]; DNA unwinding involved in DNA replication [GO:0006268]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; reverse gyrase activity [GO:0160097]; zinc ion binding [GO:0008270]
|
PF00270;PF01131;PF01751;PF17915;
|
2.60.510.20;3.30.56.80;3.40.50.140;3.40.50.300;1.10.460.10;1.10.290.10;
|
DEAD box helicase family, DDVD subfamily; Type IA topoisomerase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01125}.
|
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:0000255|HAMAP-Rule:MF_01125, ECO:0000269|PubMed:18614530};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=44 uM for ATP without DNA {ECO:0000269|PubMed:21051354}; KM=12 uM for ATP with 60 base ssDNA {ECO:0000269|PubMed:21051354}; KM=16 uM for ATP with 60 bp dsDNA {ECO:0000269|PubMed:21051354}; KM=15.6 uM for ATP with negatively supercoiled plasmid dsDNA {ECO:0000269|PubMed:21051354}; KM=0.45 uM for ssDNA with ATP {ECO:0000269|PubMed:21051354}; KM=2.2 uM for ssDNA with ATP {ECO:0000269|PubMed:21051354}; Note=kcat is 0.02 sec(-1) in the absence of DNA, 0.108 sec(-1) with 60 base ssDNA, 0.117 sec(-1) with 60 bp dsDNA, 0.199 sec(-1) with plasmid dsDNA (PubMed:21051354). {ECO:0000269|PubMed:21051354};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 90 degrees Celsius for production of positive supercoils (PubMed:9440516). Thermostable for at least 4 hours at 85 degrees Celsius (PubMed:9440516). Optimum temperature is 65 degrees Celsius for ATPase activity (PubMed:18614530). The necessity for high temperature for positive supercoiling is probably because reverse gyrase preferentially binds to ssDNA (PubMed:21051354). {ECO:0000269|PubMed:18614530, ECO:0000269|PubMed:21051354, ECO:0000269|PubMed:9440516};
|
FUNCTION: Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process (PubMed:18614530, PubMed:21051354, PubMed:23209025, PubMed:9440516). Increases the linking number in steps of +1 (Probable) (PubMed:23209025). Probably recognizes regions with a low GC content which melt and form a ssDNA bubble, allowing the enzyme to bind and cleave the DNA prior to strand passage; the bubble is probably cleaved by 2 reverse gyrase molecules, one on each strand (Probable) (PubMed:32592697). Positively supercoils DNA with all NTPS, although it strongly prefers ATP (PubMed:18614530). In the presence of non-hydrolyzable ATP analogs it partially relaxes negative supercoils (PubMed:18614530, PubMed:21051354, PubMed:32592697). Has an intrinsic ATPase activity that is stimulated by DNA; ssDNA is most effective (PubMed:18614530, PubMed:21051354, PubMed:32592697). Binds to single-stranded DNA, transiently cleaves and then rejoins the ends, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate (Probable) (PubMed:18614530, PubMed:32592697). The helicase-like domain is a nucleotide-dependent switch that alternates between a physically closed ATP-bound state with a slight preference for dsDNA, and an open ADP-bound state with a high preference for ssDNA (PubMed:21350762). Whole enzyme has a very poor (k-unwind=0.001 sec(-1)) non-processive helicase activity in the 3'-5' direction that works on short substrates, while the isolated helicase domain has a slightly better helicase activity that works in both directions (PubMed:23123378). Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair and/or for DNA protection. {ECO:0000269|PubMed:18614530, ECO:0000269|PubMed:21051354, ECO:0000269|PubMed:21350762, ECO:0000269|PubMed:23123378, ECO:0000269|PubMed:23209025, ECO:0000269|PubMed:32592697, ECO:0000269|PubMed:9440516, ECO:0000305|PubMed:18614530, ECO:0000305|PubMed:23209025, ECO:0000305|PubMed:32592697}.
|
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
|
O52063
|
ATZC_PSESD
|
MSKDFDLIIRNAYLSEKDSVYDIGIVGDRIIKIEAKIEGTVKDEIDAKGNLVSPGFVDAHTHMDKSFTSTGERLPKFWSRPYTRDAAIEDGLKYYKNATHEEIKRHVIEHAHMQVLHGTLYTRTHVDVDSVAKTKAVEAVLEAKEELKDLIDIQVVAFAQSGFFVDLESESLIRKSLDMGCDLVGGVDPATRENNVEGSLDLCFKLAKEYDVDIDYHIHDIGTVGVYSINRLAQKTIENGYKGRVTTSHAWCFADAPSEWLDEAIPLYKDSGMKFVTCFSSTPPTMPVIKLLEAGINLGCASDNIRDFWVPFGNGDMVQGALIETQRLELKTNRDLGLIWKMITSEGARVLGIEKNYGIEVGKKADLVVLNSLSPQWAIIDQAKRLCVIKNGRIIVKDEVIVA
|
3.5.4.42
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12218024, ECO:0000269|PubMed:26390431, ECO:0000269|Ref.3}; Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000269|PubMed:12218024, ECO:0000269|PubMed:26390431, ECO:0000269|Ref.3};
|
atrazine catabolic process [GO:0019381]
|
cytoplasm [GO:0005737]
|
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines [GO:0016814]; metal ion binding [GO:0046872]; N-isopropylammelide isopropylaminohydrolase activity [GO:0018764]
|
PF07969;
|
3.20.20.140;2.30.40.10;
|
Metallo-dependent hydrolases superfamily, N-acyl-D-amino-acid deacylase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + H2O + N-isopropylammelide = cyanurate + isopropylamine; Xref=Rhea:RHEA:23608, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17247, ChEBI:CHEBI:38028, ChEBI:CHEBI:57492; EC=3.5.4.42; Evidence={ECO:0000269|PubMed:12218024, ECO:0000269|PubMed:26390431};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=817 uM for N-methylammelide {ECO:0000269|PubMed:12218024}; KM=308 uM for N-ethylammelide {ECO:0000269|PubMed:12218024}; KM=3860 uM for N-hydroxyethylammelide {ECO:0000269|PubMed:12218024}; KM=406 uM for N-isopropylammelide {ECO:0000269|PubMed:12218024}; KM=580 uM for N-cyclopropylammelide {ECO:0000269|PubMed:12218024}; KM=299 uM for N-t-butylammelide {ECO:0000269|PubMed:12218024}; KM=155 uM for N-dimethylammelide {ECO:0000269|PubMed:12218024}; KM=1320 uM for ammelide {ECO:0000269|PubMed:12218024}; Note=kcat is 178 sec(-1) for N-methylammelide. kcat is 209 sec(-1) for N-ethylammelide. kcat is 80.6 sec(-1) for N-hydroxyethylammelide. kcat is 13.3 sec(-1) for N-isopropylammelide. kcat is 98.2 sec(-1) for N-cyclopropylammelide. kcat is 0.07 sec(-1) for N-t-butylammelide. kcat is 10.7 sec(-1) for N-dimethylammelide. kcat is 1.65 sec(-1) for ammelide. {ECO:0000269|PubMed:12218024};
|
PATHWAY: Xenobiotic degradation; atrazine degradation; cyanurate from atrazine: step 3/3.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.25. {ECO:0000269|PubMed:26390431};
| null |
FUNCTION: Transforms N-isopropylammelide to cyanuric acid and isopropylamine. {ECO:0000269|PubMed:12218024, ECO:0000269|PubMed:9422605}.
|
Pseudomonas sp. (strain ADP)
|
O52378
|
NAGAA_RALSP
|
MELVVEPLNLHLNAETGSTLLDVLRSNEVPISYSCMSGRCGTCRCRVIAGHLRDNGPETGRPQAGKGTYVLACQAVLTEDCTIEIPESDEIVVHPARIVKGTVTAIDEATHDIRRLRIKLAKPLEFSPGQYATVQFTPECVRPYSMAGLPSDAEMEFQIRAVPGGHVSNYVFNELSVGASVRISGPLGTAYLRRTHTGPMLCVGGGTGLAPVLSIVRGALESGMSNPIHLYFGVRSEQDIYDEERLHALAARFPNLKVNVVVATGPAGPGRRSGLVTDLIGRDLPNLAGWRAYLCGAPAMVEALNLLVARLGIVPGHIHADAFYPSGV
|
1.18.1.7
|
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:Q52126, ECO:0000255|PROSITE-ProRule:PRU00465}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00465}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q52126};
|
electron transport chain [GO:0022900]; naphthalene catabolic process [GO:1901170]; salicylic acid catabolic process [GO:0046244]
|
catalytic complex [GO:1902494]
|
2 iron, 2 sulfur cluster binding [GO:0051537]; ferredoxin-NAD+ reductase activity [GO:0008860]; ferredoxin-NADP+ reductase activity [GO:0004324]; metal ion binding [GO:0046872]
|
PF00970;PF00111;PF00175;
|
3.10.20.30;3.40.50.80;2.40.30.10;
|
Bacterial ring-hydroxylating dioxygenase ferredoxin reductase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.18.1.7; Evidence={ECO:0000269|PubMed:11872705}; CATALYTIC ACTIVITY: Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.18.1.7; Evidence={ECO:0000269|PubMed:11872705};
| null |
PATHWAY: Aromatic compound metabolism; naphthalene degradation. {ECO:0000269|PubMed:11872705, ECO:0000269|PubMed:9573207}.
| null | null |
FUNCTION: Component of two multicomponent enzyme systems which are involved in the catabolism of naphthalene (PubMed:11872705, PubMed:9573207). Plays a role as an electron transfer component for both salicylate 5-hydroxylase (S5H) and naphthalene 1,2-dioxygenase (NDO) systems, by transferring electrons from NAD(P)H to the oxygenase component via the ferredoxin NagAb (PubMed:11872705, PubMed:9573207). The electron transport chain from the two systems can use both NADH and NADPH as electron donors at approximately similar rates (PubMed:11872705). {ECO:0000269|PubMed:11872705, ECO:0000269|PubMed:9573207}.
|
Ralstonia sp
|
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