Datasets:

lhallee

/

exp_new_unprocessed

like 0

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 product (PubMed:36048923). {ECO:0000269|PubMed:29395922, ECO:0000269|PubMed:36048923}.

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 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:0000269|PubMed:29395922, ECO:0000269|PubMed:36048923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000269|PubMed:29395922, ECO:0000269|PubMed:36048923}; CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) = ADP-D-ribose 2'-phosphate + H(+) + nicotinamide; Xref=Rhea:RHEA:19849, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:58349, ChEBI:CHEBI:58673; Evidence={ECO:0000269|PubMed:36048923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19850; Evidence={ECO:0000269|PubMed:36048923};

3D-structure;Coiled coil;Hydrolase;NAD

NAD catabolic process [GO:0019677]; signal transduction [GO:0007165]

NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NADP+ nucleosidase activity [GO:0050135]

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:36048923}.

IPR000157;IPR035897;

3.40.50.10140;

A0A023I7E1

MRFQVIVAAATITMITSYIPGVASQSTSDGDDLFVPVSNFDPKSIFPEIKHPFEPMYANTENGKIVPTNSWISNLFYPSADNLAPTTPDPYTLRLLDGYGGNPGLTIRQPSAKVLGSYPPTNDVPYTDAGYMINSVVVDLRLTSSEWSDVVPDRQVTDWDHLSANLRLSTPQDSNSYIDFPIVRGMAYITANYNNLTPQFLSQHAIISVEADEKKSDDNTSTFSGRKFKITMNDDPTSTFIIYSLGDKPLELRKQDNSNLVASKPYTGVIRVAKLPAPEFETLLDASRAVWPTGGDISARSDDNNGASYTIKWKTNSNEAPLLTYAYAHHLTSIDDSNVKRTDMTLQSATKGPMTALVGNEWTLRETELSPVEWLPLQAAPNPTTINEIMTEINKDIASNYTQETAKEDNYFSGKGLQKFAMLALILNKSDQTQLRNPELAQIALDKLKAAFLPYLQNEQADPFRYDTLYKGIVAKAGLPTSMGGTDDLSAEFGHSYYSDHHYHQGYFVVTAAIIHHLDPTWNADRLKAWTEALIRDVNNANDGDEYFAAFRNWDWFAGHSWAGGIKPDGALDGRDQESVPESVNFYWGAKLWGLATGNTPLTKLASLQLAVTKRTTYEYFWMLDGNKNRPENIVRNKVIGIYFEQKTDYTTYFGRFLEYIHGIQQLPMTPELMEYIRTPEFVSQEWDEKLGAIAPTVQSPWAGVLYLNYAIINPAEAYPALRKVQMDDGQTRSYSLYLTATRPHFFRRSLLAALARHGSTRRPSLPSSGDDDKHEDGFLLRFRRLNPFNLKHRIY

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};

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}.

IPR005200;IPR040720;IPR040451;

1.10.287.1170;1.20.5.420;

A0A024B7W1

MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLMWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAVKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMTICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRHGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPMLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGNRIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMVRRIIGDEEKYMDYLSTQVRYLGEEGSTPGVL

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 proteins (By similarity). Can migrate to the cell nucleus where it modulates host functions (By similarity). Inhibits the integrated stress response (ISR) in the infected cell (PubMed:28592527). {ECO:0000250|UniProtKB:P17763, ECO:0000269|PubMed:28592527}.; FUNCTION: [Capsid protein C]: Inhibits RNA silencing by interfering with host Dicer. {ECO:0000250|UniProtKB:P03314}.; FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH 6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Protein prM]: Plays a role in host immune defense modulation and protection of envelope protein E during virion synthesis. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion. Contributes to fetal microcephaly in humans. Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Small envelope protein M]: May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Envelope protein E]: Binds to host cell surface receptors and mediates fusion between viral and cellular membranes. Efficient virus attachment to cell is, at least in part, mediated by host HAVCR1 in a cell-type specific manner (By similarity). In addition, host NCAM1 can also be used as entry receptor (By similarity). Interaction with host HSPA5 plays an important role in the early stages of infection as well (By similarity). Envelope protein is synthesized in the endoplasmic reticulum and forms a heterodimer with protein prM. The heterodimer plays a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimers between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes the dissociation of PrM-E heterodimers and formation of E homodimers. PrM-E cleavage is inefficient, many virions are only partially matured and immature prM-E proteins could play a role in immune evasion (By similarity). {ECO:0000250|UniProtKB:A0A142I5B9, ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 1]: Plays a role in the inhibition of host RLR-induced interferon-beta activation by targeting TANK-binding kinase 1/TBK1. In addition, recruits the host deubiquitinase USP8 to cleave 'Lys-11'-linked polyubiquitin chains from caspase-1/CASP1 thus inhibiting its proteasomal degradation. In turn, stabilized CASP1 promotes cleavage of cGAS, which inhibits its ability to recognize mitochondrial DNA release and initiate type I interferon signaling. {ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [Non-structural protein 2A]: Component of the viral RNA replication complex that recruits genomic RNA, the structural protein prM/E complex, and the NS2B/NS3 protease complex to the virion assembly site and orchestrates virus morphogenesis (By similarity). Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (By similarity). May disrupt adherens junction formation and thereby impair proliferation of radial cells in the host cortex (By similarity). {ECO:0000250|UniProtKB:A0A142I5B9, ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [Serine protease subunit NS2B]: Required cofactor for the serine protease function of NS3. {ECO:0000250|UniProtKB:Q32ZE1}.; FUNCTION: [Serine protease NS3]: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity). Inhibits the integrated stress response (ISR) in the infected cell by blocking stress granules assembly (PubMed:28592527). Disrupts host centrosome organization in a CEP63-dependent manner to degrade host TBK1 and inhibits innate immune response (PubMed:35793002). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000269|PubMed:28592527, ECO:0000269|PubMed:35793002}.; FUNCTION: [Non-structural protein 4A]: Regulates the ATPase activity of the NS3 helicase activity (By similarity). NS4A allows NS3 helicase to conserve energy during unwinding (By similarity). Cooperatively with NS4B suppresses the Akt-mTOR pathway and leads to cellular dysregulation (PubMed:27524440). By inhibiting host ANKLE2 functions, may cause defects in brain development, such as microcephaly (PubMed:30550790). Antagonizes also the host MDA5-mediated induction of alpha/beta interferon antiviral response (By similarity). Inhibits the integrated stress response (ISR) in the infected cell by blocking stress granules assembly (PubMed:28592527). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440, ECO:0000269|PubMed:28592527, ECO:0000269|PubMed:30550790}.; FUNCTION: [Peptide 2k]: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Non-structural protein 4B]: Induces the formation of ER-derived membrane vesicles where the viral replication takes place (By similarity). Also plays a role in the inhibition of host RLR-induced interferon-beta production at TANK-binding kinase 1/TBK1 level (By similarity). Cooperatively with NS4A suppresses the Akt-mTOR pathway and leads to cellular dysregulation (PubMed:27524440). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000250|UniProtKB:Q9Q6P4, ECO:0000269|PubMed:27524440}.; FUNCTION: [RNA-directed RNA polymerase NS5]: Replicates the viral (+) and (-) RNA genome, and performs the capping of genomes in the cytoplasm (PubMed:30951555). Methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Once sufficient NS5 is expressed, binds to the cap-proximal structure and inhibits further translation of the viral genome (By similarity). Besides its role in RNA genome replication, also prevents the establishment of a cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Mechanistically, interferes with host kinases TBK1 and IKKE upstream of interferon regulatory factor 3/IRF3 to inhibit the RIG-I pathway (By similarity). Antagonizes also type I interferon signaling by targeting STAT2 for degradation by the proteasome thereby preventing activation of JAK-STAT signaling pathway (By similarity). Within the host nucleus, disrupts host SUMO1 and STAT2 co-localization with PML, resulting in PML degradation (PubMed:32699085). May also reduce immune responses by preventing the recruitment of the host PAF1 complex to interferon-responsive genes (PubMed:30550790). {ECO:0000250|UniProtKB:Q32ZE1, ECO:0000269|PubMed:30550790, ECO:0000269|PubMed:30951555, ECO:0000269|PubMed:32699085}.

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:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase NS5]: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000255|PROSITE-ProRule:PRU00924}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539, ECO:0000269|PubMed:30951555}; CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; Evidence={ECO:0000250|UniProtKB:Q32ZE1}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:Q32ZE1}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:Q9Q6P4};

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;Helicase;Host cytoplasm;Host endoplasmic reticulum;Host membrane;Host nucleus;Host-virus interaction;Hydrolase;Inhibition of host innate immune response by virus;Inhibition of host interferon signaling pathway by virus;Inhibition of host STAT1 by virus;Inhibition of host STAT2 by virus;Inhibition of host TYK2 by virus;Interferon antiviral system evasion;Iron;Iron-sulfur;Isopeptide bond;Membrane;Metal-binding;Methyltransferase;mRNA capping;mRNA processing;Nucleotide-binding;Nucleotidyltransferase;Phosphoprotein;Protease;RNA-binding;RNA-directed RNA polymerase;S-adenosyl-L-methionine;Secreted;Serine protease;Suppressor of RNA silencing;Transcription;Transcription regulation;Transferase;Transmembrane;Transmembrane helix;Ubl conjugation;Viral attachment to host cell;Viral envelope protein;Viral immunoevasion;Viral penetration into host cytoplasm;Viral RNA replication;Virion;Virus endocytosis by host;Virus entry into host cell;Zinc

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 cascade via inhibition of host TYK2 activity [GO:0039574]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]

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-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198]

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}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Non-structural protein 1]: Secreted {ECO:0000250|UniProtKB:P17763}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Lumenal side {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [Non-structural protein 2A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Serine protease NS3]: Host endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU00860}; Peripheral membrane protein {ECO:0000255|PROSITE-ProRule:PRU00860}; Cytoplasmic side {ECO:0000255|PROSITE-ProRule:PRU00860}. Note=Remains non-covalently associated to serine protease subunit NS2B. {ECO:0000255|PROSITE-ProRule:PRU00860}.; SUBCELLULAR LOCATION: [Non-structural protein 4A]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-associated vesicles hosting the replication complex. {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P17763}. Note=Located in RE-derived vesicles hosting the replication complex. {ECO:0000250|UniProtKB:Q9Q6P4}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase NS5]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q32ZE1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q32ZE1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q32ZE1}. Host nucleus {ECO:0000269|PubMed:32699085}. Note=Located in RE-associated vesicles hosting the replication complex. NS5 protein is mainly localized in the nucleus rather than in ER vesicles. {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-mediated cleavage at the 4A-2K site. {ECO:0000250|UniProtKB:P17763}.; PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.; PTM: [Envelope protein E]: N-glycosylation plays a role in virulence in mammalian and mosquito hosts, but may have no effect on neurovirulence. {ECO:0000269|PubMed:29091758}.; PTM: [Envelope protein E]: Ubiquitination by host TRIM7 promotes virus attachment and fusion of the virus and the host endosome membrane. {ECO:0000250|UniProtKB:A0A142I5B9}.; PTM: [Non-structural protein 1]: N-glycosylated. The excreted form is glycosylated, which is required for efficient secretion of the protein from infected cells. {ECO:0000250|UniProtKB:P17763}.; PTM: [Non-structural protein 1]: Ubiquitination by host TRIM22 leads to proteasomal degradation. {ECO:0000269|PubMed:36042495}.; PTM: [Serine protease NS3]: Ubiquitination by host TRIM22 leads to proteasomal degradation. {ECO:0000269|PubMed:36042495}.; PTM: [Serine protease NS3]: Acetylated by host KAT5. Acetylation modulates NS3 RNA-binding and unwinding activities and plays an important positive role for viral replication. {ECO:0000250|UniProtKB:Q32ZE1}.; PTM: [RNA-directed RNA polymerase NS5]: Phosphorylated on serines residues. This phosphorylation may trigger NS5 nuclear localization. {ECO:0000250|UniProtKB:P17763}.; PTM: [RNA-directed RNA polymerase NS5]: Sumoylated, required for regulating IFN induced interferon stimulated genes/ISGs. {ECO:0000269|PubMed:32699085}.

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 disordered region at the N-terminus may be involved in lipid-droplet binding. {ECO:0000250|UniProtKB:P12823}.; DOMAIN: [Serine protease subunit NS2B]: The central disordered region transitions to ordered by binding to NS3. {ECO:0000250|UniProtKB:Q32ZE1}.; DOMAIN: [RNA-directed RNA polymerase NS5]: Comprises a methyltransferase (MTase) in the N-terminal region and an RNA-dependent RNA polymerase in the C-terminal region. {ECO:0000250|UniProtKB:Q32ZE1}.

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;IPR027417;IPR009003;IPR007094;IPR002877;IPR029063;

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

MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI

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.-

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 development [GO:0021549]; cerebral cortex cell migration [GO:0021795]; choline transport [GO:0015871]; DNA damage response [GO:0006974]; dorsal/ventral neural tube patterning [GO:0021904]; embryonic limb morphogenesis [GO:0030326]; epithelial cell proliferation [GO:0050673]; heart looping [GO:0001947]; hematopoietic progenitor cell differentiation [GO:0002244]; intracellular signal transduction [GO:0035556]; L-glutamate import across plasma membrane [GO:0098712]; locomotion [GO:0040011]; membrane protein ectodomain proteolysis [GO:0006509]; memory [GO:0007613]; mitochondrial transport [GO:0006839]; myeloid dendritic cell differentiation [GO:0043011]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of axonogenesis [GO:0050771]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of ubiquitin-dependent protein catabolic process [GO:2000059]; neural retina development [GO:0003407]; neuron apoptotic process [GO:0051402]; neuron cellular homeostasis [GO:0070050]; neuron development [GO:0048666]; neuron migration [GO:0001764]; Notch receptor processing [GO:0007220]; Notch signaling pathway [GO:0007219]; positive regulation of apoptotic process [GO:0043065]; positive regulation of coagulation [GO:0050820]; positive regulation of L-glutamate import across plasma membrane [GO:0002038]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of receptor recycling [GO:0001921]; post-embryonic development [GO:0009791]; protein catabolic process at postsynapse [GO:0140249]; protein glycosylation [GO:0006486]; protein processing [GO:0016485]; protein transport [GO:0015031]; regulation of canonical Wnt signaling pathway [GO:0060828]; regulation of postsynapse organization [GO:0099175]; regulation of resting membrane potential [GO:0060075]; regulation of synaptic plasticity [GO:0048167]; regulation of synaptic transmission, glutamatergic [GO:0051966]; regulation of synaptic vesicle cycle [GO:0098693]; response to oxidative stress [GO:0006979]; sequestering of calcium ion [GO:0051208]; skeletal system morphogenesis [GO:0048705]; skin morphogenesis [GO:0043589]; smooth endoplasmic reticulum calcium ion homeostasis [GO:0051563]; somitogenesis [GO:0001756]; synaptic vesicle targeting [GO:0016080]; T cell activation involved in immune response [GO:0002286]; T cell receptor signaling pathway [GO:0050852]; thymus development [GO:0048538]

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:0005794]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; lysosomal membrane [GO:0005765]; mitochondrial inner membrane [GO:0005743]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; postsynapse [GO:0098794]; presynaptic membrane [GO:0042734]; sarcolemma [GO:0042383]; smooth endoplasmic reticulum [GO:0005790]; synaptic vesicle [GO:0008021]

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}. Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Endosome membrane {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004337}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Synapse {ECO:0000256|ARBA:ARBA00034103}.

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};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-7. {ECO:0000269|PubMed:25219509};

3D-structure;Disulfide bond;Hydrolase;Secreted;Serine esterase;Signal

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

MYWQLVRILVLFDCLQKILAIEHDSICIADVDDACPEPSHTVMRLRERNDKKAHLIAKQHGLEIRGQPFLDGKSYFVTHISKQRSRRRKREIISRLQEHPDILSIEEQRPRVRRKRDFLYPDIAHELAGSSTNIRHTGLISNTEPRIDFIQHDAPVLPFPDPLYKEQWYLNNGAQGGFDMNVQAAWLLGYAGRNISVSILDDGIQRDHPDLAANYDPLASTDINGHDDDPTPQDDGDNKHGTRCAGEVASIAGNVYCGVGVAFHAKIGGVRMLDGPVSDSVEAASLSLNRHHIDIYSASWGPEDDGRTFDGPGPLAREAFYRGVKAGRGGKGSIFVWASGNGGSRQDSCSADGYTTSVYTLSVSSATIDNRSPWYLEECPSTIATTYSSANMNQPAIITVDVPHGCTRSHTGTSASAPLAAGIIALALEANPNLTWRDMQHIVLRTANPVPLLNNPGWSVNGVGRRINNKFGYGLMDAGALVKLALIWKTVPEQHICTYDYKLEKPNPRPITGNFQMNFSLEVNGCESGTPVLYLEHVQVLATFRFGKRGDLKLTLFSPRGTSSVLLPPRPQDFNSNGIHKWPFLSVQTWGEDPRGKWTLMVESVSTNRNVGGTFHDWSLLLYGTAEPAQPNDPRHSSVVPSSVSAESPFDRITQHIASQEKKKKQRDSRDWQPKKVENKKSLLVSAQPELRV

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|PubMed:12855702};

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12855702}; Note=Binds 3 calcium ions per subunit. {ECO:0000250|UniProtKB:P09958};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Active from pH 7.0 to 8.5. {ECO:0000269|PubMed:12855702};

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 second cleavage within the inhibition propeptide results in propeptide dissociation and bli activation. {ECO:0000269|PubMed:12855702}.

IPR008979;IPR034182;IPR002884;IPR000209;IPR036852;IPR023827;IPR022398;IPR023828;IPR015500;IPR032815;IPR038466;

2.60.120.260;3.30.70.850;3.40.50.200;

A0A059AF78

MESCNCVEPQWPADELLMKYQYLSDFFIALAYFSIPLELIYFVKKSAVFPYRWVLVQFGAFIVLCGATHLINLWTFAIHSRTVAYVMTIAKVLTAAVSCITALMLVHIIPDLLSVKTRELFLKNKAAELDREMGLIRTQEETGRHCALWMPTRSGLELQLSYTLRQQQNPVGYTVPIHLPVINRVFSSNRALKISPNSPVARIRPLAGKYIPGEVVAVRVPLLHLSNFQINDWPELSTKRYALMVLMLPSDSARQWHVHELELVEVVADQVAVALSHAAILEESMRARDLLMEQNVALDLARREAETAIRARNDFLAVMNHEMRTPMHAIIALSSLLQETELTPEQRLMVETIMKSSNLLATLINDVLDLSRLEDGSFQLNIATFNLHAVFREVLNLIKPVASVKKLLITLNLAPDLPEYAVGDEKRLMQVILNVVGNAVKFSKEGGISITAFVAKAEYLREARPPEFIPVPSDNHFYLRVQVRDSGSGINPQDIPKLFTKFAHNQSLATRNSGGSGLGLAICKRFVTLMDGHIWIESEGIGKGCTATFIVGLGIPEKLNESKFPVLPRGSSNHVLANFSGLKVLVMDDNGVGRAATKGLLLHLGCDVTTVSSGDELLHAVSQEHKVVLMDICTPGIDSYEVAVQIHRLYSQHHERPLLVAITGSTDKVTKENCMRVGMDGVIQKPVSLDKMRNVLSELLECGHQMSSLARV

Eucalyptus grandis (Flooded gum)

2.7.13.3

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};

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 signaling pathway [GO:0010105]; phloem or xylem histogenesis [GO:0010087]; regulation of seedling development [GO:1900140]; regulation of stomatal movement [GO:0010119]; response to abscisic acid [GO:0009737]; response to auxin [GO:0009733]; response to gibberellin [GO:0009739]; response to heat [GO:0009408]; response to insect [GO:0009625]; response to molecule of bacterial origin [GO:0002237]; response to salt stress [GO:0009651]; seed dormancy process [GO:0010162]

endoplasmic reticulum [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}.

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

MRSVSGQVVCVTGAGGFIASWLVKILLEKGYTVRGTVRNPDDPKNGHLRELEGAKERLTLCKADLLDYQSLREAINGCDGVFHTASPVTDDPEQMVEPAVIGTKNVINAAAEANVRRVVFTSSIGAVYMDPNRDPETVVDETCWSDPDFCKNTKNWYCYGKMVAEQAAWEEAKEKGVDLVVINPVLVQGPLLQTTVNASVLHILKYLTGSAKTYANSVQAYVDVKDVALAHILLYETPEASGRYLCAESVLHRGDVVEILSKFFPEYPIPTKCSDVTKPRVKPYKFSNQKLKDLGLEFTPVKQCLYETVKSLQEKGHLPIPTQKDEPIIRIQP

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:24985707, PubMed:25217505). Also active toward p-coumaroyl-CoA and sinapoyl-CoA (PubMed:24985707, PubMed:25217505). Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (PubMed:24985707). {ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}.

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}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64650; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumaraldehyde + CoA + NADP(+) = (E)-4-coumaroyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64652, ChEBI:CHEBI:15378, ChEBI:CHEBI:28353, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85008; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64654; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; CATALYTIC ACTIVITY: Reaction=(E)-sinapaldehyde + CoA + NADP(+) = (E)-sinapoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64656, ChEBI:CHEBI:15378, ChEBI:CHEBI:27949, ChEBI:CHEBI:57287, ChEBI:CHEBI:57393, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64658; Evidence={ECO:0000269|PubMed:24985707, ECO:0000269|PubMed:25217505}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamaldehyde + CoA + NADP(+) = (E)-cinnamoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:10620, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731, ChEBI:CHEBI:57252, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.44; Evidence={ECO:0000250|UniProtKB:Q9S9N9}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10622; Evidence={ECO:0000250|UniProtKB:Q9S9N9};

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:25217505}; Vmax=5713 nmol/sec/mg enzyme with feruloyl-CoA as substrate {ECO:0000269|PubMed:25217505}; Vmax=3384.7 nmol/sec/mg enzyme with sinapoyl-CoA as substrate {ECO:0000269|PubMed:25217505}; Note=kcat is 1.2 sec(-1) with p-coumaroyl-CoA as substrate (PubMed:25217505). kcat is 5.8 sec(-1) with feruloyl-CoA as substrate (PubMed:25217505). kcat is 3.4 sec(-1) with sinapoyl-CoA as substrate (PubMed:25217505). {ECO:0000269|PubMed:25217505};

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};

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}.

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 acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate to the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000256|HAMAP-Rule:MF_03205}.

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-to-right; Xref=Rhea:RHEA:39680; Evidence={ECO:0000256|ARBA:ARBA00001296}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H(+) + malonyl-CoA = (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36475, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57384, ChEBI:CHEBI:73852; Evidence={ECO:0000256|ARBA:ARBA00000904}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476; Evidence={ECO:0000256|ARBA:ARBA00000904}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA = (8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35379, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57363, ChEBI:CHEBI:57384, ChEBI:CHEBI:71481; Evidence={ECO:0000256|ARBA:ARBA00000735}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35380; Evidence={ECO:0000256|ARBA:ARBA00000735}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + H(+) + malonyl-CoA = (8Z,11Z,14Z,17Z)-3-oxoicosatetraenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35391, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:71489, ChEBI:CHEBI:71491; Evidence={ECO:0000256|ARBA:ARBA00000337}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35392; Evidence={ECO:0000256|ARBA:ARBA00000337}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(11Z)-octadecenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39675, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:61540, ChEBI:CHEBI:76555; Evidence={ECO:0000256|ARBA:ARBA00001297}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39676; Evidence={ECO:0000256|ARBA:ARBA00001297}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = (11Z)-3-oxoicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36511, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:57387, ChEBI:CHEBI:74011; Evidence={ECO:0000256|ARBA:ARBA00001347}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512; Evidence={ECO:0000256|ARBA:ARBA00001347}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z)-3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36503, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:57384, ChEBI:CHEBI:74012; Evidence={ECO:0000256|ARBA:ARBA00000592}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504; Evidence={ECO:0000256|ARBA:ARBA00000592}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36523, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:74034, ChEBI:CHEBI:74054; Evidence={ECO:0000256|ARBA:ARBA00001158}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524; Evidence={ECO:0000256|ARBA:ARBA00001158}; CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000256|HAMAP-Rule:MF_03205, ECO:0000256|RuleBase:RU361115};

PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03205}.

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:0030148]; unsaturated fatty acid biosynthetic process [GO:0006636]; very long-chain fatty acid biosynthetic process [GO:0042761]

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=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. {ECO:0000256|HAMAP-Rule:MF_03205}.

IPR002076;IPR033677;

A0A060XQE7

MEEIVVAGISGRLPESNNLEEFWENLFNGVDMVTEDDRRWKPGLYGLPKRNGKLKDISRFDAAFFGVHPKQAHTMDPQLRLMLEIAYEAIVDGGLNPTELRGSRTGVYIGVSGSEAGEAFSRDPEELLGYSMTGCQRAMFANRLSYFFDFNGPSTAIDTACSSSLLALENAFNAIRHGHCDAALVGGVNLLLKPNTSVQFMKLGMLSPEGTCKSFDSSGNGYCRSEAAVAVLLTRRSMAKRVYATVLNAGNNTDGYKEQGVTFPSGEMQQRLVRSLYQEVNITPDQVEYIEAHGTGTKVGDPQEVNGIVSVFCHSKRDPLLIGSTKSNMGHPEPASGLAALAKVVLSLERGVWAPNIHYNSPNTDIPALSDGRLRVVNEPIPVRGGIVGINSFGFGGSNVHVILRPPGFNTPKSFKVPPNTPSVSSQVPRLLQACGRTEEAVSALLSKGKEHSGDDNFLCLLNDVSGVPTAGMPYRGYTLIGSQDDVTEVQKTEATPRPLWYICSGMGTQWGGMGRSLMQLPEFRESILRSDIALKDTGMCVSSLLMEADESTFEDTVQAFVGLAAIQIAQIDLLQKLGLQPDGIVGHSVGELACGYADGSLSHSEAILAAYWRGRSIKEANLPPGGMAAVGLTWAECKAQCPQGVVPACHNAEDTVTISGPAEAVSKFVSELKESGVFAKEVRSAGVAFHSYYMASIAPALLAALKRVIKEPKQRSARWISTSIPQKDWDSPLALYSSADYHCNNLVSPVLFQEGLSLVPDNAVVVEIAPHALLQAILKRSLKPTCSILPLMRRGHANNLEFFLSHIGKVYMNGINVDSKQLYPCVEYPVPAGTPLISPLVQWDHTQTWDVPKAEDFPAGSGGSTSATIYNIDMNPESPDYYMIGHCIDGRVLYPATGYLVLAWRTLMRSLGVVMETTPVTFEDVTIHRATILPKTGSVQLEVRLMPATSRFEVSENGNLAVSGKVSILEDAALDAFHSEIGKPVTGDDGDPNLRLTAHDIYKELRLRGYDYGKTFQGILESNNAGDSGKLQWTGNWVTFLDTMLQMIVVGLSGRSLRLPTRIRSVCVDPTVHQERVTEYGEAKKAVVVHVNRCLDNIVAGGVQICGLHATVAPRRQQQQSPPTLEEFLFVPYLETECLSANEKLGNQLKNCKGLIHKLQKKLAPQGVKLSIPGLGGVSGPAVPSPESAEPGLLRLLSLLCGLELNGNLRSELEQTVEKERGCLLQDPLLHGLLDGPALRHCLDTALENTTPGKIKVLEALSNDGHLFSRAVPLLNIQPMLRLDYVATAATLDLLTPHQTTLDAMGVTSAQWDPQQGPVPGGAVGGADLVVCNHAWGPLGAGAEVVVGNLASGAKEGGFVMLHTLLKGETLGEMVAFLTSKDSQNNQQRLLSQTEWEKAFSDASLNLVAVRKSFYGSALFLCRRRLPSKLPIFLPVDSLDYQWVETLKTTLAEPSDSPVWLTATQGHSGVVGMVNCLRQEPGGSRIRCAFVSNLCESSAVPTLQPAHNSMRSVLEGDLCMNVFRDGHWGVFRHQLISQDLSEELTEQAYVNVLTRGDLSSLRWIASPLRHFVASSPHVQLCRVYYSSLNFRDIMLATGKLPPDAIPGDLALQQCMLGMEFSGRDPSGRRVMGLLPAKGLATCVDADTRFLWDIPDGWTLEQAASVPVVYATAYYSLVVRGRLRPGESVLIHSGSGGVGQAAISIALSQRCRVFTTVGSAEKRAYLQERFPQLTSESFANSRDATFEQHVLLHTQGKGVDMVLNSLAEEKLQASLRCLARHGRFLEIGKYDLSNNSPLGMALFLKNVAFHGILLDALFEEGNREWEEVSQLLKGGIVGGVVKPLRTTVFERDQVEEAFRYMAQGKHIGKVLLQVRSEEKGGGTQAVGSPLSLPAICRTFCPASHSYIITGGLGGFGLELAHWLTERGARKLVLTSRSGIRNGYQAKRVREWQGMGVQVLVSTSDVSTLEGAERLINEACRLGPVGGVFHLAMVLKDGMLENLTPQLFLDVNKPKYNGTLHLDRVTRKLCPDLSYFVAFSSVSCGRGNAGQSNYGYANSAMERVCEQRRHDGLPGLAVQWGAIGDVGVVLETMGGNDVVVGGTLPQRITSCLEVLDRFLCERRPVMSSFVLAERSVVKSEGTGQRDLVEAVAHILGVRDVSSLNADASLADLGLDSLMGVEVRQTLERDYDIVMAMREIRQLTINKLRELSSQPAGTAESCQSPVKKGGVRSLLESDLSLMLVNPDGPTVSRLNEVQSAERPLFLVHPIEGSIAAFHTLTAKLSVPCYGLQCTKAAPLDSIQSLATYYVECIRQVQSEGPYRIAGYSFGACVAFEMCSQLQAQGRTVDYLFLFDGSHSYVAAYTQSYKSKLTPGKESEAETEALCAFIQQFTGIEYNKLLETLLPLSDLKARVNMAVDLITSSHKNVSKESLRFAAATFYYKLKAADGYVPATKYHGNVTLLRAKASSDYGDNLGADYKLSEVCDGKVSVHVIEGDHRSFLEGEGVESISSIIHSSLAEPRVTAREG

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'-phosphopantetheine of the acyl carrier protein ([ACP]) domain. {ECO:0000256|ARBA:ARBA00023442}.

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-to-right; Xref=Rhea:RHEA:41813; Evidence={ECO:0000256|ARBA:ARBA00023357}; CATALYTIC ACTIVITY: Reaction=(2E)-decenoyl-[ACP] + H(+) + NADPH = decanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41864, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78467, ChEBI:CHEBI:78468; Evidence={ECO:0000256|ARBA:ARBA00023387}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41865; Evidence={ECO:0000256|ARBA:ARBA00023387}; CATALYTIC ACTIVITY: Reaction=(2E)-dodecenoyl-[ACP] + H(+) + NADPH = dodecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41880, Rhea:RHEA-COMP:9643, Rhea:RHEA-COMP:9644, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65264, ChEBI:CHEBI:78472; Evidence={ECO:0000256|ARBA:ARBA00023385}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41881; Evidence={ECO:0000256|ARBA:ARBA00023385}; CATALYTIC ACTIVITY: Reaction=(2E)-hexadecenoyl-[ACP] + H(+) + NADPH = hexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41912, Rhea:RHEA-COMP:9651, Rhea:RHEA-COMP:9652, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78481, ChEBI:CHEBI:78483; Evidence={ECO:0000256|ARBA:ARBA00023345}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41913; Evidence={ECO:0000256|ARBA:ARBA00023345}; CATALYTIC ACTIVITY: Reaction=(2E)-hexenoyl-[ACP] + H(+) + NADPH = hexanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41832, Rhea:RHEA-COMP:9631, Rhea:RHEA-COMP:9632, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78458, ChEBI:CHEBI:78459; Evidence={ECO:0000256|ARBA:ARBA00023359}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41833; Evidence={ECO:0000256|ARBA:ARBA00023359}; CATALYTIC ACTIVITY: Reaction=(2E)-octadecenoyl-[ACP] + H(+) + NADPH = NADP(+) + octadecanoyl-[ACP]; Xref=Rhea:RHEA:41928, Rhea:RHEA-COMP:9655, Rhea:RHEA-COMP:9656, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78489, ChEBI:CHEBI:78495; Evidence={ECO:0000256|ARBA:ARBA00023376}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41929; Evidence={ECO:0000256|ARBA:ARBA00023376}; CATALYTIC ACTIVITY: Reaction=(2E)-octenoyl-[ACP] + H(+) + NADPH = NADP(+) + octanoyl-[ACP]; Xref=Rhea:RHEA:41848, Rhea:RHEA-COMP:9635, Rhea:RHEA-COMP:9636, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78462, ChEBI:CHEBI:78463; Evidence={ECO:0000256|ARBA:ARBA00023420}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41849; Evidence={ECO:0000256|ARBA:ARBA00023420}; CATALYTIC ACTIVITY: Reaction=(2E)-tetradecenoyl-[ACP] + H(+) + NADPH = NADP(+) + tetradecanoyl-[ACP]; Xref=Rhea:RHEA:41896, Rhea:RHEA-COMP:9647, Rhea:RHEA-COMP:9648, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78475, ChEBI:CHEBI:78477; Evidence={ECO:0000256|ARBA:ARBA00023368}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41897; Evidence={ECO:0000256|ARBA:ARBA00023368}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41808, Rhea:RHEA-COMP:9626, Rhea:RHEA-COMP:9627, ChEBI:CHEBI:15377, ChEBI:CHEBI:78451, ChEBI:CHEBI:78453; Evidence={ECO:0000256|ARBA:ARBA00023402}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41809; Evidence={ECO:0000256|ARBA:ARBA00023402}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639, ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467; Evidence={ECO:0000256|ARBA:ARBA00023388}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861; Evidence={ECO:0000256|ARBA:ARBA00023388}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41876, Rhea:RHEA-COMP:9642, Rhea:RHEA-COMP:9643, ChEBI:CHEBI:15377, ChEBI:CHEBI:78470, ChEBI:CHEBI:78472; Evidence={ECO:0000256|ARBA:ARBA00023351}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41877; Evidence={ECO:0000256|ARBA:ARBA00023351}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41908, Rhea:RHEA-COMP:9650, Rhea:RHEA-COMP:9651, ChEBI:CHEBI:15377, ChEBI:CHEBI:78480, ChEBI:CHEBI:78481; Evidence={ECO:0000256|ARBA:ARBA00023401}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41909; Evidence={ECO:0000256|ARBA:ARBA00023401}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41828, Rhea:RHEA-COMP:9630, Rhea:RHEA-COMP:9631, ChEBI:CHEBI:15377, ChEBI:CHEBI:78457, ChEBI:CHEBI:78458; Evidence={ECO:0000256|ARBA:ARBA00023373}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829; Evidence={ECO:0000256|ARBA:ARBA00023373}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyoctadecanoyl-[ACP] = (2E)-octadecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41924, Rhea:RHEA-COMP:9654, Rhea:RHEA-COMP:9655, ChEBI:CHEBI:15377, ChEBI:CHEBI:78488, ChEBI:CHEBI:78489; Evidence={ECO:0000256|ARBA:ARBA00023399}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41925; Evidence={ECO:0000256|ARBA:ARBA00023399}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41844, Rhea:RHEA-COMP:9634, Rhea:RHEA-COMP:9635, ChEBI:CHEBI:15377, ChEBI:CHEBI:78461, ChEBI:CHEBI:78462; Evidence={ECO:0000256|ARBA:ARBA00023332}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41845; Evidence={ECO:0000256|ARBA:ARBA00023332}; CATALYTIC ACTIVITY: Reaction=(3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] + H2O; Xref=Rhea:RHEA:41892, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9647, ChEBI:CHEBI:15377, ChEBI:CHEBI:78474, ChEBI:CHEBI:78475; Evidence={ECO:0000256|ARBA:ARBA00023398}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41893; Evidence={ECO:0000256|ARBA:ARBA00023398}; CATALYTIC ACTIVITY: Reaction=3-oxobutanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxybutanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41804, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9626, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78450, ChEBI:CHEBI:78451; Evidence={ECO:0000256|ARBA:ARBA00023413}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41805; Evidence={ECO:0000256|ARBA:ARBA00023413}; CATALYTIC ACTIVITY: Reaction=3-oxodecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41856, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9638, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78464, ChEBI:CHEBI:78466; Evidence={ECO:0000256|ARBA:ARBA00023418}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41857; Evidence={ECO:0000256|ARBA:ARBA00023418}; CATALYTIC ACTIVITY: Reaction=3-oxododecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydodecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41872, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9642, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78469, ChEBI:CHEBI:78470; Evidence={ECO:0000256|ARBA:ARBA00023416}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41873; Evidence={ECO:0000256|ARBA:ARBA00023416}; CATALYTIC ACTIVITY: Reaction=3-oxohexadecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyhexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41904, Rhea:RHEA-COMP:9649, Rhea:RHEA-COMP:9650, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78478, ChEBI:CHEBI:78480; Evidence={ECO:0000256|ARBA:ARBA00023390}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41905; Evidence={ECO:0000256|ARBA:ARBA00023390}; CATALYTIC ACTIVITY: Reaction=3-oxohexanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyhexanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41824, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9630, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78456, ChEBI:CHEBI:78457; Evidence={ECO:0000256|ARBA:ARBA00023346}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41825; Evidence={ECO:0000256|ARBA:ARBA00023346}; CATALYTIC ACTIVITY: Reaction=3-oxooctadecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyoctadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41920, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9654, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78487, ChEBI:CHEBI:78488; Evidence={ECO:0000256|ARBA:ARBA00023419}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41921; Evidence={ECO:0000256|ARBA:ARBA00023419}; CATALYTIC ACTIVITY: Reaction=3-oxooctanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyoctanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41840, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9634, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78460, ChEBI:CHEBI:78461; Evidence={ECO:0000256|ARBA:ARBA00023364}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41841; Evidence={ECO:0000256|ARBA:ARBA00023364}; CATALYTIC ACTIVITY: Reaction=3-oxotetradecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxytetradecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41888, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9646, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78473, ChEBI:CHEBI:78474; Evidence={ECO:0000256|ARBA:ARBA00023367}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41889; Evidence={ECO:0000256|ARBA:ARBA00023367}; CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-[ACP] + malonyl-[ACP] = 3-oxooctadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41916, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78483, ChEBI:CHEBI:78487; Evidence={ECO:0000256|ARBA:ARBA00023365}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41917; Evidence={ECO:0000256|ARBA:ARBA00023365}; CATALYTIC ACTIVITY: Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460; Evidence={ECO:0000256|ARBA:ARBA00023361}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837; Evidence={ECO:0000256|ARBA:ARBA00023361}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464; Evidence={ECO:0000256|ARBA:ARBA00023414}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853; Evidence={ECO:0000256|ARBA:ARBA00023414}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477, ChEBI:CHEBI:78478; Evidence={ECO:0000256|ARBA:ARBA00023341}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901; Evidence={ECO:0000256|ARBA:ARBA00023341}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-[ACP] = H(+) + hexadecanoate + holo-[ACP]; Xref=Rhea:RHEA:41932, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:78483; EC=3.1.2.14; Evidence={ECO:0000256|ARBA:ARBA00023378}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41933; Evidence={ECO:0000256|ARBA:ARBA00023378}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-[ACP] = H(+) + holo-[ACP] + tetradecanoate; Xref=Rhea:RHEA:30123, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:64479, ChEBI:CHEBI:78477; EC=3.1.2.14; Evidence={ECO:0000256|ARBA:ARBA00023410}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30124; Evidence={ECO:0000256|ARBA:ARBA00023410}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100; Evidence={ECO:0000256|ARBA:ARBA00023333}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399; Evidence={ECO:0000256|ARBA:ARBA00023333}; CATALYTIC ACTIVITY: Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O; Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59; Evidence={ECO:0000256|ARBA:ARBA00023394}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13098; Evidence={ECO:0000256|ARBA:ARBA00023394}; CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] + H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.39; Evidence={ECO:0000256|ARBA:ARBA00023381}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22566; Evidence={ECO:0000256|ARBA:ARBA00023381}; CATALYTIC ACTIVITY: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; EC=2.3.1.41; Evidence={ECO:0000256|ARBA:ARBA00023389}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837; Evidence={ECO:0000256|ARBA:ARBA00023389}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + n CO2 + (n+1) CoA + 2n NADP(+); Xref=Rhea:RHEA:14993, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57560, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=2.3.1.85; Evidence={ECO:0000256|ARBA:ARBA00023370}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14994; Evidence={ECO:0000256|ARBA:ARBA00023370}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA; Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446; EC=2.3.1.38; Evidence={ECO:0000256|ARBA:ARBA00023397}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41789; Evidence={ECO:0000256|ARBA:ARBA00023397}; CATALYTIC ACTIVITY: Reaction=acetyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41800, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78446, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; Evidence={ECO:0000256|ARBA:ARBA00023352}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41801; Evidence={ECO:0000256|ARBA:ARBA00023352}; CATALYTIC ACTIVITY: Reaction=butanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456; Evidence={ECO:0000256|ARBA:ARBA00023403}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821; Evidence={ECO:0000256|ARBA:ARBA00023403}; CATALYTIC ACTIVITY: Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469; Evidence={ECO:0000256|ARBA:ARBA00023396}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869; Evidence={ECO:0000256|ARBA:ARBA00023396}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473; Evidence={ECO:0000256|ARBA:ARBA00023348}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885; Evidence={ECO:0000256|ARBA:ARBA00023348}; CATALYTIC ACTIVITY: Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP]; Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449; EC=2.3.1.39; Evidence={ECO:0000256|ARBA:ARBA00023404}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793; Evidence={ECO:0000256|ARBA:ARBA00023404};

PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|ARBA:ARBA00005194}.

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-malonyltransferase activity [GO:0004314]; enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity [GO:0047117]; fatty acid synthase activity [GO:0004312]; fatty acyl-[ACP] hydrolase activity [GO:0016297]; phosphopantetheine binding [GO:0031177]

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

MLTPRDENNEGDAMPMLKKPRYSSLSGQSTNITYQEHTISREERAAAVGRHEGFRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESENVKFIEVHVSTTLEVCEQRDPKPSELYKKARAGQILGFTGIDSAYEPPENAEIILDAGKDGVQQCVQKVLDHLESKGLLPEQIPDVPAVRELFVSDDLTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDLKHKVAFVGEKSDDKEDSWPMMDDINQSIPIVLPISDDVKKGLEGVTRIALKYNGQVYAILSDPEIFEHRKDERVCRQFGTNDPRHPAVAQVLESGNWLLGGDVAVVQKIQFNDGLDKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMRDTREKLLAEHKNPILLLHPLGGWTKDDDVPLDIRIKQHEAVIAERVLDPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAGIQKPGSPDALYETTHGAKVLSMAPGLSALHILPFRVAAYDKTAKKMSFFDTSRKEDFENISGTKMRGLARNGDTPPEGFMAPTAWEVLAGYYKSLQNSN

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 from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase) (PubMed:16497669). Required for normal growth and development (PubMed:16497669). Involved in several aspects of both embryonic and postembryonic development, including molting, changes in cell shape, and patterning of epithelial and muscle cells (PubMed:16497669). {ECO:0000269|PubMed:16497669}.

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 + 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; Evidence={ECO:0000269|PubMed:16497669};

PATHWAY: Sulfur metabolism; sulfate assimilation. {ECO:0000303|PubMed:16497669}.

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}.

IPR002891;IPR025980;IPR027417;IPR015947;IPR014729;IPR024951;IPR002650;

3.40.50.620;3.40.50.300;3.10.400.10;

A0A061I403

MPMASVIAVAEPKWISVWGRFLWLTLLSMALGSLLALLLPLGAVEEQCLAVLRSFHLLRSKLDRTQHVVTKCTSPSTELSVTSGDVGLLTVKTKTSPAGKLEAKAALNQALEMKRQGKREKAHKLFLHALKMDPGFVDALNEFGIFSEEEKDIIQADYLYTRALTISPFHEKALVNRDRTLPLVEEIDQRYFSIIDSKVKKVMSIPKGSSALRRVMEETYYHHIYHTVAIEGNTLTLSEIRHILETRYAVPGKSLEEQNEVIGMHAAMKYINTTLVSRIGSVTIDDMLEIHRRVLGYVDPVEAGRFRRTQVLVGHHIPPHPRDVEKQMQEFTQWLNSEDAMNLHPVEFAALAHYKLVYIHPFIDGNGRTSRLLMNLILMQAGYPPITILKEQRSEYYHVLEVANEGDVRPFIRFIAKCTEVTLDTLLLATTEYSVALPEAQPNHSGLKETLPVRP

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 opposing activities (AMPylase or de-AMPylase) will take place (PubMed:27918543). Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP (PubMed:27918543). In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (PubMed:26673894, PubMed:27918543, PubMed:29064368). In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (PubMed:27918543). Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates (By similarity). {ECO:0000250|UniProtKB:Q9BVA6, ECO:0000269|PubMed:26673894, ECO:0000269|PubMed:27918543, ECO:0000269|PubMed:29064368}.

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 ACTIVITY: Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:27918543}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108; Evidence={ECO:0000269|PubMed:26673894, ECO:0000269|PubMed:27918543, ECO:0000269|PubMed:29064368};

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};

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

MESKALLLVALGVWLQSLTASQGGVAAADGGRDFTDIESKFALRTPDDTAEDNCHLIPGIAESVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNVGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESDKQLNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWKSDSYFSWSDWWSSPGFVIEKIRVKAGETQKKVIFCAREKVSHLQKGKDSAVFVKCHDKSLKKSGWEKSQGTYWRVSE

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 lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans. {ECO:0000256|RuleBase:RU362020}.

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-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000256|ARBA:ARBA00000652}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000256|ARBA:ARBA00001601}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000256|ARBA:ARBA00001601}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083; Evidence={ECO:0000256|ARBA:ARBA00001885}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700; Evidence={ECO:0000256|ARBA:ARBA00001885}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999; Evidence={ECO:0000256|ARBA:ARBA00000879}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385; Evidence={ECO:0000256|ARBA:ARBA00000879}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000256|ARBA:ARBA00000111}; 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:0000256|ARBA:ARBA00000137, ECO:0000256|RuleBase:RU362020};

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|RuleBase:RU362020}. Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells. Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles. {ECO:0000256|RuleBase:RU362020}.

PTM: Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity. {ECO:0000256|RuleBase:RU362020}.

IPR029058;IPR013818;IPR016272;IPR033906;IPR002330;IPR001024;IPR036392;IPR000734;

3.40.50.1820;2.60.60.20;

A0A067XGX8

MALTATATTRGGSALPNSCLQTPKFQSLQKPTFISSFPTNKKTKPRTKHISAVQSPPSTTKWNLESWKTKPAFQLPDYPDKVELESVLKTLSTYPPIVFAGEARNLEEKLGEAALGNAFLLQGGDCAESFKEFSANNIRDTFRVMLQMGVVLMFGGQMPVIKVGRMAGQFAKPRSDPFEEKDGVKLPSYRGDNVNGDAFDEKSRIPDPHRMVRAYTQSVATLNLLRAFASGGYAAMQRVNQWNLDFTDQSEQGDRYRELAHRVDEAMGFMTAAGLTVDHTIMTTTDFWTSHECLLLPYEQALTREDSTSGLYYDCSAHMIWVGERTRQLDGAHVEFLRGIANPLGIKVSHKMDPDELVKLIDILNPQNKPGRITVITRMGADNMRVKLPHLIRAVRGAGQIVTWVSDPMHGNTTKAPCGLKTRSFDSIRAELRAFFDVHEQEGSYPGGVHLEMTGQNVTECVGGSRTITYNDLSSRYHTHCDPRLNASQALELAFAIAERLRRRRLGPKFSL

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:0000250|UniProtKB:O53512, ECO:0000269|PubMed:24815009}.

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};

PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000250|UniProtKB:O53512}.

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}.

IPR013785;IPR002480;

3.20.20.70;

A0A067XH53

MALSTNSTTSSLLPKTPLVQQPLLKNASLPTTTKAIRFIQPISAIHSSDSSKNTPIVSAKPSSPPAATSTAAATAVTKQEWSIDSWKTKKALQLPEYPNQEELKNVLKTIEDFPPIVFAGEARHLEEKLGEAAMGRAFLLQGGDCAESFKEFNANNIRDTFRILLQMGAVLMFGGQMPVIKVGRMAGQFAKPRSDNFEEKNGVKLPSYRGDNVNGDAFDLKSRTPDPQRLIRAYCQSAATLNLLRAFATGGYAAMQRVTQWNLDFTEHSEQGDRYRELANRVDEALGFMNAAGLTTDHPIMTTTEFWTSHECLLLPYEQSLTRLDSTSGLYYDCSAHFLWVGERTRQLDGAHVEFLRGIANPLGIKVSDKMDPSALVKLIEILNPQNKAGRITIITRMGAENMRVKLPHLIRAVRGAGQIVTWVSDPMHGNTIKAPCGLKTRPFDSIRAEVRAFFDVHEQEGSHPGGVHLEMTGQNVTECIGGSRTVTFDDLSSRYHTHCDPRLNASQSLELAFIIAERLRKRRLGSQSVLGQ

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). 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:0000250|UniProtKB:O53512, ECO:0000269|PubMed:24815009}.

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};

PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7. {ECO:0000250|UniProtKB:O53512}.

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}.

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:0000269|PubMed:27242828};

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};

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}.

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 transgenic tomato plants promotes fruit ripening and softening. Probably involved in cell wall restructuring during postharvest fruit softening. {ECO:0000269|PubMed:27966647}.

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:0000269|PubMed:27966647};

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}.

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 acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate to the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000256|HAMAP-Rule:MF_03205}.

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-to-right; Xref=Rhea:RHEA:39680; Evidence={ECO:0000256|ARBA:ARBA00001296}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H(+) + malonyl-CoA = (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36475, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57384, ChEBI:CHEBI:73852; Evidence={ECO:0000256|ARBA:ARBA00000904}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36476; Evidence={ECO:0000256|ARBA:ARBA00000904}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA = (8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35379, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57363, ChEBI:CHEBI:57384, ChEBI:CHEBI:71481; Evidence={ECO:0000256|ARBA:ARBA00000735}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35380; Evidence={ECO:0000256|ARBA:ARBA00000735}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + H(+) + malonyl-CoA = (8Z,11Z,14Z,17Z)-3-oxoicosatetraenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:35391, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:71489, ChEBI:CHEBI:71491; Evidence={ECO:0000256|ARBA:ARBA00000337}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35392; Evidence={ECO:0000256|ARBA:ARBA00000337}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H(+) + malonyl-CoA = 3-oxo-(11Z)-octadecenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:39675, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:61540, ChEBI:CHEBI:76555; Evidence={ECO:0000256|ARBA:ARBA00001297}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39676; Evidence={ECO:0000256|ARBA:ARBA00001297}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H(+) + malonyl-CoA = (11Z)-3-oxoicosenoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36511, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:57387, ChEBI:CHEBI:74011; Evidence={ECO:0000256|ARBA:ARBA00001347}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36512; Evidence={ECO:0000256|ARBA:ARBA00001347}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z)-3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36503, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:57384, ChEBI:CHEBI:74012; Evidence={ECO:0000256|ARBA:ARBA00000592}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36504; Evidence={ECO:0000256|ARBA:ARBA00000592}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H(+) + malonyl-CoA = (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:36523, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:74034, ChEBI:CHEBI:74054; Evidence={ECO:0000256|ARBA:ARBA00001158}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36524; Evidence={ECO:0000256|ARBA:ARBA00001158}; CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000256|HAMAP-Rule:MF_03205, ECO:0000256|RuleBase:RU361115};

PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03205}.

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:0030148]; unsaturated fatty acid biosynthetic process [GO:0006636]; very long-chain fatty acid biosynthetic process [GO:0042761]

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=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. {ECO:0000256|HAMAP-Rule:MF_03205}.

IPR002076;IPR033677;

A0A072TFB1

MKKLLAALALAVVAVPVWAATQTVTLSVPGMTCAACPITVKHALSQVTGVEKTDVRFEQREAVVTFDDGKTSVQALTKATADAGYPSPVCLAASCRRWAVRAASRDRQSGRHHWSGLPEPVRRVVHPHPATGLRRRRAVRQCGRLAQASAVAPYRARPDRAAAGAGSRVCDARLWRAQRLAALSRSRHYGGDIALGPVLPGPTQRSKAMMTLKIDGMTCASCAEHVRQALEKVPGVRSAAVSYSKALADLTVDEGVSHDTLTAAVTTAGYHARVADVPPHSAGLPGKTPGSAETGGKRSGGDSALRVAVIGSGGAAMAAALKAAENGAQVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAYLRQTSPFDAGITATAPAIDRPRMLAQQQARVDELRHAKYENILDTSPNINVLHGEARFTGSHSLTITLTAGGERTVSFDRCLIATGATAAVPPIPGLKDTPYWTSTEALVNDAIPERLAVIGSSVVALELAQAFARLGSHVTVLARHTLLYQEDPAIGEAVTAAFRAEGIEVLEQTQATHVSHADGKFVVTTNHGELRADQLLVATGRAPNTGSLNVAGAGVQLDERGAIVIDGGMRTSAPDIYAAGDCTNQPQFVYVAAAAGTRAAINMTGGDVRLNLDTMPTVVFTEPQVATVGYSEAQAHRAGIETDNRTLTLDNVPRGGARGGRTHPDGRDRDPRKDDRAGPRRPAVPVPDNGRGAQARCADLLEGCEAALMLRGITCGGTTMNLARHTAELVERLAMANQLEGFADLFVVLLRELSKGAPVSPAALALALDWPIERVSVALEQAVSTEWDDYGNVVGYGLTLRETPHTFEVDGRRLYTWCAFDTLFFPALIDRTAHVVSRCAATGTPVSLTVTPTAIEDIEPTGAAVSLILPQNTPDIRAAFCCHVHFFASAAAGQQWAATRPGIEVVSVRDAFAVGRECAERLLGATCLRNAGSTNRA

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=Rhea:RHEA:18777, ChEBI:CHEBI:15378, ChEBI:CHEBI:16793, ChEBI:CHEBI:18310, ChEBI:CHEBI:83725; EC=4.99.1.2; Evidence={ECO:0000256|ARBA:ARBA00000165};

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|ARBA:ARBA00001974};

Copper;FAD;Flavoprotein;Lyase;Mercuric resistance;Mercury;Metal-binding;NADP;Oxidoreductase;Periplasm;Redox-active center;Reference proteome;Signal

organomercury catabolic process [GO:0046413]

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]; NADP binding [GO:0050661]; oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor [GO:0016668]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]

SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.

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

MEENKKTVDGSVDFTEEQEALVVKSWNAMKNNSCDLSLKFFTKILEIAPPAKQMFSFLKDSNVPLEQNPKLKPHAMSVFLMTCESAVQLRKAGKVRVRESNLKKLGATHFKTGVQDEHFEVTKQALLETIEEAIPEMWSLAMKNAWAEAHDQLANAIKVEMKEAHDQMDNANLIINMEENTGSCFTEEQEALVVKSWNAIKYNSGDLSLKFFKKILEIAPPAKQLFSFLKDSNVPLEHNPKLKPHAMSVFLMTCESAVQLRKAGKVTVRESNLKKLGATHFKTGVKDEHFEVTKQALLETIKEALPEMWSPAMENAWGEAHDQLANAIKAEMKKTDHDHQTNVEDKSKPSS

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) activity in the absence of O(2) (e.g. during flooding or in waterlogged soil) (PubMed:33329665). May not function as an oxygen storage or transport protein (By similarity). Extremely reactive toward the physiological ligands O(2), nitric oxide (NO), and nitrite with a very high affinity for O(2) through an hexacoordinate heme iron because of a very low dissociation constant (PubMed:33329665). {ECO:0000250|UniProtKB:O04986, ECO:0000269|PubMed:33329665}.; FUNCTION: [Isoform 2]: Very high affinity for O(2) through two hexacoordinate heme irons (PubMed:33329665). Extremely reactive toward the physiological ligands O(2), nitric oxide (NO), and nitrite (PubMed:33329665). {ECO:0000269|PubMed:33329665}.; FUNCTION: [Isoform 4]: Very high affinity for O(2) through a single hexacoordinate heme iron (PubMed:33329665). Extremely reactive toward the physiological ligands O(2), nitric oxide (NO), and nitrite (PubMed:33329665). {ECO:0000269|PubMed:33329665}.

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:0000269|PubMed:33329665}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77712; Evidence={ECO:0000269|PubMed:33329665}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000269|PubMed:33329665};

COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:33329665}; Note=Binds 2 heme groups per subunit. {ECO:0000269|PubMed:33329665};

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]

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}.

IPR000971;IPR009050;IPR012292;IPR001032;IPR019824;

1.10.490.10;

A0A072UR65

MANILNLKHLLTLALILLALATKSSTSSSSSITRVKGIYWLENPFFPPTTVDTSLFTHIFYSFLTPNNITYKLEISSSQILSLNTFTKTFKTKSPPAATLFSIGGAGSNSSLLAFIASDPPACAAFINSTIDVARTFGFDGIDLDWEFPKNTKEMNDLGEMLFQWRKAISDEGATTGRPPLLLTAAVYFAVNFSIYGEPRMYPVNSINENLDWVNVMSYELRGPRSNKTGAPSGTFDPKSNVSVVSGLLSWIHSGVVPEKLVMGMPLYGKSWKLRDPNVHGIGAPSVGSGPGVNGLMAYFQVLDFNRQKSAKVEYDVDTASVYSYSGSTWIGYDNPFTVSIKVGFAQALKLRGYFFWVAGLDTLDWKIATQASKAWKLV

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 to reduce hyphal growth of the fungus Trichoderma viride in an agar-plate bioassay (PubMed:27383628). {ECO:0000269|PubMed:27383628}.

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};

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}.

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]

IPR011583;IPR029070;IPR001223;IPR001579;IPR017853;

3.10.50.10;3.20.20.80;

A0A072VDF2

MPAATAAAAAESSSVSGETICVTGAGGFIASWMVKLLLEKGYTVRGTLRNPDDPKNGHLKKLEGAKERLTLVKVDLLDLNSVKEAVNGCHGVFHTASPVTDNPEEMVEPAVNGAKNVIIAGAEAKVRRVVFTSSIGAVYMDPNRSVDVEVDESCWSDLEFCKKTKNWYCYGKAVAEAAAWDVAKEKGVDLVVVNPVLVLGPLLQPTINASTIHILKYLTGSAKTYANATQAYVHVRDVALAHILVYEKPSASGRYLCAETSLHRGELVEILAKYFPEYPIPTKCSDEKNPRVKPHIFSNKKLKDLGLEFTPVSECLYETVKSLQDQGHLSIPNKEDSLAVKS

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 active, with a lower efficiency, toward coumaroyl-CoA, caffeoyl CoA and sinapoyl-CoA (PubMed:20876124). Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (By similarity). {ECO:0000250|UniProtKB:A0A059TC02, ECO:0000269|PubMed:20876124}.

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-left; Xref=Rhea:RHEA:64650; Evidence={ECO:0000269|PubMed:20876124}; CATALYTIC ACTIVITY: Reaction=(E)-4-coumaraldehyde + CoA + NADP(+) = (E)-4-coumaroyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64652, ChEBI:CHEBI:15378, ChEBI:CHEBI:28353, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85008; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64654; Evidence={ECO:0000269|PubMed:20876124}; CATALYTIC ACTIVITY: Reaction=(E)-sinapaldehyde + CoA + NADP(+) = (E)-sinapoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:64656, ChEBI:CHEBI:15378, ChEBI:CHEBI:27949, ChEBI:CHEBI:57287, ChEBI:CHEBI:57393, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.44; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64658; Evidence={ECO:0000269|PubMed:20876124}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamaldehyde + CoA + NADP(+) = (E)-cinnamoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:10620, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731, ChEBI:CHEBI:57252, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.44; Evidence={ECO:0000250|UniProtKB:Q9S9N9}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10622; Evidence={ECO:0000250|UniProtKB:Q9S9N9}; CATALYTIC ACTIVITY: Reaction=(E)-caffeyl aldehyde + CoA + NADP(+) = (E)-caffeoyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:74867, ChEBI:CHEBI:15378, ChEBI:CHEBI:28323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:87136; Evidence={ECO:0000269|PubMed:20876124}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:74869; Evidence={ECO:0000269|PubMed:20876124};

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|PubMed:20876124}; KM=56.8 uM for coumaroyl-CoA (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Vmax=1.64 umol/min/mg enzyme with feruloyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Vmax=0.15 umol/min/mg enzyme with sinapoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Vmax=0.085 umol/min/mg enzyme with caffeoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Vmax=0.25 umol/min/mg enzyme with coumaroyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) {ECO:0000269|PubMed:20876124}; Note=kcat is 60.1 min(-1) with feruloyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 5.5 min(-1) with sinapoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 3.1 min(-1) with caffeoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 9.0 min(-1) with coumaroyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). {ECO:0000269|PubMed:20876124};

PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis. {ECO:0000250|UniProtKB:A0A059TC02}.

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}.

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 low efficiency, 21-hydroxycyclolochnericine and norajmaline as substrates (PubMed:26848097). {ECO:0000269|PubMed:26848097}.

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:RHEA:76144; Evidence={ECO:0000269|PubMed:26848097};

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-methionine as substrate {ECO:0000269|PubMed:26848097}; Note=kcat is 5.8 sec(-1) with picrinine as substrate (PubMed:26848097). kcat is 4.5 sec(-1) with S-adenosyl-L-methionine as substrate (PubMed:26848097). {ECO:0000269|PubMed:26848097};

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}.

IPR025714;IPR025774;IPR029063;

3.40.50.150;

A0A075D657

MYTCSIIIYILTFWQLSKIKKQVAAAEKQVMTVTEKQEAVAEFYDKSTDAWEVFFGEHLHDGFYEPGTTATIPGSKVAVVRMIDELLRFAGISDDPEKKPKTMLDVGCGLGGTCLHVAKKYDIKCTGITISPEQVKCAQDLAATQGLESKVSFDVGDALDMPYKDGTFDLVFTIQCIEHIQDKEKFIREMVRVAAPGAPVVIAGYAARNLSPSEESLKPEEKMVLEKICDHIVLSWLCSTGDYVKWLTPLPVQDIKVWDLTQNITPFYPLCIKEAFTWKSFTSLLKMGGWSAIKVVFAVKMMAMAAEEGLLKFAAVTCRKSK

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 low efficiency, 21-hydroxycyclolochnericine and norajmaline as substrates (PubMed:26848097). {ECO:0000269|PubMed:26848097}.

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:RHEA:76144; Evidence={ECO:0000269|PubMed:26848097};

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-methionine as substrate {ECO:0000269|PubMed:26848097}; Note=kcat is 5.1 sec(-1) with picrinine as substrate (PubMed:26848097). kcat is 6.9 sec(-1) with S-adenosyl-L-methionine as substrate (PubMed:26848097). {ECO:0000269|PubMed:26848097};

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}.

IPR013216;IPR025774;IPR029063;

3.40.50.150;

A0A075FBG7

MSITFNLKIAPFSGPGIQRSKETFPATEIQITASTKSTMTTKCSFNASTDFMGKLREKVGGKADKPPVVIHPVDISSNLCMIDTLQSLGVDRYFQSEINTLLEHTYRLWKEKKKNIIFKDVSCCAIAFRLLREKGYQVSSDKLAPFADYRIRDVATILELYRASQARLYEDEHTLEKLHDWSSNLLKQHLLNGSIPDHKLHKQVEYFLKNYHGILDRVAVRRSLDLYNINHHHRIPDVADGFPKEDFLEYSMQDFNICQAQQQEELHQLQRWYADCRLDTLNYGRDVVRIANFLTSAIFGEPEFSDARLAFAKHIILVTRIDDFFDHGGSREESYKILDLVQEWKEKPAEEYGSKEVEILFTAVYNTVNDLAEKAHIEQGRCVKPLLIKLWVEILTSFKKELDSWTEETALTLDEYLSSSWVSIGCRICILNSLQYLGIKLSEEMLSSQECTDLCRHVSSVDRLLNDVQTFKKERLENTINSVGLQLAAHKGERAMTEEDAMSKIKEMADYHRRKLMQIVYKEGTVFPRECKDVFLRVCRIGYYLYSSGDEFTSPQQMKEDMKSLVYQPVKIHPLEAINV

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-ene, from (+)-copalyl diphosphate ((+)-CPP) to miltiradiene and from 8-hydroxycopalyl diphosphate (LPP, labda-13-en-8-ol diphosphate) to manoyl oxide (PubMed:24990389). {ECO:0000269|PubMed:24990389, ECO:0000305|PubMed:24990389}.

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=Rhea:RHEA:33983, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635, ChEBI:CHEBI:65037; EC=4.2.3.131; Evidence={ECO:0000269|PubMed:24990389}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33984; Evidence={ECO:0000269|PubMed:24990389}; CATALYTIC ACTIVITY: Reaction=8-hydroxycopalyl diphosphate = (13R)-manoyl oxide + diphosphate; Xref=Rhea:RHEA:54516, ChEBI:CHEBI:33019, ChEBI:CHEBI:64283, ChEBI:CHEBI:138234; EC=4.2.3.190; Evidence={ECO:0000269|PubMed:24990389};

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};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:24990389}.

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}.

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

MASTTPSTYKQAVFKEQGAGLTLEEVALTLPKRDEILVKVEACGVCHSDHFAQTNLMGGGFPLVPGHEIIGRVAAVGEGETVWKEGDRIGGAWHGGHDGTCGACKKGFFQMCDNEQVNGISRNGGYAEYCIIRREAAVHIPDHVNAAKYAPMLCAGVTVFNAMRHMKIPPGELVAIQGLGGLGHLALQYANKFGYRVVALSRDSTKEEFARKLGAHEYIDTSREDPVAALQKLGGASLIVSTAPVPEIINPLIQGLGVMGKLLILSIVGGIEVHTGLLVGKGKSIWSWPSGHATDSEDAIAFADLHGIDCLIEEFPLDKCNEAFAAMMEGSVRFRAVITM

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 of neopatulin into E-ascladiol (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.

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:0000269|PubMed:30680886};

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};

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

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}.

IPR013149;IPR013154;IPR011032;IPR036291;IPR020843;

3.90.180.10;3.40.50.720;

A0A075TMP8

MDILQLAPTHLLAILLSSTSALFLITYLLRAGHRPSDLPNGPPTVPLFGNELQVPKSDAHFQFSRWAKEYGGFFTLKRYNNTTIVISDQKLIKTLLDKKSNIYSHRPASLVSHLITQSDHLLVMQYGERWRMLRKTIHQYFMEPRCERDHWKVQEAEAKQMLHDYLTMPEDHMLHPKRYSNSITNSLVFGIRTKTVHDEYMKKLFYLMDKWSLVQELGATPPVDSFALLRYVPQWMLGNWRNRAVEVGDLMQSLYQTVLDQVKERRQRGIQRDSFMDRVLDTLKQTPLSENELRFLGGVLMEGGSDTSSSLILTIIQAMTKYPEVQAKAHAQIDSIIGHNRSPAWSDWSKLPYINMIIKESHRWRPVSPLGVPHAVAEDDHIDGKLIPQGSSIVLNVWGMHHDSDRWQEPEHFQPERFADFPALASGYAGSERRDHLGYGAGRRICPGIHLAERNLIIGIAKLLWAFEFLEPLGSDSDISAHSGASKGFLHCPKDYGCVIRLRSPEKRETIMREFAEAQEVFARFD

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 conversion of m-hydroxybenzyl alcohol into gentisyl alcohol (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.

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:CHEBI:17069, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62213; Evidence={ECO:0000269|PubMed:30680886};

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798};

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

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}.

IPR001128;IPR002401;IPR036396;

1.10.630.10;

A0A075TR33

MRLHQSPPRLLVCILSVLQVSAGLSSNCRCMPGDSCWPSLNDWARFNTSIGGRLVDTQPLGQPCHDPFYTASECNELKQQWTHPELHDASSSSIMSAAVANETCDAFTPRSKPCTLGAMVRYAVNASSPDDFVQTIRFSQERNIRLVIRNTGHDYAGKSTGAGALSIWTHSLKEIDFLNYTSAHYTGPAVRMTAGIQGTDINPAAHKKGLVIVGGECATVGPVGGFTQGGGHSALSSRFGLAADQVLEWEVVDGMGRLLTASPTQNPDLYWALSGGGGGTFGVVYAVTVKTFPDFAVTGVVLQFENIDPSSNRFFEAVGHYHRHLPTYTSAGGMAIAQITNSSFLLTPLTLPAYTAAATKKLLGPFLQDLHQLNISYTLNVTESASYFQHYMKLIEPNPTQLVQNAQYGGRLLPLDLIERNNSQLTDAVQKLTADGVTFVGIGLNVSSSVTGDIWNSVLPGWRTAAMTVILTTSWPLGANLTKMKILADKMTTKWVPILTALSPESGCYMSEADPQQPDWKQTFYGRNYDSLYAIKTKYDPLQTFYATTAVGSEDWQVEAGGRLCQATRKN

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 the vacuole to convert gentisyl alcohol to isoepoxydon (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.

1.-.-.-

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

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}.

IPR012951;IPR016166;IPR036318;IPR016169;IPR006094;

3.30.465.10;

A0A075TR41

MAPFVPYHYSAGQSTIVKFGGLLTTEFLEPPPGRCFLFRQTYRHTIEGSIPENLRKLINSPDRPKGPPPHFHQFQTEYFRVENGVLGISVDGVVRRITPEDGEISVKAGSVHNFFIHPDSPENMTVYLSASDSGNDYQLDRVFFENWYGYWHDALLHDGGIDWIQFLAIQDGGDAYTPAPAWVPFRRQVGYWTCVIVGRWIGGLLGYKPFFREYTTDWDFAVAKMKGSFFQRHLVHAAFEEEKSWTKQAELEPKGKPENAEFEPWTEDMSPAPLSLGPVAYEQGLFHGVQPGSVNGSNGHSTGVESKLEQLGSRAQRRVVIDDAGK

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 vacuole to convert gentisyl alcohol to isoepoxydon (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.

1.-.-.-

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

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}.

IPR014710;IPR011051;

2.60.120.10;

A0A075TRC0

MHSVSPSTYPSGGTSPAPADTPGTEYSEYEFSNDVAVVGMACRVAGGNHNPELLWQSLLSQKSAVGEIPEMRWEPYYRRDPRNAKELKKTTSRGYFLDRLEDFDCQFFGISPKEAEQMDPQQRVSLEVASEALEDAGIPAKSLSGSDTAVFWGVNSDDYSKLVLEDLPNVEAWMGIGTAYCGVPNRISYHLNLMGPSTAVDAACASSLVAVHHGVQAIRLGESQVAIVGGVNALCGPGLTRVLDKAGAISSDGSCKSFDDDAHGYARGEGAGALVLKSLHRALLDHDNVLAVIKGSAVAQDGKTNGIMAPNAKAQQLAARTALNVAGVDPSTVRYVEAHATSTPLGDPTEISAIAGVYGTNRPADDPCYIGSIKPNIGHLEAGAGVMGFIKAILTIQKGVLPPQANLTNLNSRIDWKTAGVKVVQEATPWPSSDPIRRAGVCSYGYGGTVSHAVIEEFNPILRPDPLDDGAATGPGLLLLSGPQEKRLALQAKTLREWMTADGKDNNLSEILTTLATRRDHHDYRAALVVDDHLDATQVLQALANGTDHSFTTQSRVLGADVSKDVVWVFSGHGAQWPDMGKQLIHNPVFFAAIQPLDELIQAEIGLSPIELLRTGDFESSDRVQILTYLMQIGLSAILQSNGITPQAVIGHSVGEIAASVVAGALTSAEGALIVTRRALLYRQVMGKGGMILVNLPSAETEEILGRRQDLVVAIDSSPSSCVVAGDKDIVAETAEAFKARGVKTFTVKSDIAFHSPTLNVLMDPLRDALGQALAPTVHIKLYSTALVDPRGQDVRDLEYWTGNMVNRVRLTSAIQAAVEDGYRLFLEVSTHPVVSHSINETLMDAGLEDFAVIPTLLRKKPTEKHILHSIAQLHCRGAEVNWAAQMPGRWATGLPTTTWMHKPIWRKIETAPLHTGLTHDVEKHTLLGQRIPVPGTDTFVYTSRLDNETKPFPGSHPLHGTEIVPAAGLINTFLKGTGGQMLQNVVLRVPVAINAPRSVQVVVQQDQVKVVSRLISSDPSLSDDDASWVTHTTAYWDRKVLGSADRIDLAAVKARLTTKLADNFSIDYLDKVGVSAMGFPWAVTEHYRDTKQMLARVDVNPAVLGDDPLPWDSSSWAPVLDAATSVGSTVFQTAALRMPAQIERVEIFTSEDPPKISYLFVEEASDSVPTSHVSVLSETGEVLAKFTAMRFSEIEGTPGVSGSMESLVHQIAWPPATPAEEPLLITKVILVSPDATARAQYAATLPTQVQSFQFSTTEDFFSNASSLPLEKGTVVAYIPGEVASLAEVPAASESFTWNLLELIKFIVNGSLPIKVFTLTSSVGDGQTPTALAQSPLIGLARIIASEHPDLGSLIDIEEPKIPLSTMRYIQGADVIRISDGIARVSRFRSLPRTKLRPASEGPRLLPRPDGTYLITGGLGILGLEVADFLVEKGARRLLLISRRALPPRRTWDQVSEDLQPTIAKIRLLESRGASVHVLPLDITKPDAVEQLSTALDRLSLPAVQGVVHAAGVLDNEMVLQTTRDAFNRVLAPKIAGALALHEVFPPKSVDFFVMFSSCGNLVGFTGQASYGSGNAFLDTLATHRARLGDSGAVAFQWTAWRGLGMGSSTDFINAELEAKGITDVTRDEAFAAWQHLAKYDIDHGVVLRSLAIDDGEPVPVPILNDIVVRRVSELSGSAQAAAGSSGNDAVPSSGPELKAYLDEKIRGCVAKVLQMTAEDVDSKAALADLGVDSVMTVTLRRQLQQTLKIPVPPTLTWSHPTVSHLVVWFAEKIGK

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). PatK catalyzes the first step of the pathway which is the synthesis of 6-methylsalicylic acid via condensation of 1 acetate and 3 malonate units (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000269|PubMed:35339702, ECO:0000305|PubMed:30680886}.

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; EC=2.3.1.165; Evidence={ECO:0000269|PubMed:30680886};

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

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}.

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 product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm. {ECO:0000250|UniProtKB:Q5B0D0}.

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

MRLTSGIFHAAIAVAAVGAVLPEGPSSSKTHRNEYARRMLGSSFGIPKNQTFDYLVIGGGTAGLTIATRLAEQGVGSVAVIEAGGFYELNNGNLSQIPAQDAFYVGTDLDDWQPGIDWGFHTTPQAGAYDRVSHYARGKCLGGSSARNYMAYQRGTKAAHQRWADTVGDSSYTWEQFLPFFEKSLHFTPANDALRGANASVVSDPSVLGNGDGPLSVTYPHYAQAFATWAKHAFIEIGLQIRSGFQSGALLGQSYGLYTINATTMHRESSETSFLRKGLADPNLTVFQSALAKRIRFQDKRAVGVDVETMGRAYTLSARKEIVLSAGAFQSPQLLMVSGVGPAATLKAHNIPLVADRPGVGQNMQDHIIYAPSYRVNVITQSALLNEEFEAQANRDYNERAAGIYANPTSDILAWEKIPEPKRSAWFSNHTRQVLAEYPDDWPEVEFLTMGGYFGYQRNYIRDNPSDGYNYASLAVSLCTPRSRGNVTITSPDAGVPPVINPNWLTDPVDVELAVAAFKRTRDFFNTTAIKPILIGPEYFPGSQVATDAEILDHVRKSFDTIFHASCTCAMGLANDTQAVVDSKARVIGVEALRVVDASALPFLPPGHPQSTLYALAEKIACEISGNC

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 the pathway which is the conversion of E-ascladiol to patulin (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.

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};

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

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}.

IPR036188;IPR012132;IPR000172;IPR007867;

3.50.50.60;3.30.560.10;

A0A075TRL5

MEPFLLLLLVLLPAIVLVRYAFTYGHRTSTMPIGPPTLPFIGNIHQITKKYTHIKFTEWAAQYGGLYMLKIGNGNMAVITDRRLVKEVLDRKSGIYSHRPHSFVSHDLITKGNHLLVMHYGDQWRTFRRLVHQHLMETMVENHHTKIVNAEAIQLVRDYMIDPEHHMAHPKRYSNSITNSIVFGIRTANREGANMRRLYKLMEEWSEVMETGATPPVDLFPWLKLLPQWLFNNYIDRAKAIGVQMETLYVDILNKVIKRREDGHNNGTFMDKVLDSQEKHNLPWHQLAFIGGVLMEGGSDTSSSLTLAIVQALIQNPDVQRKAHAEIDAVVGHNRSPVWEDFEKLPYINMIIKEGHRWRPILPLCFPHALGEDDWVDGKFLPKGTIVVVNTWGMHMDPSQPDDPAAFIPERFAKHPQLAPDYVPGTWERRDHYGYGVGRRICPGIHLAERNMFLGIAKLLWAFDFQPGEGPIDSDPVTGYHNGFLYCAKDYSCRPVIRNEVIRDTIEREYATATADVFSRFTEG

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 conversion of m-cresol into m-hydroxybenzyl alcohol (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.

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:CHEBI:17231, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:30680886}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62209; Evidence={ECO:0000269|PubMed:30680886};

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798};

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

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}.

IPR001128;IPR002401;IPR036396;

1.10.630.10;

A0A075TXZ1

MAKIDVHHHFYPPAMRQALDRAGGDPSGWYIPPWTLELDQDITRQMKVTTTILSVTAPGPGIEPDVTKAAALARSCNESAAAIRDAKPQQYGFFASVPSLFDTAAVLKEIEYACTTLRADGVTLFTRYGKGSNYLGHAAFRPIWADLSRRGAVVFIHPTHPVDTQLINTWLPQPMFDYPHETGRAAMDLLTSGILQDYPGCKIILSHAGGTLPYLIHRAATMLPLMPRTLGLSTEELVEAARTFYFDTAISSNPVTLKALFEFAAPGHVLFGSDFPNAPHDAILRFTNFLEAYELPEETKRQVDSGAALELFPRLKGILDKAKL

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 the decarboxylation of 6-methylsalicylic acid to yield m-cresol (PubMed:30680886). The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:30680886). {ECO:0000269|PubMed:25625822, ECO:0000269|PubMed:30100914, ECO:0000269|PubMed:30680886, ECO:0000305|PubMed:30680886}.

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:30680886};

PATHWAY: Mycotoxin biosynthesis; patulin biosynthesis. {ECO:0000269|PubMed:30680886}.

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}.

IPR032465;IPR006680;IPR032466;

3.20.20.140;

A0A076FFM5

MPFPMEVLQASSLSFPLLRRHSRNNLINKFRNPTLPRIDIPRQNIDLKTFAATTPTVACPPSDPEIIPEKKEDKFDWYENWYPVATVCDLDKRRPHGRKVIGIDVVVWWDRKENAWKVFDDTCPHRLAPLSEGRIDQWGRLQCVYHGWCFDGVGACKFIPQAPHDGPPVETSKKACVKGVYPSCVRNGIVWFWPNSDPKYKDIYLTNKPHYIPELDDPSFTCTTITREVPYGYEILAENLMDPSHVPYAHYGILELEKVKESSKRDREGGHEMEISVGTIDVNGFSAKHVSADYYFVPPYVYYGRITPNAATKTKDATLPVVPEEKTAMIVFYCIPVTPGYSRLIYAGARNFAVQIDRFVPRWITHMSHNLIFDSDLFLLHVEEQKLKDLDWHKSCYIPTKADGQVVAFRRWLNKYGGTQVDWRNNFTPALPPTPSREQLFDRYWSHTAECSSCSVACKRLNALEIGLQAMSLVFVAMAAAVSAPATRYSMVAMAVLSFLASKWLSHFIHKTFYNHGYDHAFV

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-proliferative, and anti-inflammatory effects (PubMed:25139498). Catalyzes the 8-hydroxylation of salvigenin (SALV) to produce 8-hydroxysalvigenin (8-OH-SALV) (PubMed:25139498). Can also use cirsimaritin (CIRM) as substrate with low efficiency (PubMed:25139498). {ECO:0000269|PubMed:25139498}.

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:CHEBI:192703, ChEBI:CHEBI:192704; Evidence={ECO:0000269|PubMed:25139498}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73456; Evidence={ECO:0000269|PubMed:25139498};

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}.

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}.

IPR013626;IPR017941;IPR036922;

2.102.10.10;

A0A078CGE6

MARQMTSSQFHKSKTLDNKYMLGDEIGKGAYGRVYIGLDLENGDFVAIKQVSLENIVQEDLNTIMQEIDLLKNLNHKNIVKYLGSLKTKTHLHIILEYVENGSLANIIKPNKFGPFPESLVTVYIAQVLEGLVYLHEQGVIHRDIKGANILTTKEGLVKLADFGVATKLNEADVNTHSVVGTPYWMAPEVIEMSGVCAASDIWSVGCTVIELLTCVPPYYDLQPMPALFRIVQDDSPPIPDSLSPDITDFLRQCFKKDSRQRPDAKTLLSHPWIRNSRRALQSSLRHSGTIRYMKGADSSSEKDGEGSQDIAESVSAEKVGMSKTNSKSKLGVGSFRSEKDQSSASDIGEERADSEDDIMSDQGPTLSIHDNKSSLQSSTCSISSDAKGTSQDGKSEPDGNLEMEASEGRRKASATKQVGKESSIQMQQRSHSFGPKGEDRGLRKAVKTPSSYGGNELTRFSDPPGDACLHDLFHPLNKVPEGKLNEASASTPASNANQGDSPVADGGKNDLATKLRARIAQKQMEGETGHSNDGGDLFRLMMGVLKDDVIDIDGLVFDEKASPDNLLPLQAVEFSRLVSSLRPSETEDAIVTSCQKLVAMFRHRPEQKVVFVTQHGFLPVMDLLDSPKSRVTCAVLQLINEIIKDNIDFQENACLVGLIPLVMSFAGPERDRSREIRKEAAYFLQQLCQSSSLTLQMFIACRGIPVLVGFLEADYAKYRSMVHLAIDGMWQVFKLKRSTPRNDFCRIAAKNGILLRLINTLYSLNEATLLASEGRSGQLDQHEALLSVIDHPDVLKTRPGGGEEPSNSQRSDLYQPDGDRPRSSSAALDATEDVKQHHRISISSNRTSTDKIQKLAESASNGYAVTQPEQVRPLLSLLEKEPPSRHVSGQLDYVKHIAGLEKHESILPLLRASIDTMPRYFSKTMSKKVMAIEGAASASGVLSGSGVLNARLGSDTSSGLLSHMVTTLSAEVASQYLEKVADLLLEFARADTTVKSYMCSQSLLSRLFHMFNRVEPPILLKILKCTNHLSTDPNCLESLQRADAIKHLIPNLEVKEGNLVDQIHHEVLSALFNLCKINKRRQEQAAENGIIPHLMLFVMSDSPLKQYALPLLCDMAHASRNSREQLRSHGGLDVYLSLLDDEYWSVIALDSIAVCLAQDNDNRKVEQALLKDDAIYTLVNFFQSCPERHFVHILEPFLKIITKSSRINTTLAVNGLTPLLIARLDHQDAIARLNLLKLIKAVYEHHPRPKQLIVENDLPQRLQNLIEERREGQHLGGQVLVKQMATSLLKALHINTVL

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 development (By similarity). {ECO:0000250|UniProtKB:Q9LJD8, ECO:0000269|PubMed:11489177}.

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 ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11489177};

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 developing pollen grains (By similarity). {ECO:0000250|UniProtKB:Q9LJD8, ECO:0000269|PubMed:15292395}.

PTM: Autophosphorylated. {ECO:0000269|PubMed:11489177}.

IPR011989;IPR016024;IPR011009;IPR000719;IPR017441;IPR001245;IPR008271;

1.25.10.10;1.10.510.10;

A0A087QH05

LQCYCHLCTKDNFTCVTDGLCFTSVTRTADKVIHNSMCIAEIDLIPRDRPFVCAPSARDGVITLPHCCDKDHCNKIELPIPTPGKPASNLGPVELAAVIAGPVCFVCISLMLILYLCHNRTVIHHRVPSEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQKLRPNIPNRWQSCEVLTNLAK

Aptenodytes forsteri (Emperor penguin)

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:ARBA00023945}; 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; Evidence={ECO:0000256|ARBA:ARBA00023948};

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};

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 system development [GO:0007399]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of gene expression [GO:0010628]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of gene expression [GO:0010468]; transforming growth factor beta receptor signaling pathway [GO:0007179]

activin receptor complex [GO:0048179]; bicellular tight junction [GO:0005923]; cell surface [GO:0009986]; 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:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR000472;IPR003605;IPR011009;IPR000719;IPR017441;IPR008271;IPR045860;IPR000333;

2.10.60.10;1.10.510.10;

A0A087X1C5

MGLEALVPLAMIVAIFLLLVDLMHRHQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREAMVTRGEDTADRPPAPIYQVLGFGPRSQGVILSRYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFADQAGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLPHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAKKEKAKGSPESSFNDENLRIVVGNLFLAGMVTTSTTLAWGLLLMILHLDVQRGRRVSPGCPIVGTHVCPVRVQQEIDDVIGQVRRPEMGDQAHMPCTTAVIHEVQHFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWKKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQPRPSHSRVVSFLVTPSPYELCAVPR

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:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000269|PubMed:15051713};

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413;

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}.

IPR001128;IPR017972;IPR002401;IPR008069;IPR036396;

1.10.630.10;

A0A087X296

MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPGLWTWLRNSLRPSPSFTHFLLTHGRWFWEFVNATFIREMLMRLVLTGKKQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFKVGSQEYSYEQFLFNTSMLVDYGVEALVDAFSRQIAGRIGGGRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGFNIVKTATLKKLVCLNTKTCPYVSFRVPDASQDDGPAVERPSTEL

Homo sapiens (Human)

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}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1; Evidence={ECO:0000256|ARBA:ARBA00001779}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729; Evidence={ECO:0000256|ARBA:ARBA00001779}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13R)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75455, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:136655; Evidence={ECO:0000256|ARBA:ARBA00036409}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456; Evidence={ECO:0000256|ARBA:ARBA00036409}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13S)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75451, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:90850; Evidence={ECO:0000256|ARBA:ARBA00036358}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452; Evidence={ECO:0000256|ARBA:ARBA00036358}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9R)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75447, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77895; Evidence={ECO:0000256|ARBA:ARBA00036313}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448; Evidence={ECO:0000256|ARBA:ARBA00036313}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9S)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75459, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77852; Evidence={ECO:0000256|ARBA:ARBA00035976}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460; Evidence={ECO:0000256|ARBA:ARBA00035976}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:42600, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57405, ChEBI:CHEBI:82629; Evidence={ECO:0000256|ARBA:ARBA00000489}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601; Evidence={ECO:0000256|ARBA:ARBA00000489};

COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000256|ARBA:ARBA00001970};

PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000256|ARBA:ARBA00004702}.

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}.

IPR000742;IPR019791;IPR010255;IPR037120;

1.10.640.10;2.10.25.10;

A0A089QRB9

MRTATATSVAVIGMACRLPGGIDSPQRLWEALLRGDDLVGEIPADRWDANVYYDPEPGVPGRSVSRWGAFLDDVGGFDCDFFGLTEREATAIDPQHRLLLEVSWEAIEHAGVDPATLAESQTGVFVGLTHGDYELLSADCGAAEGPYGFTGTSNSFASGRVAYTLGLHGPAVTVDTACSSGLTAVHQACRSLDDGESDLALAGGVVVTLEPRKSVSGSLQGMLSPTGRCHAFDEAADGFVSGEGCVVLLLKRLPDAVRDGDRVLAIVRGTAANQDGRTVNIAAPSAQAQIAVYQQALAAAGVEASTVGMVEAHGTGTPVGDPVEYASLAAVYGTEGPCALTSVKTNFGHLQSASGPLGLMKTILALRHGVVPQNLHFCRLPDQLAEIDTELFVPQANTSWPDNTGQPRRAAVSSYGMSGTNVHAILEQAPVSEPAASGPELTPEAGGLALFPVSATSAEQLHVTAARLADWVDQNGNAGSRVSMRDLGYTLSCRRAHRPVRTVVTASSFDELSAALRDVAGDQIPYQPAVGHDDRGPVWVFSGQGSQWPGMGTELLVAEPVFAATVAAMEPVIARESGFSVTEAMSAPQTVSGIDRVQPTIFAVQVALAAALKSYGVRPGAIIGHSLGEAAAAVVAGALSLHDGLRVICRRSRLMSRIAGSGAMASVELPGQQVLSELAIRGISDVVLSVVASPTSTVVGGATQSIRDLVAAWEQQDVLAREVAVDVASHTPQVDPILDELLEVLAEVDPTAPEIPYYSATLWDPRERPSFTGEYWVENLRYTVRFAAAVQAALKDGYRVFGELAPHPLLTYAVEQNAASLDMPIATLAAMRRGEQLPFGLRGFVADVHNAGAKVDFSVQYPDGRLVDAPLPSWTHRTLMLSREDSHRSHTGAVQAVHPLLGAHVHLLEEPERHVWQAGVGTGAHPWLGDHRIHNVAAFPGAAYCEMALAAARTTLGELSEVRDIKFEQTLLLDEQTVVSSAATIAAPGILQFAVESHQEGEPARRASAMLHALEEMPQPPGYDTNALTAAHESSMSGEELRKMFNSLGIQYGPAFSGLVAVHTARGDVTTVLAEVALPGAIRSQQSAYASHPALLDACFQSVLVHPEVQKATVGGLMLPVGVRRLRNYHSTRSAHYCLARVTSSSRAGECEADLDVFDQAGTVLLTVEGLRLAAGISEHERANRVFDERLLTIEWERGELPEVPQIDAGSWLLLSASEADPLTAQLADALNAVGAQSTSVASASDVAQLRSLLGGRLTGVVVVTGPPTGGLTQCGRDYVSQLVGIARELAELPGEPPRLFVVTRSAASVLPSDLANLEQAGLRGLMRVIDSEHPHLGATAIDVDNDETVAALVASQLQSGSQEDETAWRNGIWYTARLRPGPLRPAERRTAVVEYRRDGMRLQIRTPGDLESLEFVTFDRVAPGPGEIEVAVTASSVNFADVLVAFGRYPTFEGYRQQLGIDFAGVVTAVGPDVTEHRIGDHVGGMSANGCWSTFVRCDARLAVTLPPELPVAAAAAVPTASATAWYALHDLARICSDDKVLIHSGTGGVGQAAIAIARAAGCEIFATAGSAQRRQLLHDMGVEHVYDSRSTEFAEQIRGDTDGYGVDVVLNSLPGAAQRAGIELLAFGGRFVEIGKRDIYGDTRLGLFPFRRNLSLYAVDLALLTHSHPHTVRRLLKTVYQHTVEGTLPVPQTTHYPIHDAAVAIRLVGGAGHTGKVVLDVPRTGEGVAVVPPEQVRTSRPDGAYLVTGGLGGLGLFLAGELAAAGCGRIVLNSRSTPSPHATRVIERLRAAGADIQVECGDIADAATAHRVVAVATASGLPVRGVLHAAAVVEDATLANVTDELIDRCWAPKVHGAWNIHRATAAQPLEWFCLFSSAAALVGSPGQGAYAAANSWLDAFAHWRRAQGLPATSIAWGAWAEIGRATALAEGTGAAIAPAEGARAFQTLLRYGRAYSGYAPIMGTPWLTAFAQRSRFAEAFHATGQNQPATGKFLAELGSLPREEWPRTVRRLVSDQISLLLRRTIDPDRPLSDYGLDSLGNLELRTRIETETGIRVSPTKITTVRGLAEHVCDELAAAQSAPV

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 three methylmalonyl (but not malonyl) residues, to form trimethyl-branched fatty-acids. {ECO:0000269|PubMed:12207710}.

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:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57327, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64479, ChEBI:CHEBI:83139, ChEBI:CHEBI:132361; EC=2.3.1.252; Evidence={ECO:0000305|PubMed:12207710};

PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305|PubMed:12207710}.

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}.

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

MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHRKCNYSFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP

Homo sapiens (Human)

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, ChEBI:CHEBI:61961; EC=2.1.1.356; Evidence={ECO:0000256|ARBA:ARBA00000090};

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 [GO:0070314]; G1/S transition of mitotic cell cycle [GO:0000082]; hepatocyte homeostasis [GO:0036333]; hippocampus development [GO:0021766]; keratinocyte differentiation [GO:0030216]; liver regeneration [GO:0097421]; methylation [GO:0032259]; negative regulation of cytokine production involved in inflammatory response [GO:1900016]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of keratinocyte differentiation [GO:0045617]; negative regulation of stem cell differentiation [GO:2000737]; negative regulation of striated muscle cell differentiation [GO:0051154]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; positive regulation of dendrite development [GO:1900006]; protein localization to chromatin [GO:0071168]; protein modification process [GO:0036211]; regulation of cell population proliferation [GO:0042127]; regulation of circadian rhythm [GO:0042752]; regulation of gliogenesis [GO:0014013]; regulation of kidney development [GO:0090183]; regulation of protein phosphorylation [GO:0001932]; response to estradiol [GO:0032355]; response to tetrachloromethane [GO:1904772]; rhythmic process [GO:0048511]; skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration [GO:0014834]; stem cell differentiation [GO:0048863]; synaptic transmission, GABAergic [GO:0051932]

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 promoter sequence-specific DNA binding [GO:0000979]; transcription corepressor activity [GO:0003714]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR026489;IPR045318;IPR048358;IPR021654;IPR044439;IPR041343;IPR041355;IPR001005;IPR001214;IPR046341;IPR033467;

1.20.58.1880;2.170.270.10;

A0A093GWH1

MLRLSTLLRRTRPVSRALAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKAIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARAIAREGFEKISKGANPVEIRRGVMLAVDAVITELKKLSKPVTTPEEIAQVATISANGDQEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLISEKKISSVQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNVEDIQPHDFGKVGEVIVTKDDTMLLKGKGEKAQIEKRIQEIIEQLEVTTSDYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVPGGGCALLRCIPALDALTPANEDQKIGIEIIRRTLKIPAVTIAKNAGVEGSLIVEKIMQSPSEVGYDAMLGDFVNMVEKGIIDPTKVVRTALMDAAGVASLLSTAEAVVTEVPKEEKEPAMGGMGGMGGGMGGGMF

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 mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. {ECO:0000256|ARBA:ARBA00037436}.

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};

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]; mitochondrial unfolded protein response [GO:0034514]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; negative regulation of apoptotic process [GO:0043066]; positive regulation of apoptotic process [GO:0043065]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of macrophage activation [GO:0043032]; positive regulation of T cell activation [GO:0050870]; positive regulation of T cell mediated immune response to tumor cell [GO:0002842]; positive regulation of type II interferon production [GO:0032729]; protein import into mitochondrial intermembrane space [GO:0045041]; protein refolding [GO:0042026]; protein stabilization [GO:0050821]; response to cold [GO:0009409]; response to heat [GO:0009408]; T cell activation [GO:0042110]

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 matrix [GO:0005759]; secretory granule [GO:0030141]; sperm midpiece [GO:0097225]; sperm plasma membrane [GO:0097524]

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 [GO:0051087]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082]

IPR018370;IPR001844;IPR002423;IPR027409;IPR027413;IPR027410;

3.50.7.10;1.10.560.10;3.30.260.10;