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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//