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 |
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O46600 | GHR_BOVIN | MDLWQLLLTLAVAGSSDAFSGSEATPAFLVRASQSLQILYPVLETNSSGNPKFTKCRSPELETFSCHWTDGANHSLQSPGSVQMFYIRRDIQEWKECPDYVSAGENSCYFNSSYTSVWTPYCIKLTSNGGIVDHKCFSVEDIVQPDPPVGLNWTLLNISLTEIHADILVKWEPPPNTDVKMGWIILEYELHYKELNETQWKMMDPLMVTSVPMYSLRLDKEYEVRVRTRQRNTEKYGKFSEVLLITFPQMNPSACEEDFQFPWFLIIIFGILGLAVTLYLLIFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNT... | 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]: ... | 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 G... | Bos taurus (Bovine) |
O46606 | DDHD1_BOVIN | MNYPGHGSPRSSERNGGRGGDGAAWELGSDTEPAFGGSVCRFDHLPVGEPGDDEVPLALLRGEPGLHLAPGAEDHNHHLALDPCLSDDNYDFSSAESGSSLRYYSEGESGGGGSSSSLHPPQQPLVPSNSGGGGAAGGGPGERKRTRPGGAAARHRYEVVTELGPEEVRWFYKEDKKTWKPFIGYDSLRIELAFRTLLQATGARARAQDPDGDHVCGPASPAGPASSSVEDEDEDRVCGFCPRIAGHGREMEELVNIERVCVRGGLYEVDVTQGECYPVYWNQSDKIPVMRGQWFIDGTWQPLEEEESNLIEQEHLSRFR... | 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:79... | 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 hydrol... | Bos taurus (Bovine) |
O46629 | ECHB_BOVIN | MISLLTYTLKNLPNTSKWALRFCMRPLSSSSQLQAAAASQTKSKKTLAKPNIRNIVVVDGVRTPFLLSGTSYKDLMPHDLARAALSGLLHRTSVPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDIPIRHSRKMRKMMLDLNKAKTLAQRLSIISKFRLNFLSPELPAVSEFSTSETMGHSADRLAAAFAISREEQDEYALRSHSLAKKAQDEGLLSDVVPFKVPGRDTVTQDNGIRPSSLDQMAKLKPAFIKPYGTVTAANSSFLTDGASAVL... | 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:00... | 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|UniProt... | 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... | Bos taurus (Bovine) |
O46631 | SHPS1_BOVIN | MEPARPAPGRLRPLLCLLLAASNAWTGTAGDGELQVIQPERSVSVAAGETATLHCTVTSLSPVGPIKWFKGTGPGREFIYSQKEAPFPRVTNVSDATKRNNMDFSIRISNITPADAGVYYCVKFRKEERGDMEFKSGPGTHLTVSAKPSPPVLSGPTVRATPEQTVNFTCTSHGFSPRNISLKWFKNGNELSASQTSVDPEDNNVSYSINSTTKVLLATGDVHSQVICEVAHVTLQGGPPLRGTANLSETIRVPPTLEITGSPSAGNQVNVTCQVNKFYPRHLQLTWLENGNMSRTEAASVFVENKDGTFNQTSWFLVNS... | 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 ... | Bos taurus (Bovine) |
O46635 | 5HT2A_CANLF | MDVLFEDNAPLSPTTSSLMPSNGDPRLYGNDLNAGDANTSDAFNWTVDAENRTNLSCEGCLSPPCFSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDPGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYGRRTMQSISNEQKA... | 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... | 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... | 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 tha... | Canis lupus familiaris (Dog) (Canis familiaris) |
O46647 | LIPL_NEOVI | MESKALLLVALGMWFQSLTATRGGVAAADRGGDFIDIESKFALRTPEDTAEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGKDVAKFINWMAEEFHYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKV... | 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 synth... | 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 triglyc... | Neovison vison (American mink) (Mustela vison) |
O46658 | CP2DP_PIG | MGLLTGDLLGILALAMVIFLLLVDLMHRRSRWAPRYPPGPMPLPGLGNLLQVNFQDPRLSFIQLRRRFGDVFSLQQIWRPVVVLNGLAAVREALVSHSHETSDRPPVFILEHLGYGPRSEGVILARYGKAWREQRRFSVSTLRNFGLGKKSLEEWVTQEASCLCAAFADQAGRPFSPNNLLNKAVSNVIASLTFARRFEYNDPRMLKLLDLVLEGLKEEVGLMRQVLEAMPVLRHIPGLCAKLFPRQKAFLVMIDELITEHKMTRDLAQPPRDLTDAFLDEMKEAKGNPESSFNDENLRLVVAHLFSAGMITTSTTLAWA... | 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 fla... | 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:CH... | 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 | MEFPFGSLETTNFRRFTPESLVEIEKRIAAKQAAKKAKGKHREQKDQEEKPRPQLDLKACNQPPKFYGELPAELVGEPLEDLDPFYSTHRTFMVLDKGRTISRFSATRALWLFSPFNLIRRTAIKVSVHSWFSLFITVTILVNCVGMTQTELPDRIEYVFTVIYTFEALIKILARGFCLNEFAYLRDPWDWLDFSVITLAYIGEATALRGISGLRTFRVLRALKTVSVIPGLKVIVGALIHSVRKLADVTILTVFCLSVFALVGLQLFKGNLKNKCVKNCAALNETGNYSSYGKQEWNFCHRDEDFYYNKPGTSDPLLCG... | 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... | 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 wi... | Canis lupus familiaris (Dog) (Canis familiaris) |
O46674 | AT2A2_CANLF | MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLA... | 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]; regulati... | 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|U... | 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;... | 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 ... | Canis lupus familiaris (Dog) (Canis familiaris) |
O46680 | TGFR1_BOVIN | MEAAAATPRPRLFLLMLAAAATLVPEATPLQCFCHLCTKDNFTCVTDGLCFVSVTETTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGSITTTYCCNQDHCNKIELPTVGKPSSGLGPVELAAVIAGPVCFVCISLMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQ... | 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]; hear... | 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... | 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: Rea... | 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 plethor... | 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 membran... | 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:000025... | 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 simila... | 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 nucle... | 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/... | Arabidopsis thaliana (Mouse-ear cress) |
O48538 | RBOHF_ARATH | MKPFSKNDRRRWSFDSVSAGKTAVGSASTSPGTEYSINGDQEFVEVTIDLQDDDTIVLRSVEPATAINVIGDISDDNTGIMTPVSISRSPTMKRTSSNRFRQFSQELKAEAVAKAKQLSQELKRFSWSRSFSGNLTTTSTAANQSGGAGGGLVNSALEARALRKQRAQLDRTRSSAQRALRGLRFISNKQKNVDGWNDVQSNFEKFEKNGYIYRSDFAQCIGMKDSKEFALELFDALSRRRRLKVEKINHDELYEYWSQINDESFDSRLQIFFDIVDKNEDGRITEEEVKEIIMLSASANKLSRLKEQAEEYAALIMEEL... | 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]; osmosenso... | 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-depend... | Arabidopsis thaliana (Mouse-ear cress) |
O48573 | LAZ5_ARATH | MAASSEILPESWQVFINFRGADLRNGFISHLAGALTSAGITYYIDTEEVPSEDLTVLFKRIEESEIALSIFSSNYAESKWCLDELVKIMEQVKKGKLRIMPVFFNVKPEEVREQNGEFGLKLYGEGKSKRPNIPNWENALRSVPSKIGLNLANFRNEKELLDKIIDSIKKVLARITRASRVAESLNGISKDSEAKNVDTFSPNSSDFPSTSIDDDLSINSPQYQATIPPASREGERLNTISTVSSTGSIEHPPPNYGIEPRLKEMEEKLDFDSLETKTVGIVGMPGIGKTTLAETLYRKWEHKFERSMFFPDASKMANEH... | 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; Ev... | 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 | MAATFLPATSLRLTQNSTLRFLSFFTISNPSYSLFRPLRRRVLPPFDAFPANSRRRCFCTAVSESLGSGDGNKVESYEKRFGSKVGEFRKKLRIAEVKGGADEGLSRVGQSLNIMGWVRTLRSQSSVTFIEINDGSCLSNLQCVMTSDAEGYDQVESGSILTGASVSVQGTIVASQGTKQKVELKVEKIIVVGECDSSYPIQKKRVSREFLRTKAHLRPRTNTFGAVARVRNTLAYATHKFFQESGFVWVASPIITASDCEGAGEQFCVTTLIPSSHENTDTSIDAIPKTKGGLIDWSQDFFGKPAFLTVSGQLNGETYA... | 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... | null | null | null | null | null | Arabidopsis thaliana (Mouse-ear cress) |
O48626 | ZW10_ARATH | MPEIDALFESINVRDLLAGHDLNDPTTPLSAPDLRLLINRLESHSLRIKSKVQSYLVAHHSDFSELFSLCQDTVSRTRLISDDVSDVLQLVSDRPIDVEIRSVVDEITEKTKEVKLKRESLDLVNAIVGICEALQETKEALKNGRFRFAAERIRELKVVLRIGEEEDGEPVAYALLRKEWSNCFDEIQEVLAKFMENAVRFELDSSRIRIKYQLSVGETAGIALSTVLEAMEVIGILDYGLAKAADSIFKHVITPAVTHASTFAAVEDLCKSAGEVTEATLRLEQSSDHKFEDVDGDAMYSGILKVVKFICSSLCFGNVT... | 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 spind... | 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 | MNSSSSTTTTDTLHSFMEASALLIDQYFLGWIFAFLFGFLLLLNFKRKREKNNSTEFGTDDSNGYYTPENIAGSTDVIIVGAGVAGSALAYTLANDGRRVHVIERDLTEQDRIVGELLQPGGYLKLIELGLEDCVNEIDAQRVFGYALYMDGKNTRLSYPLEKFHSDVAGRSFHNGRFVQRMREKAASLPNVRMEQGTVTSLVEKKGSVKGVQYKTKDGQELSAFAPLTIVCDGCFSNLRRSLCNPKVEVPSCFVGLILENIDLPHINHGHVILADPSPILFYKISSTEIRCLVDVPGQKVPCISNGELANYLKTVVAPQ... | 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:1902... | 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:15... | 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... | Panax ginseng (Korean ginseng) |
O48652 | UVR3_ARATH | MQRFCVCSPSSYRLNPITSMATGSGSLIWFRKGLRVHDNPALEYASKGSEFMYPVFVIDPHYMESDPSAFSPGSSRAGVNRIRFLLESLKDLDSSLKKLGSRLLVFKGEPGEVLVRCLQEWKVKRLCFEYDTDPYYQALDVKVKDYASSTGVEVFSPVSHTLFNPAHIIEKNGGKPPLSYQSFLKVAGEPSCAKSELVMSYSSLPPIGDIGNLGISEVPSLEELGYKDDEQADWTPFRGGESEALKRLTKSISDKAWVANFEKPKGDPSAFLKPATTVMSPYLKFGCLSSRYFYQCLQNIYKDVKKHTSPPVSLLGQLLW... | 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 ... | Arabidopsis thaliana (Mouse-ear cress) |
O48653 | DPOLA_ORYSJ | MDEGSADAGASGRRSRARGSEAVARSAALERLRAIRDGGARAAAAVQVRIEAPIYDTVAEEDYAALVARRRKDAGAFIVDDDGLGYADDGREEDWTHRTIHSSSDEGSDGEDGAPRKRKQPRPQSKRPPQQSAAAASLSAAAAMMGKQRLSSMFTSSVFRKPGSDRGRDSSLAADSIVDDVIAEFAPDDNDREERRRRVGRVCAPAPAPTTTAHIKAENVAVDTAMAFRSDNVFEAHEVSDHGNDMDMELKPDVEMEPKLDTPLGASAELANNSNSLEEPKQEANGEVKIEKVHRLNAKIKTEDSRNGDMASATAGWMKI... | 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 | MGSLGAILKHPEDFYPLLKLKFAARHAEKQIPPEPHWAFCYSMLHKVSRSFGLVIQQLGPQLRDAVCIFYLVLRALDTVEDDTSIPTEVKVPILMAFHRHIYDKDWHFSCGTKEYKVLMDEFHHVSNAFLELGSGYQEAIEDITMRMGAGMAKFICKEVETINDYDEYCHYVAGLVGLGLSKLFHASGAEDLATDSLSNSMGLFLQKTNIIRDYLEDINEIPKSRMFWPRQIWSKYVDKLEDLKYEENSAKAVQCLNDMVTDALVHAEDCLKYMSDLRGPAIFRFCAIPQIMAIGTLALCFNNTQVFRGVVKMRRGLTAK... | 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]; res... | 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}; PhysiologicalDirec... | 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 | MAETTPKVKGHVVILPYPVQGHLNPMVQFAKRLVSKNVKVTIATTTYTASSITTPSLSVEPISDGFDFIPIGIPGFSVDTYSESFKLNGSETLTLLIEKFKSTDSPIDCLIYDSFLPWGLEVARSMELSAASFFTNNLTVCSVLRKFSNGDFPLPADPNSAPFRIRGLPSLSYDELPSFVGRHWLTHPEHGRVLLNQFPNHENADWLFVNGFEGLEETQDCENGESDAMKATLIGPMIPSAYLDDRMEDDKDYGASLLKPISKECMEWLETKQAQSVAFVSFGSFGILFEKQLAEVAIALQESDLNFLWVIKEAHIAKLP... | 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-glucosylt... | 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-(met... | 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 hy... | Arabidopsis thaliana (Mouse-ear cress) |
O48709 | PI5K3_ARATH | MQETVFLFTEENLNKEQSLGVKYKQSSRRVVPMTSCEVSDTAAEIRIVEKVLKNGDLYNGGLSAGVPHGTGKYLWSDGCMYEGEWTRGKASGKGRFSWPSGATYEGQFKDGRMDGEGTFIGIDGDTYRGHWLWGRKHGYGEKRYANGDGYQGNWKANLQDGNGRYVWSDGNEYVGEWKNGVISGKGKMTWANGNRYDGLWENGAPVGKGVLSWGEEKTSYNGWGRKSKKKDEEIVQNHKLSSVETLSANTNFPRICISELEDTGVCDHVEASPYTSESDTSGCGEQEWARSPLLLESGGAMSVQQSPRWLDEGDVKKPGH... | 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; Evide... | 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... | Arabidopsis thaliana (Mouse-ear cress) |
O48711 | PME12_ARATH | MALSSFNLSSLLFLLFFTPSVFSYSYQPSLNPHETSATSFCKNTPYPDACFTSLKLSISINISPNILSFLLQTLQTALSEAGKLTDLLSGAGVSNNLVEGQRGSLQDCKDLHHITSSFLKRSISKIQDGVNDSRKLADARAYLSAALTNKITCLEGLESASGPLKPKLVTSFTTTYKHISNSLSALPKQRRTTNPKTGGNTKNRRLLGLFPDWVYKKDHRFLEDSSDGYDEYDPSESLVVAADGTGNFSTINEAISFAPNMSNDRVLIYVKEGVYDENIDIPIYKTNIVLIGDGSDVTFITGNRSVGDGWTTFRSATLAV... | 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 | MQMDSPKSPLQPPTYGNLVTILSIDGGGIRGLIPAVILGFLESELQKLDGEEARLADYFDVIAGTSTGGLVTAMLTAPNKEGRPLFAASEIKDFYLEQCPKIFPQDHFPFSAAKKLVKSLTGPKYDGKYLHQLIHAKLGDTKLSQTLTNVVIPTFDIKHLQPTIFSSYEVKNHPLKDATLADIAISTSAAPTYLPAHFFKVEDLNGNAKEYNLIDGGVAANNPALLAIGEVTNEISGGSSDFFPIRPNDYGRFLVLSLGTGNHKAEEKFNAKEVAGWGLLNWLTHDNSTPIIDAFSQASSDMVDFHLSAVFRALHSEANY... | 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... | 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), ph... | 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... | Arabidopsis thaliana (Mouse-ear cress) |
O48741 | PORC_ARATH | MALQAAYSLLPSTISIQKEGKFNASLKETTFTGSSFSNHLRAEKISTLLTIKEQRRQKPRFSTGIRAQTVTATPPANEASPEQKKTERKGTAVITGASSGLGLATAKALADTGKWHVIMACRNFLKAEKAARSVGMSKEDYTVMHLDLASLESVKQFVENFRRTEQPLDVLVCNAAVYQPTAKEPSFTAEGFEISVGTNHLGHFLLSRLLLDDLKKSDYPSKRMIIVGSITGNTNTLAGNVPPKANLGDLRGLASGLNGQNSSMIDGGEFDGAKAYKDSKVCNMLTMQELHRRYHEETGVTFASLYPGCIATTGLFREHI... | 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 | MYKSPLTLLTLLTICFGFFDLSSALYGSSSPVVQLTASNFKSKVLNSNGVVLVEFFAPWCGHCKALTPTWEKVANILKGVATVAAIDADAHQSAAQDYGIKGFPTIKVFVPGKAPIDYQGARDAKSIANFAYKQIKGLLSDRLEGKSKPTGGGSKEKKSEPSASVELNASNFDDLVIESNELWIVEFFAPWCGHCKKLAPEWKRAAKNLQGKVKLGHVNCDVEQSIMSRFKVQGFPTILVFGPDKSSPYPYEGARSASAIESFASELVESSAGPVEVTELTGPDVMEKKCGSAAICFISFLPDILDSKAEGRNKYLEMLL... | 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 grow... | 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:1724... | 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 w... | Arabidopsis thaliana (Mouse-ear cress) |
O48791 | SCAB1_ARATH | MTRVTRDFRDSLQRDGVPAVSADVKFASSRFPNYRIGANDQIFDVKDDPKVMSMKEVVARETAQLMDQQKRLSVRDLAHKFEKGLAAAAKLSEEAKLKEATSLEKHVLLKKLRDALESLRGRVAGRNKDDVEEAIAMVEALAVQLTQREGELFIEKAEVKKLASFLKQASEDAKKLVDEERAFARAEIESARAAVQRVEEALREHEQMSRASGKQDMEDLMKEVQEARRIKMLHQPSRVMDMEYELRALRNQLAEKSKHFLQLQKKLAMCRKSEENISLVYEIDGTEALGSCLRVRPCSNDAPDLSKCTIQWYRSSSDGS... | 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:... | Arabidopsis thaliana (Mouse-ear cress) |
O48802 | PHOX2_ARATH | MGKSGGRKKKSGGSNSNSSQVNSSETSGLSKPSTIVNGGVDFDASIFLKRAHELKEEGNKKFQARDYVGALEQYENGIKLIPKSHPDRAVFHSNRAACLMQMKPIDYESVISECSMALKSQPGFTRALLRRARAFEAVGKFDLAVQDVNVLLGSDPNHKDAGEISKRLKTALGPHQDLQSRPSPAALGASAALGGPIAGLGPCLPSRNVHKKGVTSPVGSVSLPNASNGKVERPQVVNPVTENGGSVSKGQASRVVLKPVSHSPKGSKVEELGSSSVAVVGKVQEKRIRWRPLKFVYDHDIRLGQMPVNCRFKELREIVS... | 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:2809... | Arabidopsis thaliana (Mouse-ear cress) |
O48814 | BIK1_ARATH | MGSCFSSRVKADIFHNGKSSDLYGLSLSSRKSSSTVAAAQKTEGEILSSTPVKSFTFNELKLATRNFRPDSVIGEGGFGCVFKGWLDESTLTPTKPGTGLVIAVKKLNQEGFQGHREWLTEINYLGQLSHPNLVKLIGYCLEDEHRLLVYEFMQKGSLENHLFRRGAYFKPLPWFLRVNVALDAAKGLAFLHSDPVKVIYRDIKASNILLDADYNAKLSDFGLARDGPMGDLSYVSTRVMGTYGYAAPEYMSSGHLNARSDVYSFGVLLLEILSGKRALDHNRPAKEENLVDWARPYLTSKRKVLLIVDNRLDTQYLPEE... | 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];... | 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:225041... | 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:... | 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... | 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... | Arabidopsis thaliana (Mouse-ear cress) |
O48847 | LUH_ARATH | MAQSNWEADKMLDVYIYDYLVKKKLHNTAKSFMTEGKVSPDPVAIDAPGGFLFEWWSVFWDIFIARTNEKHSEAAAAYIEAQQGKAKEQQMQIQQLQMMRQAQMQRRDPNHPSLGGPMNAIGSEGMIGQSNASALAAKMYEERMKQPNPMNSETSQPHLDARMALLKSATNHHGQIVQGNHQGGVSAALQQIQSRTQQPTEIKTEVNLGTSPRQLPVDPSTVYGQGILQSKPGMGSAGLNPGVSGLPLKGWPLTGIEQMRPGLGGPQVQKSFLQNQSQFQLSPQQQQHQMLAQVQAQGNMTNSPMYGGDMDPRRFTGLPR... | 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... | 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 condensat... | Arabidopsis thaliana (Mouse-ear cress) |
O48849 | RLP23_ARATH | MSKALLHLHFLSLFLLCCVCHSSIFTLNFHFTGIVACRPHQIQAFTKFTNEFDTRGCNNSDTFNGVWCDNSTGAVAVLQLRKCLSGTLKSNSSLFGFHQLRYVDLQNNNLTSSSLPSGFGNLKRLEGLFLSSNGFLGQVPSSFSNLTMLAQLDLSYNKLTGSFPLVRGLRKLIVLDLSYNHFSGTLNPNSSLFELHQLRYLNLAFNNFSSSLPSKFGNLHRLENLILSSNGFSGQVPSTISNLTRLTKLYLDQNKLTSSFPLVQNLTNLYELDLSYNKFFGVIPSSLLTLPFLAHLALRENNLAGSVEVSNSSTSSRLEI... | 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:014... | 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 | MQSLGGIRSWPATWRTTTASMTTTTTESVRKVAQVLTVAGSDSGAGAGIQADIKVCAARGVYCASVKTAVKAKNTRAVQSVHLLPPDSVSEQLKSVLSDFEVDVVKTGMLPSPEIVEVLLQNLSEYPVRALVVDPVMVSTSGHVLAGSSILSIFRERLLPLADIITPNVKEASALLGGVRIQTVAEMRSAAKSLHQMGPRFVLVKGGDLPDSSDSVDVYFDGNEFHELHSPRIATRNTHGTGCTLASCIAAELAKGSNMLSAVKVAKRFVDSALNYSKDIVIGSGMQGPFDHFLSLKDPQSYRQSTFKPDDLFLYAVTDS... | 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, ChEB... | 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-p... | 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 ... | 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) a... | Arabidopsis thaliana (Mouse-ear cress) |
O48917 | SQD1_ARATH | MAHLLSASCPSVISLSSSSSKNSVKPFVSGQTFFNAQLLSRSSLKGLLFQEKKPRKSCVFRATAVPITQQAPPETSTNNSSSKPKRVMVIGGDGYCGWATALHLSKKNYEVCIVDNLVRRLFDHQLGLESLTPIASIHDRISRWKALTGKSIELYVGDICDFEFLAESFKSFEPDSVVHFGEQRSAPYSMIDRSRAVYTQHNNVIGTLNVLFAIKEFGEECHLVKLGTMGEYGTPNIDIEEGYITITHNGRTDTLPYPKQASSFYHLSKVHDSHNIAFTCKAWGIRATDLNQGVVYGVKTDETEMHEELRNRLDYDAVFG... | 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 | MEASAGLVAGSYRRNELVRIRHESDGGTKPLKNMNGQICQICGDDVGLAETGDVFVACNECAFPVCRPCYEYERKDGTQCCPQCKTRFRRHRGSPRVEGDEDEDDVDDIENEFNYAQGANKARHQRHGEEFSSSSRHESQPIPLLTHGHTVSGEIRTPDTQSVRTTSGPLGPSDRNAISSPYIDPRQPVPVRIVDPSKDLNSYGLGNVDWKERVEGWKLKQEKNMLQMTGKYHEGKGGEIEGTGSNGEELQMADDTRLPMSRVVPIPSSRLTPYRVVIILRLIILCFFLQYRTTHPVKNAYPLWLTSVICEIWFAFSWLL... | 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, E... | 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 com... | Arabidopsis thaliana (Mouse-ear cress) |
O48947 | CESA2_ARATH | MNTGGRLIAGSHNRNEFVLINADESARIRSVQELSGQTCQICGDEIELTVSSELFVACNECAFPVCRPCYEYERREGNQACPQCKTRYKRIKGSPRVDGDDEEEEDIDDLEYEFDHGMDPEHAAEAALSSRLNTGRGGLDSAPPGSQIPLLTYCDEDADMYSDRHALIVPPSTGYGNRVYPAPFTDSSAPPQARSMVPQKDIAEYGYGSVAWKDRMEVWKRRQGEKLQVIKHEGGNNGRGSNDDDELDDPDMPMMDEGRQPLSRKLPIRSSRINPYRMLILCRLAILGLFFHYRILHPVNDAYGLWLTSVICEIWFAVSW... | 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 | MEPTEKPSTKPSSRTLPRDTRGSLEVFNPSTQLTRPDNPVFRPEPPAWQNLSDPRGTSPQPRPQQEPAPSNPVRSDQEIAVTTSWMALKDPSPETISKKTITAEKPQKSAVAAEQRAAEWGLVLKTDTKTGKPQGVGVRNSGGTENDPNGKKTTSQRNSQNSCRSSGEMSDGDVPGGRSGIPRVSEDLKDALSTFQQTFVVSDATKPDYPIMYASAGFFNMTGYTSKEVVGRNCRFLQGSGTDADELAKIRETLAAGNNYCGRILNYKKDGTSFWNLLTIAPIKDESGKVLKFIGMQVEVSKHTEGAKEKALRPNGLPES... | 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]; regulat... | 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... | 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 exposu... | 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:000026... | 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 sto... | Arabidopsis thaliana (Mouse-ear cress) |
O49006 | PME3_ARATH | MAPSMKEIFSKDNFKKNKKLVLLSAAVALLFVAAVAGISAGASKANEKRTLSPSSHAVLRSSCSSTRYPELCISAVVTAGGVELTSQKDVIEASVNLTITAVEHNYFTVKKLIKKRKGLTPREKTALHDCLETIDETLDELHETVEDLHLYPTKKTLREHAGDLKTLISSAITNQETCLDGFSHDDADKQVRKALLKGQIHVEHMCSNALAMIKNMTDTDIANFEQKAKITSNNRKLKEENQETTVAVDIAGAGELDSEGWPTWLSAGDRRLLQGSGVKADATVAADGSGTFKTVAAAVAAAPENSNKRYVIHIKAGVYR... | 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]; reg... | 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;... | 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.... | 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 ... | Arabidopsis thaliana (Mouse-ear cress) |
O49048 | VPS45_ARATH | MVLVTSVRDYINRMLQDISGMKVLILDSETVSNVSIVYSQSELLQKEVFLVEMIDSISVSKESMSHLKAVYFIRPTSDNIQKLRYQLANPRFGEYHLFFSNLLKDTQIHILADSDEQEVVQQVQEYYADFVSGDPYHFTLNMASNHLYMIPAVVDPSGLQRFSDRVVDGIAAVFLALKRRPVIRYQRTSDTAKRIAHETAKLMYQHESALFDFRRTESSPLLLVIDRRDDPVTPLLNQWTYQAMVHELIGLQDNKVDLKSIGSLPKDQQVEVVLSSEQDAFFKSNMYENFGDIGMNIKRMVDDFQQVAKSNQNIQTVEDM... | 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]; vesi... | 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 v... | Arabidopsis thaliana (Mouse-ear cress) |
O49139 | CMT1_ARATH | MAARNKQKKRAEPESDLCFAGKPMSVVESTIRWPHRYQSKKTKLQAPTKKPANKGGKKEDEEIIKQAKCHFDKALVDGVLINLNDDVYVTGLPGKLKFIAKVIELFEADDGVPYCRFRWYYRPEDTLIERFSHLVQPKRVFLSNDENDNPLTCIWSKVNIAKVPLPKITSRIEQRVIPPCDYYYDMKYEVPYLNFTSADDGSDASSSLSSDSALNCFENLHKDEKFLLDLYSGCGAMSTGFCMGASISGVKLITKWSVDINKFACDSLKLNHPETEVRNEAAEDFLALLKEWKRLCEKFSLVSSTEPVESISELEDEEVE... | 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.... | 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 | MAEKESNGVRVCVTGGAGFIGSWLVRKLLEKGYTVHATLRNTGDEAKAGLLRRLVPGAAERLRLFQADLFDAATFAPAIAGCQFVFLVATPFGLDSAGSQYKSTAEAVVDAVHAILRQCEESRTVKRVIHTASVAAASPLLEEEVPASGVGYRDFIDESCWTSLNVDYPLRSAHFDKYILSKLQSEQELLSYNNGESPAFEVVTLPLGLVAGDTVLGRAPETVESAVAPVSRSEPYFGLLRILQQLLGSLPLVHVDDVCDALVFCMERRPSVAGRFLCAAAYPTIHDVVAHYASKFPHLDILKETTEAVATVRPARDRLG... | 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.ca... | 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 ribonucleosid... | 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 | MEVCNCIEPQWPADELLMKYQYISDFFIAVAYFSIPLELIYFVKKSAVFPYRWVLVQFGAFIVLCGATHLINLWTFTTHSRTVALVMTTAKVLTAVVSCATALMLVHIIPDLLSVKTRELFLKNKAAELDREMGLIRTQEETGRHVRMLTHEIRSTLDRHTILKTTLVELGRTLALEECALWMPTRTGLELQLSYTLRQQHPVEYTVPIQLPVINQVFGTSRAVKISPNSPVARLRPVSGKYLLGEVVAVRVPLLHLSNFQINDWPELSTKRYALMVLMLPSDSARQWHVHELELVEVVADQVAVALSHAAILEESMRAR... | 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 ... | 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... | Arabidopsis thaliana (Mouse-ear cress) |
O49326 | JAL21_ARATH | MVQKVEARGGEIGDVWDDGAYDGVRKVYVGQGEDGIAFVKFEYVNGSQEVVGDERGKKTLLGAEEFEVDPDDYIVYVEGYHEKVFGVTTKEIISTLTFKTYKGKTSPPFGIVSGTKFVLQGGKIVGFHGRSTDVLHSLGAYISSPATPKLRGKWIKVEQKGEGPGPRCSHDIAQVGNKIFSFGGELTPNQPIDKHLYVFDLETRTWSISPATGDVPNLSCLGVRMVSIGSSLYVFGGRDASRKYNGFYSFDTTKNEWKLLTPVEQGPTPRSFHSMTADENNVYVFGGVSATVRLKTLDAYNIVDHKWVQCSTPGGSCSVR... | 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 ... | 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 (... | Arabidopsis thaliana (Mouse-ear cress) |
O49339 | PTI12_ARATH | MRRWICCGDKKGDSDLSNEEVHLKSPWQNSEANQKNQKPQAVVKPEAQKEALPIEVPPLSVDEVKEKTDNFGSKSLIGEGSYGRVYYATLNDGKAVALKKLDVAPEAETNTEFLNQVSMVSRLKHENLIQLVGYCVDENLRVLAYEFATMGSLHDILHGRKGVQGAQPGPTLDWLTRVKIAVEAARGLEYLHEKVQPPVIHRDIRSSNVLLFEDYQAKVADFNLSNQAPDNAARLHSTRVLGTFGYHAPEYAMTGQLTQKSDVYSFGVVLLELLTGRKPVDHTMPRGQQSLVTWATPRLSEDKVKQCVDPKLKGEYPPKS... | 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:PRU100... | 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 | MLASVRVNQLQRLLLSARRLSSSPIIPPSRLLHQRLFSTSDTDASAASFSSSHPKIQTLEGKASNKSRSTSSTTSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHFSKDPSSAKPFEGLKFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIARLHADMDPVTSTIEYLCTTAEKLADEGRKFDAVLSLEVIEHVANPAEFCKSLSALTIPNGATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEEMSMILQRASVDVKEIAGFVYNPITGRWLLSDDISVNYIAYGTKRKDLG... | 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:CH... | 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 | MDTSLFSLFVPILVFVFIALFKKSKKPKHVKAPAPSGAWPIIGHLHLLSGKEQLLYRTLGKMADQYGPAMSLRLGSSETFVVSSFEVAKDCFTVNDKALASRPITAAAKHMGYDCAVFGFAPYSAFWREMRKIATLELLSNRRLQMLKHVRVSEISMVMQDLYSLWVKKGGSEPVMVDLKSWLEDMSLNMMVRMVAGKRYFGGGSLSPEDAEEARQCRKGVANFFHLVGIFTVSDAFPKLGWFDFQGHEKEMKQTGRELDVILERWIENHRQQRKVSGTKHNDSDFVDVMLSLAEQGKFSHLQHDAITSIKSTCLALILG... | 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:CHEB... | 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-hydr... | Arabidopsis thaliana (Mouse-ear cress) |
O49397 | ARR10_ARATH | MTMEQEIEVLDQFPVGMRVLAVDDDQTCLRILQTLLQRCQYHVTTTNQAQTALELLRENKNKFDLVISDVDMPDMDGFKLLELVGLEMDLPVIMLSAHSDPKYVMKGVKHGACDYLLKPVRIEELKNIWQHVVRKSKLKKNKSNVSNGSGNCDKANRKRKEQYEEEEEEERGNDNDDPTAQKKPRVLWTHELHNKFLAAVDHLGVERAVPKKILDLMNVDKLTRENVASHLQKFRVALKKVSDDAIQQANRAAIDSHFMQMNSQKGLGGFYHHHRGIPVGSGQFHGGTTMMRHYSSNRNLGRLNSLGAGMFQPVSSSFPR... | 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 ... | 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... | 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... | Arabidopsis thaliana (Mouse-ear cress) |
O49403 | HFA4A_ARATH | MDENNHGVSSSSLPPFLTKTYEMVDDSSSDSIVSWSQSNKSFIVWNPPEFSRDLLPRFFKHNNFSSFIRQLNTYGFRKADPEQWEFANDDFVRGQPHLMKNIHRRKPVHSHSLPNLQAQLNPLTDSERVRMNNQIERLTKEKEGLLEELHKQDEEREVFEMQVKELKERLQHMEKRQKTMVSFVSQVLEKPGLALNLSPCVPETNERKRRFPRIEFFPDEPMLEENKTCVVVREEGSTSPSSHTREHQVEQLESSIAIWENLVSDSCESMLQSRSMMTLDVDESSTFPESPPLSCIQLSVDSRLKSPPSPRIIDMNCEPD... | 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 | MAMISHRLRRALLTATSYVNRSISSSITPASDFPSVSAAVLKRSVIGRSTEVATRAPARLFSTRQYKLYKEGDEITEDTVLFEGCDYNHWLITMDFSKEETPKSPEEMVAAYEETCAQGLGISVEEAKQRMYACSTTTYQGFQAIMTEQESEKFKDLPGVVFILPDSYIDPQNKEYGGDKYENGVITHRPPPIQSGRARPRPRFDRSGGGSGGPQNFQRNTQYGQQPPMQGGGGSYGPQQGYATPGQGQGTQAPPPFQGGYNQGPRSPPPPYQAGYNQGQGSPVPPYQAGYNQVQGSPVPPYQGTQSSYGQGGSGNYSQG... | 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:... | Arabidopsis thaliana (Mouse-ear cress) |
O49432 | QRT3_ARATH | MELRKSQVAMPVFLAIMSLMVSQVVFAEKDSGSMSPHDRALAEMQALKASLVRRNLPALVSPPPTPPQAVPGPRVYQVISYGADPTGKLDSTDAILKAMEEAFDGPNHGVLMQGINDLGGARIDLQGGSYLISRPLRFPSAGAGNLLISGGTLRASNDFPVDRYLIELKDESSKLQYIFEYITLRDLLIDCNYRGGAIAVINSLRTSIDNCYITRFGDTNGILVKSGHETYIRNSFLGQHITAGGDRGERSFSGTAINLMGNDNAVTDTVIFSARIGVMVSGQANLLSGVHCYNKATGFGGTGIYLRLPGLTQNRIVNSY... | 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 | MAVPHPSSSSSRSHPFLSHVYHTSFHHHHHHNHPSLVLFWCLVFSLLSPLALSSSSSSSSSSSDSSSSSSSHISLGIGETEGTKHDLHQAILRDEAVARLHELGQVSDAATHLERTFMSPASIRAIPLIRGWMEDAGLSTWVDYMGNVHGRVEPKNGSSQALLIGSHMDTVIDAGKYDGSLGIISAISALKVLKIDGRLGELKRPVEVIAFSDEEGVRFQSTFLGSAALAGIMPVSRLEVTDKSGISVQDALKENSIDITDENLMQLKYDPASVWGYVEVHIEQGPVLEWVGYPLGVVKGIAGQTRLKVTVKGSQGHAGT... | 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, Pub... | Arabidopsis thaliana (Mouse-ear cress) |
O49447 | ADT3_ARATH | MDGSKHPSVFQKLHGQSYLINRLSPSVQARGYCVSGAYVNGGLQSLLQPTSHGVGSSLIPHGSFPVLAHAPSEKTGTGFLIDFLMGGVSAAVSKTAAAPIERVKLLIQNQDEMIKAGRLSEPYKGISDCFARTVKDEGMLALWRGNTANVIRYFPTQALNFAFKDYFKRLFNFKKEKDGYWKWFAGNLASGGAAGASSLLFVYSLDYARTRLANDAKAAKKGGQRQFNGMVDVYKKTIASDGIVGLYRGFNISCVGIVVYRGLYFGLYDSLKPVVLVDGLQDSFLASFLLGWGITIGAGLASYPIDTVRRRMMMTSGEAV... | 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-... | 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 subuni... | Arabidopsis thaliana (Mouse-ear cress) |
O49482 | CADH5_ARATH | MGIMEAERKTTGWAARDPSGILSPYTYTLRETGPEDVNIRIICCGICHTDLHQTKNDLGMSNYPMVPGHEVVGEVVEVGSDVSKFTVGDIVGVGCLVGCCGGCSPCERDLEQYCPKKIWSYNDVYINGQPTQGGFAKATVVHQKFVVKIPEGMAVEQAAPLLCAGVTVYSPLSHFGLKQPGLRGGILGLGGVGHMGVKIAKAMGHHVTVISSSNKKREEALQDLGADDYVIGSDQAKMSELADSLDYVIDTVPVHHALEPYLSLLKLDGKLILMGVINNPLQFLTPLLMLGRKVITGSFIGSMKETEEMLEFCKEKGLSS... | 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... | 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 ... | 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|Pub... | 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 link... | Arabidopsis thaliana (Mouse-ear cress) |
O49485 | SERA1_ARATH | MSATAAASSSIAVATNSLRNVTLSSRSPLPSAISVAFPSRGRNTLQRRLVLVSCSTGDGSKPTILVAEKLGDAGIKLLEDVANVDCSYNMTPEELNIKISLCDALIVRSGTKVGREVFESSHGRLKVVGRAGVGIDNVDLSAATEFGCLVVNAPTANTIAAAEHGIALMAAMARNVAQADASVKAGEWKRNKYVGVSLVGKTLAVLGFGKVGTEVARRAKGLGMRVIAHDPYAPADRAHAIGVDLVSFDEALATADFISLHMPLTPTTSKILNDETFAKMKKGVRIVNVARGGVIDEDALVRALDAGIVAQAALDVFTKE... | 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:00... | 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 | MQGPRSTGDSSTGINYADGEPICSTNSETTSNNILNPVDVQFPNNTTGSGRPTYASSSSHVVQNHNWWSFGESSSRLGPSDHLNSNGSKTDRQLLSDGYGFEEGQSGMLLPGESFLRGSSSSHMLSHVNLGKDMDIGSGLQTSGVVIRHNNCETSLGSSSQTAEERSSGPGSSLGGLGSSCKRKALEGAPSHSFPGESHGCFFQTENGAWNEGLAQYDASSSLSLSMPSQNSPNVNNQSGLPEPRFGLGGGRAVTASAFPSTRSTETISRPGRRLNPGQPPESVAFSFTQSGSSVRQQQQLPATSPFVDPLDARAIPVTG... | 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 a... | Arabidopsis thaliana (Mouse-ear cress) |
O49506 | GLO5_ARATH | MEITNVMEYEKIAKEKLPKMVYDYYASGAEDQWTLQENRNAFSRILFRPRILIDVSKIDVSTTVLGFNISMPIMIAPTAMQKMAHPDGELATARATSAAGTIMTLSSWATCSVEEVASTGPGIRFFQLYVYKDRNVVIQLVKRAEEAGFKAIALTVDTPRLGRRESDIKNRFALPRGLTLKNFEGLDLGKIDKTNDSGLASYVAGQVDQSLSWKDIKWLQSITSLPILVKGVITAEDARIAVEYGAAGIIVSNHGARQLDYVPATIVALEEVVKAVEGRIPVFLDGGVRRGTDVFKALALGASGVFVGRPSLFSLAADGE... | 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 | MKRKKKEEEEEKLIVTREFAKRWRDLSGQNHWKGMLQPLDQDLREYIIHYGEMAQAGYDTFNINTESQFAGASIYSRKDFFAKVGLEIAHPYTKYKVTKFIYATSDIHVPESFLLFPISREGWSKESNWMGYVAVTDDQGTALLGRRDIVVSWRGSVQPLEWVEDFEFGLVNAIKIFGERNDQVQIHQGWYSIYMSQDERSPFTKTNARDQVLREVGRLLEKYKDEEVSITICGHSLGAALATLSATDIVANGYNRPKSRPDKSCPVTAFVFASPRVGDSDFRKLFSGLEDIRVLRTRNLPDVIPIYPPIGYSEVGDEFP... | 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), ... | Arabidopsis thaliana (Mouse-ear cress) |
O49543 | MNIF1_ARATH | MASKVISATIRRTLTKPHGTFSRCRYLSTAAAATEVNYEDESIMMKGVRISGRPLYLDMQATTPIDPRVFDAMNASQIHEYGNPHSRTHLYGWEAENAVENARNQVAKLIEASPKEIVFVSGATEANNMAVKGVMHFYKDTKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKTDGLVDLEMLREAIRPDTGLVSIMAVNNEIGVVQPMEEIGMICKEHNVPFHTDAAQAIGKIPVDVKKWNVALMSMSAHKIYGPKGVGALYVRRRPRIRLEPLMNGGGQERGLRSGTGATQQIVGFGAACELAMKEMEYDEKWIKG... | 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 | MKLFLLLLFLLHISHTFTASRPISEFRALLSLKTSLTGAGDDKNSPLSSWKVSTSFCTWIGVTCDVSRRHVTSLDLSGLNLSGTLSPDVSHLRLLQNLSLAENLISGPIPPEISSLSGLRHLNLSNNVFNGSFPDEISSGLVNLRVLDVYNNNLTGDLPVSVTNLTQLRHLHLGGNYFAGKIPPSYGSWPVIEYLAVSGNELVGKIPPEIGNLTTLRELYIGYYNAFEDGLPPEIGNLSELVRFDGANCGLTGEIPPEIGKLQKLDTLFLQVNVFSGPLTWELGTLSSLKSMDLSNNMFTGEIPASFAELKNLTLLNLFR... | 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-[pr... | 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... | Arabidopsis thaliana (Mouse-ear cress) |
O49562 | PDRP1_ARATH | MALLSAMKLQGRPPPISSNLNPNSKPAGSDSVSLNASEPGSERKPRKFSSQLNRWNRARTLRSGAKLDSTITNGSNNTTGPMRPIESSSRTDVSTLDSDVSSSSNGVSEADMTAAKSIYIVSDGTGWTAEHAVNAALGQFDYCLVDRGCPVNTHLFSGIEDGEKLMEIIKQAAREGAMVIYTLADPSMAEATMRACKLWKIPSLDILGPITESISSHLGTNPSGLSRGITNSSLNEDYFKRIEAIEFTIKHDDGALPENLEKADIVLVGVSRTGKTPLSTYLAQKGYKVSNVPIVNGVDLPKTLFEIDPRKVFGLMINPL... | 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... | 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, phos... | 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 | MSYEKELAAAKKAVTLAARLSQEVQKTLLQSQVWKKSDRSPVTAADYGSQAVVSLVLERELQPDKLSLVAEEETGDLRKNGSEAFLEDIAKLVKDTLASEESYTSSPLSTDDVLNAIDCGKSEGGCKGSHWVLDPIDGTRGFVRGEQYAVGLALLVEGKVVLGVMACPNLPLASAVCATDNSSQEDVGCLFFATTGSGTYVQSLKGNSLPQKVQVSSNENLDEAKFLESYHKPIPIHGTIAKKLGIKALPVRIDSQAKYAALSRGDAEIYLRFTLNGYRECIWDHAPGSIITTEAGGVVCDATGKSLDFSKGKYLAHKTG... | 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|PubM... | 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 t... | 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 IS... | 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:0000... | 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 ... | 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 ac... | Arabidopsis thaliana (Mouse-ear cress) |
O49687 | MYC4_ARATH | MSPTNVQVTDYHLNQSKTDTTNLWSTDDDASVMEAFIGGGSDHSSLFPPLPPPPLPQVNEDNLQQRLQALIEGANENWTYAVFWQSSHGFAGEDNNNNNTVLLGWGDGYYKGEEEKSRKKKSNPASAAEQEHRKRVIRELNSLISGGVGGGDEAGDEEVTDTEWFFLVSMTQSFVKGTGLPGQAFSNSDTIWLSGSNALAGSSCERARQGQIYGLQTMVCVATENGVVELGSSEIIHQSSDLVDKVDTFFNFNNGGGEFGSWAFNLNPDQGENDPGLWISEPNGVDSGLVAAPVMNNGGNDSTSNSDSQPISKLCNGSSV... | 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]; ... | 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 multipl... | Arabidopsis thaliana (Mouse-ear cress) |
O49696 | ALMTC_ARATH | MSNKVHVGSLEMEEGLSKTKWMVLEPSEKIKKIPKRLWNVGKEDPRRVIHALKVGLSLTLVSLLYLMEPLFKGIGSNAIWAVMTVVVVLEFSAGATLCKGLNRGLGTLIAGSLAFFIEFVANDSGKVLRAIFIGTAVFIIGAAATYIRFIPYIKKNYDYGVVIFLLTFNLITVSSYRVDSVINIAHDRFYTIAVGCGICLFMSLLVFPIWSGEDLHKTTVGKLQGLSRSIEACVDEYFEEKEKEKTDSKDRIYEGYQAVLDSKSTDETLALYANWEPRHTLRCHRFPCQQYVKVGAVLRQFGYTVVALHGCLQTEIQTPR... | 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 | MGCFSSKHRNTESDIINGSVQSSIPTNQPENHVSRDVLKPQKPPSPQIPTTTQSNHHHQQESKPVNQQIEKKHVLTQPLKPIVFRETETILGKPFEEIRKLYTLGKELGRGQFGITYTCKENSTGNTYACKSILKRKLTRKQDIDDVKREIQIMQYLSGQENIVEIKGAYEDRQSIHLVMELCGGSELFDRIIAQGHYSEKAAAGVIRSVLNVVQICHFMGVIHRDLKPENFLLASTDENAMLKATDFGLSVFIEEGKVYRDIVGSAYYVAPEVLRRSYGKEIDIWSAGIILYILLCGVPPFWSETEKGIFNEIIKGEID... | 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-[pr... | 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 | MVRTPCCKAELGLKKGAWTPEEDQKLLSYLNRHGEGGWRTLPEKAGLKRCGKSCRLRWANYLRPDIKRGEFTEDEERSIISLHALHGNKWSAIARGLPGRTDNEIKNYWNTHIKKRLIKKGIDPVTHKGITSGTDKSENLPEKQNVNLTTSDHDLDNDKAKKNNKNFGLSSASFLNKVANRFGKRINQSVLSEIIGSGGPLASTSHTTNTTTTSVSVDSESVKSTSSSFAPTSNLLCHGTVATTPVSSNFDVDGNVNLTCSSSTFSDSSVNNPLMYCDNFVGNNNVDDEDTIGFSTFLNDEDFMMLEESCVENTAFMKEL... | 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:CH... | 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 | MGNCLDSSAKVDNSNHSPHANSASSGSKVSSKTSRSTGPSGLSTTSYSTDSSFGPLPTLRTEGEILSSPNLKAFTFNELKNATKNFRQDNLLGEGGFGCVFKGWIDQTSLTASRPGSGIVVAVKQLKPEGFQGHKEWLTEVNYLGQLSHPNLVLLVGYCAEGENRLLVYEFMPKGSLENHLFRRGAQPLTWAIRMKVAVGAAKGLTFLHEAKSQVIYRDFKAANILLDADFNAKLSDFGLAKAGPTGDNTHVSTKVIGTHGYAAPEYVATGRLTAKSDVYSFGVVLLELISGRRAMDNSNGGNEYSLVDWATPYLGDKRK... | 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: React... | 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... | Arabidopsis thaliana (Mouse-ear cress) |
O49840 | PBL3_ARATH | MGNCLDSSAKVDSSSHSPHANSASLSSRVSSKTSRSTVPSSLSINSYSSVESLPTPRTEGEILSSPNLKAFTFNELKNATRNFRPDSLLGEGGFGYVFKGWIDGTTLTASKPGSGIVVAVKKLKTEGYQGHKEWLTEVNYLGQLSHPNLVKLVGYCVEGENRLLVYEFMPKGSLENHLFRRGAQPLTWAIRMKVAIGAAKGLTFLHDAKSQVIYRDFKAANILLDAEFNSKLSDFGLAKAGPTGDKTHVSTQVMGTHGYAAPEYVATGRLTAKSDVYSFGVVLLELLSGRRAVDKSKVGMEQSLVDWATPYLGDKRKLFR... | 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: React... | null | null | null | null | FUNCTION: May be involved in plant defense signaling. {ECO:0000250|UniProtKB:O48814}. | Arabidopsis thaliana (Mouse-ear cress) |
O50008 | METE1_ARATH | MASHIVGYPRMGPKRELKFALESFWDGKSTAEDLQKVSADLRSSIWKQMSAAGTKFIPSNTFAHYDQVLDTTAMLGAVPPRYGYTGGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYLLLSKAAKGVDKSFELLSLLPKILPIYKEVITELKAAGATWIQLDEPVLVMDLEGQKLQAFTGAYAELESTLSGLNVLVETYFADIPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLVKAGFPEGKYLFAGVVDGRNIWANDFAASLSTLQALEGIVGKD... | 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 | MLKVESNWAQACDTCRSAACTVYCRADSAYLCSSCDAQVHAANRLASRHERVRVCQSCERAPAAFFCKADAASLCTTCDSEIHSANPLARRHQRVPILPISEYSYSSTATNHSCETTVTDPENRLVLGQEEEDEDEAEAASWLLPNSGKNSGNNNGFSIGDEFLNLVDYSSSDKQFTDQSNQYQLDCNVPQRSYGEDGVVPLQIEVSKGMYQEQQNFQLSINCGSWGALRSSNGSLSHMVNVSSMDLGVVPESTTSDATVSNPRSPKAVTDQPPYPPAQMLSPRDREARVLRYREKKKMRKFEKTIRYASRKAYAEKRPR... | 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 | MAHKKTYSQLRSELLARYPVGLTKGGVSIDDIVQLRLQSPYESHLDVARAMASVMRADMAAYDRDTGKFTQSLGCWSGFHAQQMIKAVKRLRGTTKGAYVYLSGWMVAGLRNRWGHLPDQSMHEKTSVVDLIEEIYVSLRQADEVALNDLFNELKDARAKGATNKACEEIISRIDGFESHVVPIIADIDAGFGNEHATYLLAKEMIKAGACCLQIENQVSDAKQCGHQDGKVTVPREDFIEKLRACRLAFEELGVDDGVIVARTDSLGASLTQKIPVSQQAGDFASSYIKWLKTEPITDANPLSEGELAIWQSGNFARPI... | 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 substr... | 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 | MELKPNVKEIPGPKARKVIEEHHKYMATTTNDPNEYFLVIERAEGVYWIDVDGNVLLDFSSGIGVMNVGLRNPKVIEAIKKQLDLVLHAAGTDYYNPYQVELAKKLVEIAPGDIERKVFLSNSGTEANEAALKIAKWSTNRKMFIAFIGAFHGRTHGTMSLTASKPVQRSRMFPTMPGVVHVPYPNPYRNPWGIDGYENPDELINRVIDYIEEYLFEHYVPAEEVAGIFFEPIQGEGGYVVPPKNFFKELKKLADKHGILLIDDEVQMGMGRTGRMWAIEHFDIVPDIVTVAKALGGGIPIGATIFRADLDFGVSGVHSN... | 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-amin... | 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) ... | 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 (PubMe... | Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
O50146 | LYSY_THET2 | MDKKTLSIVGASGYAGGEFLRLALSHPYLEVKQVTSRRFAGEPVHFVHPNLRGRTNLKFIPPEKLEPADILVLALPHGVFAREFDRYSALAPILIDLSADFRLKDPELYRRYYGEHPRPDLLGCFVYAVPELYREALKGADWIAGAGCNATATLLGLYPLLKAGVLKPTPIFVTLLISTSAAGAEASPASHHPERAGSIRVYKPTGHRHTAEVVENLPGRPEVHLTAIATDRVRGILMTAQCFVQDGWSERDVWQAYREAYAGEPFIRLVKQKKGVHRYPDPRFVQGTNYADIGFELEEDTGRLVVMTAIDNLVKGTAGH... | 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:... | 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:784... | 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 | MSSTENPDSVAAAEELHALRVEAQVLRRQLAQSPEQVRELESKVDSLSIRNSKLMDTLKEARQQLIALREEVDRLGQPPSGYGVLLSVHEDKTVDVFTSGRKMRLTCSPNIDTDTLALGQTVRLNEALTIVEAGTYEQVGEISTLREVLDDGLRALVVGHADEERIVWLAAPLAAVFADPEADIIAYDADSPTRKLRPGDSLLVDTKAGYAFERIPKAEVEDLVLEEVPDVHYDDIGGLGRQIEQIRDAVELPFLHKDLFHEYSLRPPKGVLLYGPPGCGKTLIAKAVANSLAKKIAEARGQDSKDAKSYFLNIKGPELL... | 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 o... | Rhodococcus erythropolis (Arthrobacter picolinophilus) |
O50274 | CYSNC_PSEAE | MSHQSDLISEDILAYLGQHERKELLRFLTCGNVDDGKSTLIGRLLHDSKMIYEDHLEAITRDSKKVGTTGDDVDLALLVDGLQAEREQGITIDVAYRYFSTAKRKFIIADTPGHEQYTRNMATGASTCDLAIILIDARYGVQTQTRRHSFIASLLGIRHIVVAINKMDLKDFDQGVFEQIKADYLAFAEKIGLKTSSLHFVPMSALKGDNVVNKSERSPWYAGQSLMEILETVEIAADRNLDDMRFPVQYVNRPNLNFRGFAGTLASGVVRKGDEVVALPSGKGSKVKSIVTFEGELEQAGPGQAVTLTLEDEIDVSRGD... | 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 + AD... | 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... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
O50406 | DITCY_MYCTU | METFRTLLAKAALGNGISSTAYDTAWVAKLGQLDDELSDLALNWLCERQLPDGSWGAEFPFCYEDRLLSTLAAMISLTSNKHRRRRAAQVEKGLLALKNLTSGAFEGPQLDIKDATVGFELIAPTLMAEAARLGLAICHEESILGELVGVREQKLRKLGGSKINKHITAAFSVELAGQDGVGMLDVDNLQETNGSVKYSPSASAYFALHVKPGDKRALAYISSIIQAGDGGAPAFYQAEIFEIVWSLWNLSRTDIDLSDPEIVRTYLPYLDHVEQHWVRGRGVGWTGNSTLEDCDTTSVAYDVLSKFGRSPDIGAVLQFE... | 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... | 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:25... | Pseudomonas cichorii |
O50657 | DCLO_SELRU | MKNFRLSEKEVKTLAKRIPTPFLVASLDKVEENYQFMRRHLPRAGVFYAMKANPTPEILSLLAGLGSHFDVASAGEMEILHELGVDGSQMIYANPVKDARGLKAAADYNVRRFTFDDPSEIDKMAKAVPGADVLVRIAVRNNKALVDLNTKFGAPVEEALDLLKAAQDAGLHAMGICFHVGSQSLSTAAYEEALLVARRLFDEAEEMGMHLTDLDIGGGFPVPDAKGLNVDLAAMMEAINKQIDRLFPDTAVWTEPGRYMCGTAVNLVTSVIGTKTRGEQPWYILDEGIYGCFSGIMYDHWTYPLHCFGKGNKKPSTFGG... | 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:4691... | 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 | MGFHIYEIKARQIIDSRGNPTVEADVILEDGTYGRAAVPSGASTGINEAVELRDGDKSVYMGKGVLKAIENIKNIIAPELEGMSALNQVAIDRKMLELDGTPTKEKLGANAILAVSMATAKAAAKYLGLRPYQYLGAYKANILPTPMCNIINGGAHSDNSVDFQEFMIMPIGAKTFSEAIRMAAEVFHTLKGILSGKGYATSVGDEGGFAPNLKSNEEACEVIIEAIKKAGYEPGKDIAIALDPATSELYDPKTKKYVLKWSTKEKLTSEQMVEYWAKWVEKYPIISIEDGMAEEDWDGWKKLTDKIGNKIQLVGDDLFV... | 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 | MAVNSKYHHSCINCGGLNTDERNERGLPCEVCLPEDSPSDIYRALLERKTLKEYRFYHEFWNEYEDFRSFFKKKFGKDLTGYQRLWAKRIVQGKSFTMVAPTGVGKTTFGMMTALWLARKGKKSALVFPTVTLVKQTLERLQKLADEKVKIFGFYSSMKKEEKEKFEKSFEEDDYHILVFSTQFVSKNREKLSQKRFDFVFVDDVDAVLKASRNIDTLLMMVGIPEEIIRKAFSTIKQGKIYERPKNLKPGILVVSSATAKPRGIRPLLFRDLLNFTVGRLVSVARNITHVRISSRSKEKLVELLEIFRDGILIFAQTEE... | 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 p... | 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|Pu... | 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 necessi... | 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 f... | Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
O52063 | ATZC_PSESD | MSKDFDLIIRNAYLSEKDSVYDIGIVGDRIIKIEAKIEGTVKDEIDAKGNLVSPGFVDAHTHMDKSFTSTGERLPKFWSRPYTRDAAIEDGLKYYKNATHEEIKRHVIEHAHMQVLHGTLYTRTHVDVDSVAKTKAVEAVLEAKEELKDLIDIQVVAFAQSGFFVDLESESLIRKSLDMGCDLVGGVDPATRENNVEGSLDLCFKLAKEYDVDIDYHIHDIGTVGVYSINRLAQKTIENGYKGRVTTSHAWCFADAPSEWLDEAIPLYKDSGMKFVTCFSSTPPTMPVIKLLEAGINLGCASDNIRDFWVPFGNGDMVQG... | 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 f... | 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 | MELVVEPLNLHLNAETGSTLLDVLRSNEVPISYSCMSGRCGTCRCRVIAGHLRDNGPETGRPQAGKGTYVLACQAVLTEDCTIEIPESDEIVVHPARIVKGTVTAIDEATHDIRRLRIKLAKPLEFSPGQYATVQFTPECVRPYSMAGLPSDAEMEFQIRAVPGGHVSNYVFNELSVGASVRISGPLGTAYLRRTHTGPMLCVGGGTGLAPVLSIVRGALESGMSNPIHLYFGVRSEQDIYDEERLHALAARFPNLKVNVVVATGPAGPGRRSGLVTDLIGRDLPNLAGWRAYLCGAPAMVEALNLLVARLGIVPGHIHA... | 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|PubM... | 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 ... | Ralstonia sp |
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