ID D9D5J1_OSTNU Unreviewed; 459 AA.
AC D9D5J1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 40.
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:ADI82791.1};
RN [1] {ECO:0000313|EMBL:ADI82791.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Z {ECO:0000313|EMBL:ADI82791.1};
RC TISSUE=Pheromone gland {ECO:0000313|EMBL:ADI82791.1};
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:ADI82791.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Z {ECO:0000313|EMBL:ADI82791.1};
RC TISSUE=Pheromone gland {ECO:0000313|EMBL:ADI82791.1};
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=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; GU808267; ADI82791.1; -; mRNA.
DR AlphaFoldDB; D9D5J1; -.
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.
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 364..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 459 AA; 52259 MW; A286DA277844AE68 CRC64;
MSANTMETDE QFTYNSPIVN FYSGKSVFVT GATGFLGTVL VEKLLFSCKG INNIYILIKQ
TEDLTIEARI LNYLNSKAFH RVKNTNPELM KKIIPICGNL EDKNLGISDS DMKTLLEEVS
IVFHLAAKLL FKMSLAAAVN INTKSTEQLI AICKKMRRNP IFIYVSSAYS NVNKQIIDEK
VYSTGVPLET IYDTLDAKNT RLMDIFLDKR PNTYTYSKAL AEVLVEKEFN ESAAIVRPSI
IASSIREPIP GWLSGSHGFP RVVEAACKGL LLRWHGDGTV AFDIIPVDHV ANLIIAAAWE
SNERRLMGNK GVKVYNCCSG LRNPIDVSTV MNTCLKYRKY FGTRTMSIIT PRFIMKKNYF
LYKLLYFTYH TIPAAIIDGF FWLTGRTPMM LNTLHKLRKL SSVLEYFTLR QFLFLDSNVR
GLLRRMEGTD RQTFNFDVAE IEWEPFLQNC VRGIANNYD
//
