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Database: UniProt
Entry: D9D5I7_OSTNU
LinkDB: D9D5I7_OSTNU
Original site: D9D5I7_OSTNU 
ID   D9D5I7_OSTNU            Unreviewed;       462 AA.
AC   D9D5I7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE            EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
OS   Ostrinia nubilalis (European corn borer) (Pyralis nubilalis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC   Crambidae; Pyraustinae; Ostrinia.
OX   NCBI_TaxID=29057 {ECO:0000313|EMBL:ADI82787.1};
RN   [1] {ECO:0000313|EMBL:ADI82787.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=E {ECO:0000313|EMBL:ADI82787.1};
RC   TISSUE=Pheromone gland {ECO:0000313|EMBL:ADI82787.1};
RX   PubMed=20592730; DOI=10.1038/nature09058;
RA   Lassance J.M., Groot A.T., Lienard M.A., Antony B., Borgwardt C.,
RA   Andersson F., Hedenstrom E., Heckel D.G., Lofstedt C.;
RT   "Allelic variation in a fatty-acyl reductase gene causes divergence in moth
RT   sex pheromones.";
RL   Nature 466:486-489(2010).
RN   [2] {ECO:0000313|EMBL:ADI82787.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=E {ECO:0000313|EMBL:ADI82787.1};
RC   TISSUE=Pheromone gland {ECO:0000313|EMBL:ADI82787.1};
RA   Lassance J.-M., Groot A.T., Lienard M.A., Antony B., Borgwardt C.,
RA   Andersson F., Hedenstrom E., Heckel D.G., Lofstedt C.;
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
CC       {ECO:0000256|RuleBase:RU363097}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 2 H(+) + 2 NADPH = (9Z)-octadecen-1-ol
CC         + CoA + 2 NADP(+); Xref=Rhea:RHEA:36323, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:73504;
CC         Evidence={ECO:0000256|ARBA:ARBA00036455};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36324;
CC         Evidence={ECO:0000256|ARBA:ARBA00036455};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoyl-CoA + 2 H(+) + 2 NADPH = (9Z,12Z)-
CC         octadecadien-1-ol + CoA + 2 NADP(+); Xref=Rhea:RHEA:36363,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:73534;
CC         Evidence={ECO:0000256|ARBA:ARBA00036062};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36364;
CC         Evidence={ECO:0000256|ARBA:ARBA00036062};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + hexadecanoyl-CoA + 2 NADPH = CoA + hexadecan-1-ol + 2
CC         NADP(+); Xref=Rhea:RHEA:36315, ChEBI:CHEBI:15378, ChEBI:CHEBI:16125,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.2.1.84;
CC         Evidence={ECO:0000256|ARBA:ARBA00000203};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36316;
CC         Evidence={ECO:0000256|ARBA:ARBA00000203};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain
CC         primary fatty alcohol + CoA + 2 NADP(+); Xref=Rhea:RHEA:52716,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:77396, ChEBI:CHEBI:83139; EC=1.2.1.84;
CC         Evidence={ECO:0000256|RuleBase:RU363097};
CC   -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC       {ECO:0000256|ARBA:ARBA00005928, ECO:0000256|RuleBase:RU363097}.
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DR   EMBL; GU808263; ADI82787.1; -; mRNA.
DR   AlphaFoldDB; D9D5I7; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0102965; F:alcohol-forming long-chain fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0080019; F:alcohol-forming very long-chain fatty acyl-CoA reductase activity; IEA:InterPro.
DR   GO; GO:1901568; P:fatty acid derivative metabolic process; IEA:UniProt.
DR   CDD; cd05236; FAR-N_SDR_e; 1.
DR   CDD; cd09071; FAR_C; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR026055; FAR.
DR   InterPro; IPR033640; FAR_C.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11011:SF45; FATTY ACYL-COA REDUCTASE 1; 1.
DR   PANTHER; PTHR11011; MALE STERILITY PROTEIN 2-RELATED; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF03015; Sterile; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   2: Evidence at transcript level;
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|RuleBase:RU363097};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU363097}; Membrane {ECO:0000256|RuleBase:RU363097};
KW   NADP {ECO:0000256|RuleBase:RU363097};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363097};
KW   Transmembrane {ECO:0000256|RuleBase:RU363097};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT   TRANSMEM        360..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363097"
FT   DOMAIN          29..294
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
FT   DOMAIN          369..455
FT                   /note="Fatty acyl-CoA reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03015"
SQ   SEQUENCE   462 AA;  52708 MW;  4AE86E674A441AE9 CRC64;
     MSANTMETDE QFTYNSPIVN FYSGKSVFVT GATGFLGTVL VEKLLFSCKG INNIYILIKQ
     TEDLTIEARI LNYLNSKAFH RVKNTNPELM KKIIPICGNL EDKNLGISDS DMKTLLEEVS
     IVFHVAAKLL FKMSLTAAVN INTKPTEQLI AICKKMRRNP IFIYVSSAYS NVNEQIIDEK
     VYNTGVPLET IYDTLDTENT RITDIFLDKR PNTYTYSKAL AEVVVEKEFD ESAAIVRPSI
     IVSSIREPIP GWLSGSHGFP RVVGAACKGL LLRWHGDGTV VCDLIPVDHV ANLIIAAAWE
     SNERRLMGNK GVKVYNCCSS LRKPIDVITV VKTCIKYRKY FGTRTMSIFT PRFIMKKNYF
     IYKLLYFTYH TIPAAIIDGF FWLTGRTPIM LKTLDKLSKI SSVLEYFTHH QFIFLDSNVR
     GLLRRMEGTD RQTFNFDVTE IEWEPYLQNF VRGIANNYDY SM
//
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