Entry stringlengths 6 10 | Sequence stringlengths 6 35.2k | Organism stringlengths 9 169 | Function [CC] stringlengths 24 15.3k ⌀ | EC number stringlengths 7 118 ⌀ | Catalytic activity stringlengths 65 35.7k ⌀ | Cofactor stringlengths 43 1.77k ⌀ | Kinetics stringlengths 70 10.8k ⌀ | Pathway stringlengths 27 1.13k ⌀ | pH dependence stringlengths 64 855 ⌀ | Temperature dependence stringlengths 70 709 ⌀ | Keywords stringlengths 3 1.61k ⌀ | Gene Ontology (biological process) stringlengths 19 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.47k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.21k ⌀ | Subcellular location [CC] stringlengths 30 5.42k ⌀ | Post-translational modification stringlengths 16 6.52k ⌀ | Domain [CC] stringlengths 33 6.72k ⌀ | InterPro stringlengths 10 810 ⌀ | Gene3D stringlengths 10 250 ⌀ |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A0A009IHW8 | MSLEQKKGADIISKILQIQNSIGKTTSPSTLKTKLSEISRKEQENARIQSKLSDLQKKKIDIDNKLLKEKQNLIKEEILERKKLEVLTKKQQKDEIEHQKKLKREIDAIKASTQYITDVSISSYNNTIPETEPEYDLFISHASEDKEDFVRPLAETLQQLGVNVWYDEFTLKVGDSLRQKIDSGLRNSKYGTVVLSTDFIKKDWTNYELDGLVAREMNGHKMILPIWHKITKNDVLDYSPNLADKVALNTSVNSIEEIAHQLADVILNR | Acinetobacter baumannii (strain 1295743) | FUNCTION: NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide (PubMed:29395922). In addition to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR), termed 2'cADPR (v-cADPR) (PubMed:29395922, PubMed:36048923). Cleaves NADP(+), but does not cyclize the prod... | 3.2.2.-; 3.2.2.6 | CATALYTIC ACTIVITY: Reaction=NAD(+) = 2'cADPR + H(+) + nicotinamide; Xref=Rhea:RHEA:75299, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:194248; Evidence={ECO:0000269|PubMed:36048923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75300; Evidence={ECO:0000269|PubMed:36048923}; CATALYTIC AC... | null | null | null | null | null | 3D-structure;Coiled coil;Hydrolase;NAD | NAD catabolic process [GO:0019677]; signal transduction [GO:0007165] | null | NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NADP+ nucleosidase activity [GO:0050135] | null | null | DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity (Probable). The TIR domain alone is active and produces cADPR (residues 134-267) (PubMed:36048923). {ECO:0000255|PROSITE-ProRule:PRU00204, ECO:0000269|PubMed:36048923, ECO:0000305|PubMed:3... | IPR000157;IPR035897; | 3.40.50.10140; |
A0A023I7E1 | MRFQVIVAAATITMITSYIPGVASQSTSDGDDLFVPVSNFDPKSIFPEIKHPFEPMYANTENGKIVPTNSWISNLFYPSADNLAPTTPDPYTLRLLDGYGGNPGLTIRQPSAKVLGSYPPTNDVPYTDAGYMINSVVVDLRLTSSEWSDVVPDRQVTDWDHLSANLRLSTPQDSNSYIDFPIVRGMAYITANYNNLTPQFLSQHAIISVEADEKKSDDNTSTFSGRKFKITMNDDPTSTFIIYSLGDKPLELRKQDNSNLVASKPYTGVIRVAKLPAPEFETLLDASRAVWPTGGDISARSDDNNGASYTIKWKTNSNEA... | Rhizomucor miehei | FUNCTION: Cleaves internal linkages in 1,3-beta-glucan. {ECO:0000269|PubMed:34801773}. | 3.2.1.39 | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000269|PubMed:34801773}; | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:34801773}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:34801773}; | 3D-structure;Carbohydrate metabolism;Cell wall;Cell wall biogenesis/degradation;Glycoprotein;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal | cell wall organization [GO:0071555]; polysaccharide catabolic process [GO:0000272] | cell surface [GO:0009986]; extracellular region [GO:0005576] | glucan endo-1,3-beta-D-glucosidase activity [GO:0042973]; glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group [GO:0052861]; glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group [GO:0052862] | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250|UniProtKB:P53753}. | null | null | IPR005200;IPR040720;IPR040451; | 1.10.287.1170;1.20.5.420; |
A0A024B7W1 | MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGC... | Zika virus (isolate ZIKV/Human/French Polynesia/10087PF/2013) (ZIKV) | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of the mature virus particle (By similarity). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface ... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | CATALYTIC ACTIVITY: [RNA-directed RNA polymerase NS5]: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:C... | null | null | null | null | null | 3D-structure;4Fe-4S;Acetylation;Activation of host autophagy by virus;ATP-binding;Capsid protein;Clathrin-mediated endocytosis of virus by host;Cleavage on pair of basic residues;Disulfide bond;Fusion of virus membrane with host endosomal membrane;Fusion of virus membrane with host membrane;Glycoprotein;GTP-binding;Hel... | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; negative regulation of innate immune response [GO:0045824]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT ca... | centrosome [GO:0005813]; extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | 4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090]; mRNA (nucleoside-2'-O-)-methyltransferas... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000269|PubMed:36594413}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}... | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | DOMAIN: [Small envelope protein M]: The transmembrane domain contains an endoplasmic reticulum retention signal. {ECO:0000250|UniProtKB:P17763}.; DOMAIN: [Envelope protein E]: The transmembrane domain contains an endoplasmic reticulum retention signal. {ECO:0000250|UniProtKB:P17763}.; DOMAIN: [Capsid protein C]: The di... | IPR043502;IPR000069;IPR038302;IPR013755;IPR001122;IPR037172;IPR011492;IPR027287;IPR026470;IPR038345;IPR011998;IPR001157;IPR000752;IPR000487;IPR001850;IPR000404;IPR001528;IPR046811;IPR002535;IPR038688;IPR047530;IPR000208;IPR000336;IPR014412;IPR036253;IPR038055;IPR013756;IPR014001;IPR001650;IPR014756;IPR026490;IPR049486;... | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10; |
A0A024R6A3 | MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAEST... | Homo sapiens (Human) | FUNCTION: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors. {ECO:0000256|RuleBase:RU361148}. | 3.4.23.- | null | null | null | null | null | null | Apoptosis;Cell adhesion;Cell membrane;Cell projection;Endoplasmic reticulum;Golgi apparatus;Hydrolase;Membrane;Notch signaling pathway;Phosphoprotein;Protease;Synapse;Transmembrane;Transmembrane helix | amyloid-beta formation [GO:0034205]; apoptotic signaling pathway [GO:0097190]; autophagosome assembly [GO:0000045]; blood vessel development [GO:0001568]; brain morphogenesis [GO:0048854]; Cajal-Retzius cell differentiation [GO:0021870]; cell adhesion [GO:0007155]; cell fate specification [GO:0001708]; cerebellum devel... | cell cortex [GO:0005938]; cell junction [GO:0030054]; cell surface [GO:0009986]; ciliary rootlet [GO:0035253]; dendritic shaft [GO:0043198]; early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; gamma-secretase complex [GO:0070765]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:00... | aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296] | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection, neuron projection {ECO:0000256|ARBA:ARBA00004487}. Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004520}. Endo... | null | DOMAIN: The PAL motif is required for normal active site conformation. {ECO:0000256|RuleBase:RU361148}. | IPR002031;IPR001108;IPR006639;IPR042524; | 1.10.472.100; |
A0A024SC78 | MRSLAILTTLLAGHAFAYPKPAPQSVNRRDWPSINEFLSELAKVMPIGDTITAACDLISDGEDAAASLFGISETENDPCGDVTVLFARGTCDPGNVGVLVGPWFFDSLQTALGSRTLGVKGVPYPASVQDFLSGSVQNGINMANQIKSVLQSCPNTKLVLGGYSQGSMVVHNAASNLDAATMSKISAVVLFGDPYYGKPVANFDAAKTLVVCHDGDNICQGGDIILLPHLTYAEDADTAAAFVVPLVS | Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei) | FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:25219509). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (PubMed:25219509). {ECO:0000269|PubMed:25219509}. | 3.1.1.74 | CATALYTIC ACTIVITY: Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; Evidence={ECO:0000269|PubMed:25219509}; | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-7. {ECO:0000269|PubMed:25219509}; | null | 3D-structure;Disulfide bond;Hydrolase;Secreted;Serine esterase;Signal | null | extracellular region [GO:0005576] | cutinase activity [GO:0050525] | SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU361263}. | PTM: The 2 disulfide bonds play a critical role in holding the catalytic residues in juxta-position; reduction of the disulfide bridges results in the complete inactivation of the enzyme. {ECO:0000250|UniProtKB:P11373}. | DOMAIN: In contract to classical cutinases, possesses a lid formed by two N-terminal helices which covers its active site (PubMed:25219509). The lid opens in the presence of surfactants to uncover the catalytic crevice, allowing enzyme activity and inhibition (PubMed:25219509). {ECO:0000269|PubMed:25219509}. | IPR029058;IPR000675;IPR043580;IPR043579;IPR011150; | 3.40.50.1820; |
A0A044RE18 | MYWQLVRILVLFDCLQKILAIEHDSICIADVDDACPEPSHTVMRLRERNDKKAHLIAKQHGLEIRGQPFLDGKSYFVTHISKQRSRRRKREIISRLQEHPDILSIEEQRPRVRRKRDFLYPDIAHELAGSSTNIRHTGLISNTEPRIDFIQHDAPVLPFPDPLYKEQWYLNNGAQGGFDMNVQAAWLLGYAGRNISVSILDDGIQRDHPDLAANYDPLASTDINGHDDDPTPQDDGDNKHGTRCAGEVASIAGNVYCGVGVAFHAKIGGVRMLDGPVSDSVEAASLSLNRHHIDIYSASWGPEDDGRTFDGPGPLAREAF... | Onchocerca volvulus | FUNCTION: Serine endoprotease which cleaves substrates at the RX(K/R)R consensus motif. {ECO:0000269|PubMed:12855702}. | 3.4.21.75 | CATALYTIC ACTIVITY: Reaction=Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.; EC=3.4.21.75; Evidence={ECO:0000269|P... | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12855702}; Note=Binds 3 calcium ions per subunit. {ECO:0000250|UniProtKB:P09958}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Active from pH 7.0 to 8.5. {ECO:0000269|PubMed:12855702}; | null | Autocatalytic cleavage;Calcium;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen | dibasic protein processing [GO:0090472]; zymogen activation [GO:0031638] | extracellular region [GO:0005576]; membrane [GO:0016020]; trans-Golgi network [GO:0005802] | metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252] | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12855702}. | PTM: N-glycosylated. {ECO:0000269|PubMed:12855702}.; PTM: The inhibition peptide, which plays the role of an intramolecular chaperone, is probably autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound as a potent autoinhibitor. Probably following transport to the trans Golgi, a se... | null | IPR008979;IPR034182;IPR002884;IPR000209;IPR036852;IPR023827;IPR022398;IPR023828;IPR015500;IPR032815;IPR038466; | 2.60.120.260;3.30.70.850;3.40.50.200; |
A0A059AF78 | MESCNCVEPQWPADELLMKYQYLSDFFIALAYFSIPLELIYFVKKSAVFPYRWVLVQFGAFIVLCGATHLINLWTFAIHSRTVAYVMTIAKVLTAAVSCITALMLVHIIPDLLSVKTRELFLKNKAAELDREMGLIRTQEETGRHCALWMPTRSGLELQLSYTLRQQQNPVGYTVPIHLPVINRVFSSNRALKISPNSPVARIRPLAGKYIPGEVVAVRVPLLHLSNFQINDWPELSTKRYALMVLMLPSDSARQWHVHELELVEVVADQVAVALSHAAILEESMRARDLLMEQNVALDLARREAETAIRARNDFLAVMN... | Eucalyptus grandis (Flooded gum) | null | 2.7.13.3 | null | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000256|PIRSR:PIRSR026389-2}; Note=Binds 1 copper ion per dimer. {ECO:0000256|PIRSR:PIRSR026389-2}; | null | null | null | null | ATP-binding;Copper;Disulfide bond;Endoplasmic reticulum;Ethylene signaling pathway;Kinase;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Receptor;Transferase;Transmembrane;Transmembrane helix | 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 [GO:0005783]; 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] | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. | null | null | IPR011006;IPR014525;IPR003018;IPR029016;IPR003594;IPR036890;IPR005467;IPR003661;IPR036097;IPR004358;IPR001789; | 1.10.287.130;3.30.450.40;3.40.50.2300;3.30.565.10; |
A0A059TC02 | MRSVSGQVVCVTGAGGFIASWLVKILLEKGYTVRGTVRNPDDPKNGHLRELEGAKERLTLCKADLLDYQSLREAINGCDGVFHTASPVTDDPEQMVEPAVIGTKNVINAAAEANVRRVVFTSSIGAVYMDPNRDPETVVDETCWSDPDFCKNTKNWYCYGKMVAEQAAWEEAKEKGVDLVVINPVLVQGPLLQTTVNASVLHILKYLTGSAKTYANSVQAYVDVKDVALAHILLYETPEASGRYLCAESVLHRGDVVEILSKFFPEYPIPTKCSDVTKPRVKPYKFSNQKLKDLGLEFTPVKQCLYETVKSLQEKGHLPI... | Petunia hybrida (Petunia) | FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:24985707). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:24985707, PubMed:25217505). Mediates the conversion of feruloyl CoA to coniferylaldehyde (PubMed... | 1.2.1.44 | CATALYTIC ACTIVITY: Reaction=(E)-coniferaldehyde + CoA + NADP(+) = (E)-feruloyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64648, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87305; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; Ph... | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=208.6 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:25217505}; KM=307.6 uM for feruloyl-CoA {ECO:0000269|PubMed:25217505}; KM=270.3 uM for sinapoyl-CoA {ECO:0000269|PubMed:25217505}; Vmax=1235.7 nmol/sec/mg enzyme with p-coumaroyl-CoA as substrate {ECO:0000269|PubMed:... | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:25217505}; | null | 3D-structure;Cytoplasm;Disulfide bond;Lignin biosynthesis;NADP;Nucleotide-binding;Oxidoreductase;Phenylpropanoid metabolism | circadian rhythm [GO:0007623]; green leaf volatile biosynthetic process [GO:0010597]; lignin biosynthetic process [GO:0009809]; phenylpropanoid biosynthetic process [GO:0009699] | cytoplasm [GO:0005737] | cinnamoyl-CoA reductase activity [GO:0016621]; nucleotide binding [GO:0000166]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24985707}. | PTM: The formation of a reversible disulfide bond reduces activity by perturbing the positioning of nearby catalytic residues. {ECO:0000269|PubMed:25217505}. | null | IPR001509;IPR036291; | 3.40.50.720; |
A0A060WBM3 | MEAFNHKLNTYIDSWMGPRDERVQGWLLLDNYPPTFALTLMYLLIVWLGPKYMRHRQPVSCQGLLVLYNLALTLLSFYMFYEMVSAVWQGGYNFYCQDTHSAGETDTKIINVLWWYYFSKVIEFMDTFFFILRKNNHQITFLHIYHHASMLNIWWFVMNWVPCGHSYFGASLNSFIHVLMYSYYGLSAVPAIRPYLWWKRYITQGQLIQFFLTMSQTICAVIWPCGFPRGWLFFQIFYMASLIALFSNFYIQTYKKHRVSQKKAYHQNGSVDSLNGHANGVTPTETITHRKVRAD | Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) | FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that... | 2.3.1.199 | CATALYTIC ACTIVITY: Reaction=(11Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(13Z)-eicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39679, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:75121, ChEBI:CHEBI:76559; Evidence={ECO:0000256|ARBA:ARBA00001296}; PhysiologicalDirection=left... | null | null | PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03205}. | null | null | Cell projection;Endoplasmic reticulum;Fatty acid biosynthesis;Fatty acid metabolism;Lipid biosynthesis;Lipid metabolism;Membrane;Reference proteome;Transferase;Transmembrane;Transmembrane helix | fatty acid elongation [GO:0030497]; fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; sphingolipid biosynthetic process [GO... | dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789] | fatty acid elongase activity [GO:0009922] | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03205}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03205}. Cell projection, dendrite {ECO:0000256|HAMAP-Rule:MF_03205}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=... | null | null | IPR002076;IPR033677; | null |
A0A060XQE7 | MEEIVVAGISGRLPESNNLEEFWENLFNGVDMVTEDDRRWKPGLYGLPKRNGKLKDISRFDAAFFGVHPKQAHTMDPQLRLMLEIAYEAIVDGGLNPTELRGSRTGVYIGVSGSEAGEAFSRDPEELLGYSMTGCQRAMFANRLSYFFDFNGPSTAIDTACSSSLLALENAFNAIRHGHCDAALVGGVNLLLKPNTSVQFMKLGMLSPEGTCKSFDSSGNGYCRSEAAVAVLLTRRSMAKRVYATVLNAGNNTDGYKEQGVTFPSGEMQQRLVRSLYQEVNITPDQVEYIEAHGTGTKVGDPQEVNGIVSVFCHSKRDPL... | Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) | FUNCTION: Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-ph... | 1.1.1.100; 1.3.1.39; 2.3.1.38; 2.3.1.39; 2.3.1.41; 2.3.1.85; 3.1.2.14; 4.2.1.59 | CATALYTIC ACTIVITY: Reaction=(2E)-butenoyl-[ACP] + H(+) + NADPH = butanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41812, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78453, ChEBI:CHEBI:78454; Evidence={ECO:0000256|ARBA:ARBA00023357}; PhysiologicalDirection=left... | null | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|ARBA:ARBA00005194}. | null | null | Acetylation;Fatty acid biosynthesis;Fatty acid metabolism;Hydrolase;Lipid biosynthesis;Lipid metabolism;Lyase;NAD;Phosphopantetheine;Phosphoprotein;Pyridoxal phosphate;Reference proteome;S-nitrosylation;Transferase | cellular response to insulin stimulus [GO:0032869]; fatty acid biosynthetic process [GO:0006633] | cytoplasm [GO:0005737] | (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity [GO:0019171]; 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity [GO:0004316]; 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; [acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; [acyl-carrier-protein] S-malonyltransfer... | null | null | null | IPR029058;IPR001227;IPR036736;IPR014043;IPR016035;IPR049391;IPR011032;IPR018201;IPR014031;IPR014030;IPR016036;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049552;IPR020843;IPR013968;IPR049900;IPR020806;IPR009081;IPR006162;IPR029063;IPR001031;IPR016039; | 3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.50.1820;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;3.40.50.150; |
A0A061AE05 | MLTPRDENNEGDAMPMLKKPRYSSLSGQSTNITYQEHTISREERAAAVGRHEGFRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESENVKFIEVHVSTTLEVCEQRDPKPSELYKKARAGQILGFTGIDSAYEPPENAEIILDAGKDGVQQCVQKVLDHLESKGLLPEQIPDVPAVRELFVSDDLTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDLKHKVAFVGEKSD... | Caenorhabditis elegans | FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway (PubMed:16497669). The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group fro... | 2.7.1.25; 2.7.7.4 | 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; Evidence={ECO:0000269|PubMed:16497669}; CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate... | null | null | PATHWAY: Sulfur metabolism; sulfate assimilation. {ECO:0000303|PubMed:16497669}. | null | null | Alternative splicing;ATP-binding;Developmental protein;Kinase;Multifunctional enzyme;Nucleotide-binding;Nucleotidyltransferase;Nucleus;Reference proteome;Transferase | 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process [GO:0050428]; phosphorylation [GO:0016310]; sulfate assimilation [GO:0000103] | nucleus [GO:0005634] | adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]; sulfate adenylyltransferase (ATP) activity [GO:0004781] | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16497669}. | null | null | IPR002891;IPR025980;IPR027417;IPR015947;IPR014729;IPR024951;IPR002650; | 3.40.50.620;3.40.50.300;3.10.400.10; |
A0A061I403 | MPMASVIAVAEPKWISVWGRFLWLTLLSMALGSLLALLLPLGAVEEQCLAVLRSFHLLRSKLDRTQHVVTKCTSPSTELSVTSGDVGLLTVKTKTSPAGKLEAKAALNQALEMKRQGKREKAHKLFLHALKMDPGFVDALNEFGIFSEEEKDIIQADYLYTRALTISPFHEKALVNRDRTLPLVEEIDQRYFSIIDSKVKKVMSIPKGSSALRRVMEETYYHHIYHTVAIEGNTLTLSEIRHILETRYAVPGKSLEEQNEVIGMHAAMKYINTTLVSRIGSVTIDDMLEIHRRVLGYVDPVEAGRFRRTQVLVGHHIPPH... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) | FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (PubMed:27918543). The side chain of Glu-231 determines which of the two ... | 2.7.7.108; 3.1.4.- | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIV... | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; Note=Divalent metal cation. Prefers Mn(2+) over Mg(2+). {ECO:0000250|UniProtKB:Q9BVA6}; | null | null | null | null | ATP-binding;Endoplasmic reticulum;Glycoprotein;Hydrolase;Magnesium;Manganese;Membrane;Nucleotide-binding;Nucleotidyltransferase;Phosphoprotein;Reference proteome;Repeat;Signal-anchor;TPR repeat;Transferase;Transmembrane;Transmembrane helix;Unfolded protein response | protein adenylylation [GO:0018117]; protein deadenylylation [GO:0044602]; regulation of IRE1-mediated unfolded protein response [GO:1903894]; response to endoplasmic reticulum stress [GO:0034976]; response to unfolded protein [GO:0006986] | endoplasmic reticulum membrane [GO:0005789] | AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087] | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVA6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9BVA6}. | PTM: Auto-AMPylated in vitro. {ECO:0000250|UniProtKB:Q9BVA6}. | DOMAIN: The fido domain mediates the adenylyltransferase activity. {ECO:0000250|UniProtKB:Q9BVA6}. | IPR003812;IPR036597;IPR040198;IPR011990; | 1.10.3290.10;1.25.40.10; |
A0A061IKA1 | MESKALLLVALGVWLQSLTASQGGVAAADGGRDFTDIESKFALRTPDDTAEDNCHLIPGIAESVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNVGYEINKV... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) | 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. Mediates margination of triglyceride-rich lipopr... | 3.1.1.34 | CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000256|ARBA:ARBA00000652}; PhysiologicalDirection=left-t... | null | null | null | null | null | Calcium;Cell membrane;Chylomicron;Disulfide bond;Extracellular matrix;Glycoprotein;Heparin-binding;Hydrolase;Lipid degradation;Lipid metabolism;Lipoprotein;Membrane;Metal-binding;Nitration;Secreted;Signal;VLDL | fatty acid biosynthetic process [GO:0006633]; response to glucose [GO:0009749]; triglyceride catabolic process [GO:0019433]; very-low-density lipoprotein particle remodeling [GO:0034372] | chylomicron [GO:0042627]; plasma membrane [GO:0005886]; very-low-density lipoprotein particle [GO:0034361] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; apolipoprotein binding [GO:0034185]; heparin binding [GO:0008201]; lipoprotein lipase activity [GO:0004465]; metal ion binding [GO:0046872]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970] | SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362020}; Peripheral membrane protein {ECO:0000256|RuleBase:RU362020}; Extracellular side {ECO:0000256|RuleBase:RU362020}. Secreted {ECO:0000256|RuleBase:RU362020}. Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|... | PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity. {ECO:0000256|RuleBase:RU362020}. | null | IPR029058;IPR013818;IPR016272;IPR033906;IPR002330;IPR001024;IPR036392;IPR000734; | 3.40.50.1820;2.60.60.20; |
A0A067XGX8 | MALTATATTRGGSALPNSCLQTPKFQSLQKPTFISSFPTNKKTKPRTKHISAVQSPPSTTKWNLESWKTKPAFQLPDYPDKVELESVLKTLSTYPPIVFAGEARNLEEKLGEAALGNAFLLQGGDCAESFKEFSANNIRDTFRVMLQMGVVLMFGGQMPVIKVGRMAGQFAKPRSDPFEEKDGVKLPSYRGDNVNGDAFDEKSRIPDPHRMVRAYTQSVATLNLLRAFASGGYAAMQRVNQWNLDFTDQSEQGDRYRELAHRVDEAMGFMTAAGLTVDHTIMTTTDFWTSHECLLLPYEQALTREDSTSGLYYDCSAHMI... | Petunia hybrida (Petunia) | FUNCTION: Involved in the production of volatile organic compounds (VOCs) (PubMed:24815009). Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate (By similarity). {ECO:000... | 2.5.1.54 | CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; Evidence={ECO:0000250|UniProtKB:O53512}; | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O53512}; Note=Binds 1 divalent metal cation per subunit that could be manganese. {ECO:0000250|UniProtKB:O53512}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000250|UniProtKB:O53512}. | null | null | Amino-acid biosynthesis;Aromatic amino acid biosynthesis;Chloroplast;Manganese;Metal-binding;Plastid;Transferase;Transit peptide | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423] | chloroplast [GO:0009507] | 3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849]; metal ion binding [GO:0046872] | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24815009}. | null | null | IPR013785;IPR002480; | 3.20.20.70; |
A0A067XH53 | MALSTNSTTSSLLPKTPLVQQPLLKNASLPTTTKAIRFIQPISAIHSSDSSKNTPIVSAKPSSPPAATSTAAATAVTKQEWSIDSWKTKKALQLPEYPNQEELKNVLKTIEDFPPIVFAGEARHLEEKLGEAAMGRAFLLQGGDCAESFKEFNANNIRDTFRILLQMGAVLMFGGQMPVIKVGRMAGQFAKPRSDNFEEKNGVKLPSYRGDNVNGDAFDLKSRTPDPQRLIRAYCQSAATLNLLRAFATGGYAAMQRVTQWNLDFTEHSEQGDRYRELANRVDEALGFMNAAGLTTDHPIMTTTEFWTSHECLLLPYEQS... | Petunia hybrida (Petunia) | FUNCTION: Involved in the production of volatile organic compounds (VOCs), including floral volatile benzenoids and phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26), scent attracting pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta) (PubMed:24815009). Catalyz... | 2.5.1.54 | CATALYTIC ACTIVITY: Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate; Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54; Evidence={ECO:0000250|UniProtKB:O53512}; | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O53512}; Note=Binds 1 divalent metal cation per subunit that could be manganese. {ECO:0000250|UniProtKB:O53512}; | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000250|UniProtKB:O53512}. | null | null | Amino-acid biosynthesis;Aromatic amino acid biosynthesis;Chloroplast;Manganese;Metal-binding;Plastid;Transferase;Transit peptide | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; green leaf volatile biosynthetic process [GO:0010597] | chloroplast [GO:0009507] | 3-deoxy-7-phosphoheptulonate synthase activity [GO:0003849]; metal ion binding [GO:0046872] | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:24815009}. | null | null | IPR013785;IPR002480; | 3.20.20.70; |
A0A067XR63 | MNAEGGNLHREFEITWGDGRARIHNNGGLLTLSLDRASGSGFRSKNEYLFGRIEIQIKLVAGNSAGTVATYYLSSEGPTHDEIDFEFLGNSSGEPYTLHTNVFSQGKGNREQQFFLWFDPTMDFHTYTILWNPQRIIFYVDETPIREFKNLERHGIPFPRSQAMRVYSSMWNADDWATRGGLVKTDWTKAPFTASYRSYKADACVWSGEASSCGSQDSNPSDKWWMTEELNATRMKRLRWVQKKYMVYNYCVDKMRFPEGLAPECNIS | Diospyros kaki (Kaki persimmon) (Diospyros chinensis) | FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Probably involved in cell wall assembly and synthesis in fast growing tissues and in the maintenance of firmness in mature fruits. {ECO:0000269|PubMed:27242828}. | 2.4.1.207 | CATALYTIC ACTIVITY: Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.; EC=2.4.1.207; Evidence={ECO:0000255|RuleBase:RU361120, ECO:... | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 5-6. Activity decreases sharply when the pH is lowered from 5 to 4. {ECO:0000269|PubMed:27242828}; | null | Cell wall biogenesis/degradation;Cytoplasm;Disulfide bond;Fruit ripening;Glycoprotein;Glycosidase;Glycosyltransferase;Hydrolase;Transferase | cell wall assembly [GO:0070726]; fruit ripening [GO:0009835]; xyloglucan metabolic process [GO:0010411] | apoplast [GO:0048046]; cytoplasm [GO:0005737] | hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; xyloglucan:xyloglucosyl transferase activity [GO:0016762] | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27242828}. Note=Dispersed throughout the cell. {ECO:0000269|PubMed:27242828}. | PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity. {ECO:0000255|RuleBase:RU361120}. | null | IPR044791;IPR008264;IPR013320;IPR000757;IPR008263;IPR010713;IPR016455; | 2.60.120.200; |
A0A067YMX8 | MAASPYSIFAVQLLLLASWMLSSSSSNFNQDFNIAWGGGRARILNNGELVTLSLDKASGSGFRSKNLYLFGKIDMQLKLVPGNSAGTVTTYYLSSEGSVRDEIDFEFLGNLTGEPYTLHTNVYSHGKGEREQQFRLWFDPAADFHTYSILWNSKTIVFYVDQTPVREFKNMESIGVPYLRQPMRLFSSIWNADEWATRGGLIKTDWTQAPFTTSYRNFRADNACVWAAKASSCGLAAGGNAWLSVELDAKSRGRLRWVRRNQMIYDYCVDGKRFPRGVPPECKLNLHI | Diospyros kaki (Kaki persimmon) (Diospyros chinensis) | FUNCTION: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Overexpression in Arabidopsis transgenic plants causes accelerated dark-induced leaf senescence and higher lipid peroxidation of the leaf cells. Overexpression in tr... | 2.4.1.207 | CATALYTIC ACTIVITY: Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.; EC=2.4.1.207; Evidence={ECO:0000255|RuleBase:RU361120, ECO:... | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 6. Activity decreases sharply when the pH is lowered from 5 to 4. {ECO:0000269|PubMed:27966647}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 30-40 degrees Celsius. {ECO:0000269|PubMed:27966647}; | Apoplast;Cell wall;Cell wall biogenesis/degradation;Disulfide bond;Fruit ripening;Glycoprotein;Glycosidase;Glycosyltransferase;Hydrolase;Secreted;Signal;Transferase | cell wall biogenesis [GO:0042546]; cell wall organization [GO:0071555]; cellular response to gibberellin stimulus [GO:0071370]; fruit ripening [GO:0009835]; response to abscisic acid [GO:0009737]; xyloglucan catabolic process [GO:2000899] | apoplast [GO:0048046] | hydrolase activity, hydrolyzing O-glycosyl compounds [GO:0004553]; polysaccharide binding [GO:0030247]; xyloglucan:xyloglucosyl transferase activity [GO:0016762] | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|RuleBase:RU361120, ECO:0000269|PubMed:27966647}. Secreted, extracellular space, apoplast {ECO:0000255|RuleBase:RU361120}. | PTM: Contains at least one intrachain disulfide bond essential for its enzymatic activity. {ECO:0000255|RuleBase:RU361120}. | null | IPR044791;IPR013320;IPR000757;IPR008263;IPR010713;IPR016455; | 2.60.120.200; |
A0A068C605 | MERLDKTINSYLDVWLGPRDPRVKGWLLLENYTPTFIFSVLYLLIVWLGPKYMRNKQPFSCRGILVVYNLGLTLLSLYMFYELVTGVWEGGYNFFCQDTHSGGEADMKIIRVLWWYYFSKLIEFMDTFFFILRKNNHQITVLHVYHHATMLNIWWFVMNWVPCGHSYFGATLNSFIHVLMYSYYGLSAVPAMRPYLWWKKYITQGQLTQFVLTIFQTSCGVVWPCAFPQGWLYFQISYMISLIILFTNFYIQTYNKKASSRRKEYQNGSAATVNGYTNSFSSLENNVKQRKQRKD | Anas platyrhynchos (Mallard) (Anas boschas) | FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that... | 2.3.1.199 | CATALYTIC ACTIVITY: Reaction=(11Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(13Z)-eicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39679, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:75121, ChEBI:CHEBI:76559; Evidence={ECO:0000256|ARBA:ARBA00001296}; PhysiologicalDirection=left... | null | null | PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03205}. | null | null | Cell projection;Endoplasmic reticulum;Fatty acid biosynthesis;Fatty acid metabolism;Lipid biosynthesis;Lipid metabolism;Membrane;Transferase;Transmembrane;Transmembrane helix | fatty acid elongation [GO:0030497]; fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; sphingolipid biosynthetic process [GO... | dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789] | fatty acid elongase activity [GO:0009922] | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03205}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03205}. Cell projection, dendrite {ECO:0000256|HAMAP-Rule:MF_03205}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=... | null | null | IPR002076;IPR033677; | null |
A0A072TFB1 | MKKLLAALALAVVAVPVWAATQTVTLSVPGMTCAACPITVKHALSQVTGVEKTDVRFEQREAVVTFDDGKTSVQALTKATADAGYPSPVCLAASCRRWAVRAASRDRQSGRHHWSGLPEPVRRVVHPHPATGLRRRRAVRQCGRLAQASAVAPYRARPDRAAAGAGSRVCDARLWRAQRLAALSRSRHYGGDIALGPVLPGPTQRSKAMMTLKIDGMTCASCAEHVRQALEKVPGVRSAAVSYSKALADLTVDEGVSHDTLTAAVTTAGYHARVADVPPHSAGLPGKTPGSAETGGKRSGGDSALRVAVIGSGGAAMAAA... | Medicago truncatula (Barrel medic) (Medicago tribuloides) | FUNCTION: Cleaves the carbon-mercury bond of organomercurials such as phenylmercuric acetate. One product is Hg(2+), which is subsequently detoxified by the mercuric reductase. {ECO:0000256|ARBA:ARBA00025326}. | 1.16.1.1; 4.99.1.2 | CATALYTIC ACTIVITY: Reaction=H(+) + Hg + NADP(+) = Hg(2+) + NADPH; Xref=Rhea:RHEA:23856, ChEBI:CHEBI:15378, ChEBI:CHEBI:16170, ChEBI:CHEBI:16793, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.1; Evidence={ECO:0000256|ARBA:ARBA00000896}; CATALYTIC ACTIVITY: Reaction=an alkylmercury + H(+) = an alkane + Hg(2+); Xref=Rh... | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|ARBA:ARBA00001974}; | null | null | null | null | Copper;FAD;Flavoprotein;Lyase;Mercuric resistance;Mercury;Metal-binding;NADP;Oxidoreductase;Periplasm;Redox-active center;Reference proteome;Signal | organomercury catabolic process [GO:0046413] | null | alkylmercury lyase activity [GO:0018836]; copper ion binding [GO:0005507]; flavin adenine dinucleotide binding [GO:0050660]; mercury (II) reductase activity [GO:0016152]; mercury ion binding [GO:0045340]; mercury ion transmembrane transporter activity [GO:0015097]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955];... | SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}. | null | null | IPR036188;IPR023753;IPR016156;IPR017969;IPR006122;IPR006121;IPR036163;IPR004927;IPR024259;IPR021179;IPR011795;IPR004099;IPR012999;IPR036390; | 3.30.390.30;3.30.450.410;3.30.70.100;3.50.50.60; |
A0A072ULZ1 | MEENKKTVDGSVDFTEEQEALVVKSWNAMKNNSCDLSLKFFTKILEIAPPAKQMFSFLKDSNVPLEQNPKLKPHAMSVFLMTCESAVQLRKAGKVRVRESNLKKLGATHFKTGVQDEHFEVTKQALLETIEEAIPEMWSLAMKNAWAEAHDQLANAIKVEMKEAHDQMDNANLIINMEENTGSCFTEEQEALVVKSWNAIKYNSGDLSLKFFKKILEIAPPAKQLFSFLKDSNVPLEHNPKLKPHAMSVFLMTCESAVQLRKAGKVTVRESNLKKLGATHFKTGVKDEHFEVTKQALLETIKEALPEMWSPAMENAWGEA... | Medicago truncatula (Barrel medic) (Medicago tribuloides) | FUNCTION: Phytoglobin that regulates the fine tuning of nitric oxide (NO) concentration in the cytosol in response to sudden changes in O(2) availability, and performs both symbiotic and nonsymbiotic functions (PubMed:33329665). Exhibits NO dioxygenase activity in the presence of O(2) but nitrite reductase (NiR) activi... | 1.7.2.- | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:00002... | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:33329665}; Note=Binds 2 heme groups per subunit. {ECO:0000269|PubMed:33329665}; | null | null | null | null | Alternative splicing;Cytoplasm;Heme;Iron;Metal-binding;Nodulation;Nucleus;Oxidoreductase;Oxygen transport;Reference proteome;Repeat;Transport | response to ammonium ion [GO:0060359]; response to hypoxia [GO:0001666]; response to nitrate [GO:0010167]; response to nitric oxide [GO:0071731]; response to symbiotic bacterium [GO:0009609] | null | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825] | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2XE98}. Nucleus {ECO:0000250|UniProtKB:A2XE98}. | null | null | IPR000971;IPR009050;IPR012292;IPR001032;IPR019824; | 1.10.490.10; |
A0A072UR65 | MANILNLKHLLTLALILLALATKSSTSSSSSITRVKGIYWLENPFFPPTTVDTSLFTHIFYSFLTPNNITYKLEISSSQILSLNTFTKTFKTKSPPAATLFSIGGAGSNSSLLAFIASDPPACAAFINSTIDVARTFGFDGIDLDWEFPKNTKEMNDLGEMLFQWRKAISDEGATTGRPPLLLTAAVYFAVNFSIYGEPRMYPVNSINENLDWVNVMSYELRGPRSNKTGAPSGTFDPKSNVSVVSGLLSWIHSGVVPEKLVMGMPLYGKSWKLRDPNVHGIGAPSVGSGPGVNGLMAYFQVLDFNRQKSAKVEYDVDTA... | Medicago truncatula (Barrel medic) (Medicago tribuloides) | FUNCTION: Possesses chitinase activity in vitro toward glycol chitin, carboxymethyl-chitin, colloidal chitin, and the chitin oligosaccharides (N-acetylglucosamine) (GlcNAc)6 and (GlcNAc)5 (PubMed:27383628). Hydrolyzes (GlcNAc)6 into (GlcNAc)4 and (GlcNAc)2, or two (GlcNAc)3 molecules (PubMed:27383628). Has the capacity... | 3.2.1.14 | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000255|PROSITE-ProRule:PRU10053, ECO:0000269|PubMed:27383628}; | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.5 mM for (GlcNAc)6 {ECO:0000269|PubMed:27383628}; KM=8.6 mM for (GlcNAc)5 {ECO:0000269|PubMed:27383628}; | PATHWAY: Glycan degradation; chitin degradation. {ECO:0000305}. | null | null | Carbohydrate metabolism;Chitin degradation;Glycoprotein;Glycosidase;Hydrolase;Plant defense;Polysaccharide degradation;Reference proteome;Signal | chitin catabolic process [GO:0006032]; defense response to fungus [GO:0050832]; polysaccharide catabolic process [GO:0000272] | extracellular region [GO:0005576] | chitin binding [GO:0008061]; chitinase activity [GO:0004568] | null | null | null | IPR011583;IPR029070;IPR001223;IPR001579;IPR017853; | 3.10.50.10;3.20.20.80; |
A0A072VDF2 | MPAATAAAAAESSSVSGETICVTGAGGFIASWMVKLLLEKGYTVRGTLRNPDDPKNGHLKKLEGAKERLTLVKVDLLDLNSVKEAVNGCHGVFHTASPVTDNPEEMVEPAVNGAKNVIIAGAEAKVRRVVFTSSIGAVYMDPNRSVDVEVDESCWSDLEFCKKTKNWYCYGKAVAEAAAWDVAKEKGVDLVVVNPVLVLGPLLQPTINASTIHILKYLTGSAKTYANATQAYVHVRDVALAHILVYEKPSASGRYLCAETSLHRGELVEILAKYFPEYPIPTKCSDEKNPRVKPHIFSNKKLKDLGLEFTPVSECLYETV... | Medicago truncatula (Barrel medic) (Medicago tribuloides) | FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:20876124). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:20876124). Mediates the conversion of feruloyl-CoA to coniferylaldehyde (PubMed:20876124). Also ... | 1.2.1.-; 1.2.1.44 | CATALYTIC ACTIVITY: Reaction=(E)-coniferaldehyde + CoA + NADP(+) = (E)-feruloyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64648, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87305; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to... | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=54.5 uM for feruloyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; KM=7.2 uM for sinapoyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; KM=161 uM for caffeoyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|Pub... | PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000250|UniProtKB:A0A059TC02}. | null | null | Cytoplasm;Disulfide bond;NADP;Oxidoreductase;Reference proteome | lignin biosynthetic process [GO:0009809]; phenylpropanoid biosynthetic process [GO:0009699] | cytoplasm [GO:0005737] | cinnamoyl-CoA reductase activity [GO:0016621]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A059TC02}. | PTM: The formation of a reversible disulfide bond reduces activity by perturbing the positioning of nearby catalytic residues. {ECO:0000250|UniProtKB:A0A059TC02}. | null | IPR001509;IPR036291; | 3.40.50.720; |
A0A075D5I4 | MAEKQQAVAEFYDNSTGAWEVFFGDHLHDGFYDPGTTATIAGSRAAVVRMIDEALRFANISDDPAKKPKTMLDVGCGIGGTCLHVAKKYGIQCKGITISSEQVKCAQGFAEEQGLEKKVSFDVGDALDMPYKDGTFDLVFTIQCIEHIQDKEKFIREMVRVAAPGAPIVIVSYAHRNLSPSEGSLKPEEKKVLKKICDNIVLSWVCSSADYVRWLTPLPVEDIKAADWTQNITPFYPLLMKEAFTWKGFTSLLMKGGWSAIKVVLAVRMMAKAADDGVLKFVAVTCRKSK | Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum) | FUNCTION: S-adenosyl-L-methionine-dependent N-methyltransferase involved in the biosynthesis of biologically active monoterpenoid indole alkaloids (MIAs) natural products including vindoline (PubMed:26848097). Catalyzes the conversion of picrinine to N-methylpicrinine (ervincine) (PubMed:26848097). Accepts also, with l... | 2.1.1.- | CATALYTIC ACTIVITY: Reaction=picrinine + S-adenosyl-L-methionine = ervincine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:76143, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:70505, ChEBI:CHEBI:194555; Evidence={ECO:0000269|PubMed:26848097}; PhysiologicalDirection=left-to-right; Xref=Rhea:R... | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for picrinine {ECO:0000269|PubMed:26848097}; KM=9.3 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:26848097}; Vmax=126.1 pmol/sec/mg enzyme with picrinine as substrate {ECO:0000269|PubMed:26848097}; Vmax=97.2 pmol/sec/mg enzyme with S-adenosyl-L-methionin... | PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis. {ECO:0000269|PubMed:26848097}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:26848097}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 22 degrees Celsius. {ECO:0000269|PubMed:26848097}; | Alkaloid metabolism;Membrane;Methyltransferase;S-adenosyl-L-methionine;Transferase;Vacuole | alkaloid biosynthetic process [GO:0009821]; methylation [GO:0032259]; vindoline biosynthetic process [GO:1900985] | plant-type vacuole membrane [GO:0009705] | N-methyltransferase activity [GO:0008170] | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:35166361}. | null | null | IPR025714;IPR025774;IPR029063; | 3.40.50.150; |
A0A075D657 | MYTCSIIIYILTFWQLSKIKKQVAAAEKQVMTVTEKQEAVAEFYDKSTDAWEVFFGEHLHDGFYEPGTTATIPGSKVAVVRMIDELLRFAGISDDPEKKPKTMLDVGCGLGGTCLHVAKKYDIKCTGITISPEQVKCAQDLAATQGLESKVSFDVGDALDMPYKDGTFDLVFTIQCIEHIQDKEKFIREMVRVAAPGAPVVIAGYAARNLSPSEESLKPEEKMVLEKICDHIVLSWLCSTGDYVKWLTPLPVQDIKVWDLTQNITPFYPLCIKEAFTWKSFTSLLKMGGWSAIKVVFAVKMMAMAAEEGLLKFAAVTCRK... | Vinca minor (Common periwinkle) | FUNCTION: S-adenosyl-L-methionine-dependent N-methyltransferase involved in the biosynthesis of biologically active monoterpenoid indole alkaloids (MIAs) natural products including vindoline (PubMed:26848097). Catalyzes the conversion of picrinine to N-methylpicrinine (ervincine) (PubMed:26848097). Accepts also, with l... | 2.1.1.- | CATALYTIC ACTIVITY: Reaction=picrinine + S-adenosyl-L-methionine = ervincine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:76143, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:70505, ChEBI:CHEBI:194555; Evidence={ECO:0000269|PubMed:26848097}; PhysiologicalDirection=left-to-right; Xref=Rhea:R... | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20.1 uM for picrinine {ECO:0000269|PubMed:26848097}; KM=15.8 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:26848097}; Vmax=100.8 pmol/sec/mg enzyme with picrinine as substrate {ECO:0000269|PubMed:26848097}; Vmax=135 pmol/sec/mg enzyme with S-adenosyl-L-methion... | PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis. {ECO:0000269|PubMed:26848097}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:26848097}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 22 degrees Celsius. {ECO:0000269|PubMed:26848097}; | Alkaloid metabolism;Cytoplasm;Methyltransferase;S-adenosyl-L-methionine;Transferase | alkaloid biosynthetic process [GO:0009821]; methylation [GO:0032259]; vindoline biosynthetic process [GO:1900985] | cytosol [GO:0005829] | N-methyltransferase activity [GO:0008170]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:35166361}. | null | null | IPR013216;IPR025774;IPR029063; | 3.40.50.150; |
A0A075FBG7 | MSITFNLKIAPFSGPGIQRSKETFPATEIQITASTKSTMTTKCSFNASTDFMGKLREKVGGKADKPPVVIHPVDISSNLCMIDTLQSLGVDRYFQSEINTLLEHTYRLWKEKKKNIIFKDVSCCAIAFRLLREKGYQVSSDKLAPFADYRIRDVATILELYRASQARLYEDEHTLEKLHDWSSNLLKQHLLNGSIPDHKLHKQVEYFLKNYHGILDRVAVRRSLDLYNINHHHRIPDVADGFPKEDFLEYSMQDFNICQAQQQEELHQLQRWYADCRLDTLNYGRDVVRIANFLTSAIFGEPEFSDARLAFAKHIILVTR... | Marrubium vulgare (White horehound) | FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid including marrubiin and other labdane-related furanoid diterpenoids with potential applications as anti-diabetics, analgesics or vasorelaxants (Probable). Terpene synthase the catalyzes the conversion of peregrinol diphosphate to 9,13(R)-epoxy-labd-14-e... | 4.2.3.131; 4.2.3.189; 4.2.3.190 | CATALYTIC ACTIVITY: Reaction=peregrinol diphosphate = (13R)-9,13-epoxylabd-14-ene + diphosphate; Xref=Rhea:RHEA:54512, ChEBI:CHEBI:33019, ChEBI:CHEBI:138232, ChEBI:CHEBI:138233; EC=4.2.3.189; Evidence={ECO:0000269|PubMed:24990389}; CATALYTIC ACTIVITY: Reaction=(+)-copalyl diphosphate = diphosphate + miltiradiene; Xref=... | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q40577}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577}; | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:24990389}. | null | null | Chloroplast;Lyase;Magnesium;Metal-binding;Plastid;Transit peptide | gibberellin biosynthetic process [GO:0009686]; miltiradiene biosynthetic process [GO:1901946] | chloroplast [GO:0009507] | 9,13-epoxylabda-14-ene synthase activity [GO:0106239]; magnesium ion binding [GO:0000287]; manoyl oxide synthase activity [GO:0062206]; miltiradiene synthase activity [GO:0062205]; terpene synthase activity [GO:0010333] | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | null | DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+). {ECO:0000250|UniProtKB:G8GJ94}. | IPR008949;IPR001906;IPR036965;IPR005630;IPR008930; | 1.10.600.10;1.50.10.130; |
A0A075TMP0 | MASTTPSTYKQAVFKEQGAGLTLEEVALTLPKRDEILVKVEACGVCHSDHFAQTNLMGGGFPLVPGHEIIGRVAAVGEGETVWKEGDRIGGAWHGGHDGTCGACKKGFFQMCDNEQVNGISRNGGYAEYCIIRREAAVHIPDHVNAAKYAPMLCAGVTVFNAMRHMKIPPGELVAIQGLGGLGHLALQYANKFGYRVVALSRDSTKEEFARKLGAHEYIDTSREDPVAALQKLGGASLIVSTAPVPEIINPLIQGLGVMGKLLILSIVGGIEVHTGLLVGKGKSIWSWPSGHATDSEDAIAFADLHGIDCLIEEFPLDKC... | Penicillium expansum (Blue mold rot fungus) | FUNCTION: Alcohol dehydrogenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatD catalyzes the conversion... | 1.1.1.- | CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + neopatulin = (E)-ascladiol + NADP(+); Xref=Rhea:RHEA:62224, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145111, ChEBI:CHEBI:145112; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62225; Evidence={ECO:00002... | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q96533}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q96533}; | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | Cytoplasm;Metal-binding;NAD;NADP;Oxidoreductase;Reference proteome;Zinc | patulin biosynthetic process [GO:0140723] | cytosol [GO:0005829] | alcohol dehydrogenase (NAD+) activity [GO:0004022]; alcohol dehydrogenase (NADP+) activity [GO:0008106]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; polyketide synthase activity [GO:0016218] | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}. | null | null | IPR013149;IPR013154;IPR011032;IPR036291;IPR020843; | 3.90.180.10;3.40.50.720; |
A0A075TMP8 | MDILQLAPTHLLAILLSSTSALFLITYLLRAGHRPSDLPNGPPTVPLFGNELQVPKSDAHFQFSRWAKEYGGFFTLKRYNNTTIVISDQKLIKTLLDKKSNIYSHRPASLVSHLITQSDHLLVMQYGERWRMLRKTIHQYFMEPRCERDHWKVQEAEAKQMLHDYLTMPEDHMLHPKRYSNSITNSLVFGIRTKTVHDEYMKKLFYLMDKWSLVQELGATPPVDSFALLRYVPQWMLGNWRNRAVEVGDLMQSLYQTVLDQVKERRQRGIQRDSFMDRVLDTLKQTPLSENELRFLGGVLMEGGSDTSSSLILTIIQAMT... | Penicillium expansum (Blue mold rot fungus) | FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatI catalyzes the co... | 1.-.-.- | CATALYTIC ACTIVITY: Reaction=3-hydroxybenzyl alcohol + O2 + reduced [NADPH--hemoprotein reductase] = gentisyl alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:62212, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:5325, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI... | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | Endoplasmic reticulum;Glycoprotein;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix | patulin biosynthetic process [GO:0140723] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; polyketide synthase activity [GO:0016218] | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30680886}; Single-pass membrane protein {ECO:0000269|PubMed:30680886}. | null | null | IPR001128;IPR002401;IPR036396; | 1.10.630.10; |
A0A075TR33 | MRLHQSPPRLLVCILSVLQVSAGLSSNCRCMPGDSCWPSLNDWARFNTSIGGRLVDTQPLGQPCHDPFYTASECNELKQQWTHPELHDASSSSIMSAAVANETCDAFTPRSKPCTLGAMVRYAVNASSPDDFVQTIRFSQERNIRLVIRNTGHDYAGKSTGAGALSIWTHSLKEIDFLNYTSAHYTGPAVRMTAGIQGTDINPAAHKKGLVIVGGECATVGPVGGFTQGGGHSALSSRFGLAADQVLEWEVVDGMGRLLTASPTQNPDLYWALSGGGGGTFGVVYAVTVKTFPDFAVTGVVLQFENIDPSSNRFFEAVGH... | Penicillium expansum (Blue mold rot fungus) | FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatO acts with patJ in th... | 1.-.-.- | null | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305}; | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | FAD;Flavoprotein;Glycoprotein;Oxidoreductase;Reference proteome;Signal;Vacuole | patulin biosynthetic process [GO:0140723] | fungal-type vacuole lumen [GO:0000328]; vacuole [GO:0005773] | FAD binding [GO:0071949]; oxidoreductase activity [GO:0016491]; polyketide synthase activity [GO:0016218] | SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:30680886}. | null | null | IPR012951;IPR016166;IPR036318;IPR016169;IPR006094; | 3.30.465.10; |
A0A075TR41 | MAPFVPYHYSAGQSTIVKFGGLLTTEFLEPPPGRCFLFRQTYRHTIEGSIPENLRKLINSPDRPKGPPPHFHQFQTEYFRVENGVLGISVDGVVRRITPEDGEISVKAGSVHNFFIHPDSPENMTVYLSASDSGNDYQLDRVFFENWYGYWHDALLHDGGIDWIQFLAIQDGGDAYTPAPAWVPFRRQVGYWTCVIVGRWIGGLLGYKPFFREYTTDWDFAVAKMKGSFFQRHLVHAAFEEEKSWTKQAELEPKGKPENAEFEPWTEDMSPAPLSLGPVAYEQGLFHGVQPGSVNGSNGHSTGVESKLEQLGSRAQRRVV... | Penicillium expansum (Blue mold rot fungus) | FUNCTION: Probable oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatJ acts with patO in the ... | 1.-.-.- | null | null | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | Cytoplasmic vesicle;Oxidoreductase;Reference proteome;Vacuole | patulin biosynthetic process [GO:0140723] | cytoplasmic vesicle lumen [GO:0060205]; fungal-type vacuole lumen [GO:0000328]; vacuole [GO:0005773] | oxidoreductase activity [GO:0016491]; polyketide synthase activity [GO:0016218] | SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:30680886}. Cytoplasmic vesicle lumen {ECO:0000269|PubMed:30680886}. | null | null | IPR014710;IPR011051; | 2.60.120.10; |
A0A075TRC0 | MHSVSPSTYPSGGTSPAPADTPGTEYSEYEFSNDVAVVGMACRVAGGNHNPELLWQSLLSQKSAVGEIPEMRWEPYYRRDPRNAKELKKTTSRGYFLDRLEDFDCQFFGISPKEAEQMDPQQRVSLEVASEALEDAGIPAKSLSGSDTAVFWGVNSDDYSKLVLEDLPNVEAWMGIGTAYCGVPNRISYHLNLMGPSTAVDAACASSLVAVHHGVQAIRLGESQVAIVGGVNALCGPGLTRVLDKAGAISSDGSCKSFDDDAHGYARGEGAGALVLKSLHRALLDHDNVLAVIKGSAVAQDGKTNGIMAPNAKAQQLAAR... | Penicillium expansum (Blue mold rot fungus) | FUNCTION: 6-methylsalicylic acid synthase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886, PubMed:35339702). Pa... | 2.3.1.165 | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 3 H(+) + 3 malonyl-CoA + NADPH = 6-methylsalicylate + 3 CO2 + 4 CoA + H2O + NADP(+); Xref=Rhea:RHEA:12240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:36658, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; ... | null | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | Cytoplasm;Multifunctional enzyme;NADP;Phosphopantetheine;Phosphoprotein;Reference proteome;Transferase | fatty acid biosynthetic process [GO:0006633]; patulin biosynthetic process [GO:0140723] | cytosol [GO:0005829] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; 6-methylsalicylic acid synthase activity [GO:0050641]; fatty acid synthase activity [GO:0004312]; phosphopantetheine binding [GO:0031177]; polyketide synthase activity [GO:0016218] | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}. | null | DOMAIN: Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a produ... | IPR001227;IPR036736;IPR014043;IPR016035;IPR018201;IPR014031;IPR014030;IPR016036;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049552;IPR013968;IPR049900;IPR020806;IPR009081;IPR006162;IPR016039; | 3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.366.10;3.40.50.720;3.10.129.110; |
A0A075TRK9 | MRLTSGIFHAAIAVAAVGAVLPEGPSSSKTHRNEYARRMLGSSFGIPKNQTFDYLVIGGGTAGLTIATRLAEQGVGSVAVIEAGGFYELNNGNLSQIPAQDAFYVGTDLDDWQPGIDWGFHTTPQAGAYDRVSHYARGKCLGGSSARNYMAYQRGTKAAHQRWADTVGDSSYTWEQFLPFFEKSLHFTPANDALRGANASVVSDPSVLGNGDGPLSVTYPHYAQAFATWAKHAFIEIGLQIRSGFQSGALLGQSYGLYTINATTMHRESSETSFLRKGLADPNLTVFQSALAKRIRFQDKRAVGVDVETMGRAYTLSARK... | Penicillium expansum (Blue mold rot fungus) | FUNCTION: Patulin synthase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatE catalyzes the last step of th... | 1.1.-.- | CATALYTIC ACTIVITY: Reaction=(E)-ascladiol + A = AH2 + patulin; Xref=Rhea:RHEA:62228, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:74926, ChEBI:CHEBI:145112; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62229; Evidence={ECO:0000269|PubMed:30680886}; | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:E4QP00}; | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | 3D-structure;Cell wall;Cytoplasm;FAD;Flavoprotein;Glycoprotein;Oxidoreductase;Reference proteome;Secreted;Signal;Vacuole | patulin biosynthetic process [GO:0140723] | cell cortex [GO:0005938]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; vacuole [GO:0005773] | flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on CH-OH group of donors [GO:0016614]; polyketide synthase activity [GO:0016218] | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:30680886}. Vacuole {ECO:0000269|PubMed:30680886}. Secreted {ECO:0000269|PubMed:30680886}. Secreted, cell wall {ECO:0000269|PubMed:30680886}. | null | null | IPR036188;IPR012132;IPR000172;IPR007867; | 3.50.50.60;3.30.560.10; |
A0A075TRL5 | MEPFLLLLLVLLPAIVLVRYAFTYGHRTSTMPIGPPTLPFIGNIHQITKKYTHIKFTEWAAQYGGLYMLKIGNGNMAVITDRRLVKEVLDRKSGIYSHRPHSFVSHDLITKGNHLLVMHYGDQWRTFRRLVHQHLMETMVENHHTKIVNAEAIQLVRDYMIDPEHHMAHPKRYSNSITNSIVFGIRTANREGANMRRLYKLMEEWSEVMETGATPPVDLFPWLKLLPQWLFNNYIDRAKAIGVQMETLYVDILNKVIKRREDGHNNGTFMDKVLDSQEKHNLPWHQLAFIGGVLMEGGSDTSSSLTLAIVQALIQNPDVQ... | Penicillium expansum (Blue mold rot fungus) | FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatH catalyzes the co... | 1.-.-.- | CATALYTIC ACTIVITY: Reaction=3-methylphenol + O2 + reduced [NADPH--hemoprotein reductase] = 3-hydroxybenzyl alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:62208, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17069, ChEBI:... | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | Endoplasmic reticulum;Glycoprotein;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix | patulin biosynthetic process [GO:0140723] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]; polyketide synthase activity [GO:0016218] | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30680886}; Single-pass membrane protein {ECO:0000269|PubMed:30680886}. | null | null | IPR001128;IPR002401;IPR036396; | 1.10.630.10; |
A0A075TXZ1 | MAKIDVHHHFYPPAMRQALDRAGGDPSGWYIPPWTLELDQDITRQMKVTTTILSVTAPGPGIEPDVTKAAALARSCNESAAAIRDAKPQQYGFFASVPSLFDTAAVLKEIEYACTTLRADGVTLFTRYGKGSNYLGHAAFRPIWADLSRRGAVVFIHPTHPVDTQLINTWLPQPMFDYPHETGRAAMDLLTSGILQDYPGCKIILSHAGGTLPYLIHRAATMLPLMPRTLGLSTEELVEAARTFYFDTAISSNPVTLKALFEFAAPGHVLFGSDFPNAPHDAILRFTNFLEAYELPEETKRQVDSGAALELFPRLKGILD... | Penicillium expansum (Blue mold rot fungus) | FUNCTION: 6-methylsalicylic acid decarboxylase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (PubMed:25625822, PubMed:30100914, PubMed:30680886). PatG catalyzes... | 4.1.1.52 | CATALYTIC ACTIVITY: Reaction=6-methylsalicylate + H(+) = 3-methylphenol + CO2; Xref=Rhea:RHEA:23112, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17231, ChEBI:CHEBI:36658; EC=4.1.1.52; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23113; Evidence={ECO:0000269|PubMed:3... | null | null | PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}. | null | null | Cytoplasm;Decarboxylase;Hydrolase;Lyase;Metal-binding;Reference proteome;Zinc | patulin biosynthetic process [GO:0140723] | cytosol [GO:0005829] | 6-methylsalicylate decarboxylase activity [GO:0047596]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; polyketide synthase activity [GO:0016218] | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}. | null | null | IPR032465;IPR006680;IPR032466; | 3.20.20.140; |
A0A076FFM5 | MPFPMEVLQASSLSFPLLRRHSRNNLINKFRNPTLPRIDIPRQNIDLKTFAATTPTVACPPSDPEIIPEKKEDKFDWYENWYPVATVCDLDKRRPHGRKVIGIDVVVWWDRKENAWKVFDDTCPHRLAPLSEGRIDQWGRLQCVYHGWCFDGVGACKFIPQAPHDGPPVETSKKACVKGVYPSCVRNGIVWFWPNSDPKYKDIYLTNKPHYIPELDDPSFTCTTITREVPYGYEILAENLMDPSHVPYAHYGILELEKVKESSKRDREGGHEMEISVGTIDVNGFSAKHVSADYYFVPPYVYYGRITPNAATKTKDATLP... | Ocimum basilicum (Sweet basil) | FUNCTION: Rieske-type, PAO-family oxygenase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proli... | 1.14.15.- | CATALYTIC ACTIVITY: Reaction=2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] + salvigenin = 8-hydroxysalvigenin + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:73455, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:C... | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for salvigenin {ECO:0000269|PubMed:25139498}; Vmax=60.3 pmol/sec/mg enzyme with salvigenin as substrate {ECO:0000269|PubMed:25139498}; | PATHWAY: Flavonoid metabolism. {ECO:0000303|PubMed:30468448}. | null | null | 2Fe-2S;Chloroplast;Cytoplasm;Iron;Iron-sulfur;Membrane;Metal-binding;Oxidoreductase;Plastid;Transit peptide;Transmembrane;Transmembrane helix | flavonoid metabolic process [GO:0009812] | chloroplast [GO:0009507]; chloroplast membrane [GO:0031969]; cytoplasm [GO:0005737] | 2 iron, 2 sulfur cluster binding [GO:0051537]; chlorophyllide a oxygenase [overall] activity [GO:0010277]; metal ion binding [GO:0046872]; monooxygenase activity [GO:0004497] | SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000269|PubMed:25139498}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:25139498}. | null | null | IPR013626;IPR017941;IPR036922; | 2.102.10.10; |
A0A078CGE6 | MARQMTSSQFHKSKTLDNKYMLGDEIGKGAYGRVYIGLDLENGDFVAIKQVSLENIVQEDLNTIMQEIDLLKNLNHKNIVKYLGSLKTKTHLHIILEYVENGSLANIIKPNKFGPFPESLVTVYIAQVLEGLVYLHEQGVIHRDIKGANILTTKEGLVKLADFGVATKLNEADVNTHSVVGTPYWMAPEVIEMSGVCAASDIWSVGCTVIELLTCVPPYYDLQPMPALFRIVQDDSPPIPDSLSPDITDFLRQCFKKDSRQRPDAKTLLSHPWIRNSRRALQSSLRHSGTIRYMKGADSSSEKDGEGSQDIAESVSAEKV... | Brassica napus (Rape) | FUNCTION: Serine/threonine-protein kinase involved in the spatial and temporal control system organizing cortical activities in mitotic and postmitotic cells (PubMed:11489177). Required for the normal functioning of the plasma membrane in developing pollen. Involved in the regulation of cell expansion and embryo develo... | 2.7.11.1 | 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:11489177}; CATALYTIC... | null | null | null | null | null | ATP-binding;Cell cycle;Cell division;Cell membrane;Cytoplasm;Cytoskeleton;Kinase;Membrane;Nucleotide-binding;Nucleus;Phosphoprotein;Repeat;Serine/threonine-protein kinase;Transferase | cell cycle [GO:0007049]; cell division [GO:0051301]; MAPK cascade [GO:0000165]; protein autophosphorylation [GO:0046777]; regulation of cell division [GO:0051302] | cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nucleolus [GO:0005730]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q8T2I8}. Nucleus, nucleolus {ECO:0000269|PubMed:15292395}. Cell membrane {ECO:0000250|UniProtKB:Q9LJD8}. Note=Accumulates in the nucleolus during interphase (PubMed:15292395). Localized to the plasma membrane in developi... | PTM: Autophosphorylated. {ECO:0000269|PubMed:11489177}. | null | IPR011989;IPR016024;IPR011009;IPR000719;IPR017441;IPR001245;IPR008271; | 1.25.10.10;1.10.510.10; |
A0A087QH05 | LQCYCHLCTKDNFTCVTDGLCFTSVTRTADKVIHNSMCIAEIDLIPRDRPFVCAPSARDGVITLPHCCDKDHCNKIELPIPTPGKPASNLGPVELAAVIAGPVCFVCISLMLILYLCHNRTVIHHRVPSEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIAD... | Aptenodytes forsteri (Emperor penguin) | null | 2.7.11.30 | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.30; Evidence={ECO:0000256|ARBA:AR... | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|ARBA:ARBA00001936}; | null | null | null | null | Apoptosis;ATP-binding;Cell junction;Differentiation;Growth regulation;Isopeptide bond;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Serine/threonine-protein kinase;Signal;Tight junction;Transferase;Transmembrane;Transmembrane helix;Ubl conjugation | activin receptor signaling pathway [GO:0032924]; apoptotic process [GO:0006915]; cardiac epithelial to mesenchymal transition [GO:0060317]; endothelial cell activation [GO:0042118]; heart development [GO:0007507]; intracellular signal transduction [GO:0035556]; mesenchymal cell differentiation [GO:0048762]; nervous sys... | activin receptor complex [GO:0048179]; bicellular tight junction [GO:0005923]; cell surface [GO:0009986]; membrane [GO:0016020]; membrane raft [GO:0045121] | activin binding [GO:0048185]; activin receptor activity, type I [GO:0016361]; ATP binding [GO:0005524]; SMAD binding [GO:0046332]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity, type I [GO:0005025] | SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cell surface {ECO:0000256|ARBA:ARBA00004241}. Membrane raft {ECO:0000256|ARBA:ARBA00004285}. Membrane {ECO:0000256|ARBA... | null | null | IPR000472;IPR003605;IPR011009;IPR000719;IPR017441;IPR008271;IPR045860;IPR000333; | 2.10.60.10;1.10.510.10; |
A0A087X1C5 | MGLEALVPLAMIVAIFLLLVDLMHRHQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREAMVTRGEDTADRPPAPIYQVLGFGPRSQGVILSRYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFADQAGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLPHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAKKEKAKGSPESSFNDENLRIVVGNLFLAGMVTTSTTLAWGLLL... | Homo sapiens (Human) | FUNCTION: May be responsible for the metabolism of many drugs and environmental chemicals that it oxidizes. It may be involved in the metabolism of codeine to morphine (PubMed:15051713). However, another study could not confirm it (PubMed:18838503). {ECO:0000269|PubMed:15051713, ECO:0000269|PubMed:18838503}. | 1.14.14.1 | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; | null | null | null | null | Cytoplasm;Glycoprotein;Heme;Iron;Membrane;Metal-binding;Mitochondrion;Monooxygenase;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix | arachidonic acid metabolic process [GO:0019369]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739] | aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712] | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000305|PubMed:15051713}. Mitochondrion {ECO:0000269|PubMed:18838503}. | null | null | IPR001128;IPR017972;IPR002401;IPR008069;IPR036396; | 1.10.630.10; |
A0A087X296 | MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPGLWTWLRNSLRPSPSFTHFLLTHGRWFWEFVNATFIREMLMRLVLTGKKQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGV... | Homo sapiens (Human) | null | 1.14.99.1 | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = prostaglandin G2; Xref=Rhea:RHEA:42596, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82629; Evidence={ECO:0000256|ARBA:ARBA00000144}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597; Evidence={ECO:0000256|ARBA:ARBA00000144}; CATALYT... | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000256|ARBA:ARBA00001970}; | null | PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000256|ARBA:ARBA00004702}. | null | null | Dioxygenase;EGF-like domain;Endoplasmic reticulum;Fatty acid biosynthesis;Fatty acid metabolism;Heme;Iron;Lipid biosynthesis;Lipid metabolism;Metal-binding;Microsome;Oxidoreductase;Peroxidase;Prostaglandin biosynthesis;Prostaglandin metabolism;Proteomics identification;Reference proteome;Signal | cyclooxygenase pathway [GO:0019371]; response to oxidative stress [GO:0006979] | endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; neuron projection [GO:0043005] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666] | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Microsome membrane {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004174}. | null | null | IPR000742;IPR019791;IPR010255;IPR037120; | 1.10.640.10;2.10.25.10; |
A0A089QRB9 | MRTATATSVAVIGMACRLPGGIDSPQRLWEALLRGDDLVGEIPADRWDANVYYDPEPGVPGRSVSRWGAFLDDVGGFDCDFFGLTEREATAIDPQHRLLLEVSWEAIEHAGVDPATLAESQTGVFVGLTHGDYELLSADCGAAEGPYGFTGTSNSFASGRVAYTLGLHGPAVTVDTACSSGLTAVHQACRSLDDGESDLALAGGVVVTLEPRKSVSGSLQGMLSPTGRCHAFDEAADGFVSGEGCVVLLLKRLPDAVRDGDRVLAIVRGTAANQDGRTVNIAAPSAQAQIAVYQQALAAAGVEASTVGMVEAHGTGTPVG... | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) | FUNCTION: Polyketide synthase involved in the biosynthesis of methyl-branched fatty acids such as mycolipanoic, mycolipenic (phthienoic) and mycolipodienoic acids required for the synthesis of a major class of polyacylated trehaloses. Catalyzes the elongation of CoA esters of long-chain fatty acids by incorporation of ... | 2.3.1.252 | CATALYTIC ACTIVITY: Reaction=3 (S)-methylmalonyl-CoA + a long-chain fatty acyl-CoA + 9 H(+) + holo-[mycolipanoate synthase] + 6 NADPH = 3 CO2 + 4 CoA + 3 H2O + long-chain mycolipanoyl-[mycolipanoate synthase] + 6 NADP(+); Xref=Rhea:RHEA:50344, Rhea:RHEA-COMP:12617, Rhea:RHEA-COMP:12618, ChEBI:CHEBI:15377, ChEBI:CHEBI:1... | null | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305|PubMed:12207710}. | null | null | Acyltransferase;Cell membrane;Direct protein sequencing;Lipoprotein;Membrane;Multifunctional enzyme;NADP;Palmitate;Phosphopantetheine;Phosphoprotein;Reference proteome;Signal;Transferase | DIM/DIP cell wall layer assembly [GO:0071770]; methyl-branched fatty acid biosynthetic process [GO:1902321]; secondary metabolite biosynthetic process [GO:0044550] | plasma membrane [GO:0005886]; polyketide synthase complex [GO:0034081] | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. | null | null | IPR001227;IPR036736;IPR014043;IPR016035;IPR013149;IPR013154;IPR011032;IPR018201;IPR014031;IPR014030;IPR016036;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049551;IPR049552;IPR020843;IPR013968;IPR049900;IPR020806;IPR009081;IPR016039; | 3.40.47.10;1.10.1200.10;3.30.70.250;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110; |
A0A090N8E9 | MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHRKCNYSFHATPNTYKRKNTETAL... | Homo sapiens (Human) | null | 2.1.1.356 | CATALYTIC ACTIVITY: Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEB... | null | null | null | null | null | Biological rhythms;Chromatin regulator;Methyltransferase;Nucleus;Repressor;S-adenosyl-L-methionine;Transcription;Transcription regulation;Transferase | B cell differentiation [GO:0030183]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to trichostatin A [GO:0035984]; cerebellar cortex development [GO:0021695]; facultative heterochromatin formation [GO:0140718]; G1 to G0 transition [... | chromatin silencing complex [GO:0005677]; ESC/E(Z) complex [GO:0035098]; nucleoplasm [GO:0005654]; pericentric heterochromatin [GO:0005721]; pronucleus [GO:0045120]; synapse [GO:0045202] | chromatin DNA binding [GO:0031490]; histone H3K27 trimethyltransferase activity [GO:0140951]; lncRNA binding [GO:0106222]; primary miRNA binding [GO:0070878]; ribonucleoprotein complex binding [GO:0043021]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promot... | SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. | null | null | IPR026489;IPR045318;IPR048358;IPR021654;IPR044439;IPR041343;IPR041355;IPR001005;IPR001214;IPR046341;IPR033467; | 1.20.58.1880;2.170.270.10; |
A0A093GWH1 | MLRLSTLLRRTRPVSRALAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKAIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARAIAREGFEKISKGANPVEIRRGVMLAVDAVITELKKLSKPVTTPEEIAQVATISANGDQEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLISEKKISSVQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIAT... | Struthio camelus australis | FUNCTION: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondria... | 5.6.1.7 | CATALYTIC ACTIVITY: Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000256|ARBA:ARBA00034033}; | null | null | null | null | null | ATP-binding;Chaperone;Nucleotide-binding;Reference proteome | apoptotic mitochondrial changes [GO:0008637]; B cell proliferation [GO:0042100]; biological process involved in interaction with symbiont [GO:0051702]; cellular response to interleukin-7 [GO:0098761]; chaperone cofactor-dependent protein refolding [GO:0051085]; isotype switching to IgG isotypes [GO:0048291]; mitochondr... | cell surface [GO:0009986]; clathrin-coated pit [GO:0005905]; coated vesicle [GO:0030135]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; GroEL-GroES complex [GO:1990220]; lipopolysaccharide receptor complex [GO:0046696]; migrasome [GO:0140494]; mitochondrial inner membrane [GO:0005743]; mitochondrial ... | apolipoprotein A-I binding [GO:0034186]; ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; double-stranded RNA binding [GO:0003725]; high-density lipoprotein particle binding [GO:0008035]; lipopolysaccharide binding [GO:0001530]; p53 binding [GO:0002039]; protein-folding chaperone binding ... | null | null | null | IPR018370;IPR001844;IPR002423;IPR027409;IPR027413;IPR027410; | 3.50.7.10;1.10.560.10;3.30.260.10; |
End of preview. Expand in Data Studio
README.md exists but content is empty.
- Downloads last month
- 3