ID U5KFM9_AGRIP Unreviewed; 238 AA.
AC U5KFM9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
DE Flags: Fragment;
OS Agrotis ipsilon (Black cutworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Noctuinae; Noctuini; Agrotis.
OX NCBI_TaxID=56364 {ECO:0000313|EMBL:AGR49328.1};
RN [1] {ECO:0000313|EMBL:AGR49328.1}
RP NUCLEOTIDE SEQUENCE.
RA Gu S.-H., Zhou J.-J., Guo Y.-Y., Zhang Y.-J.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGR49328.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24053512; DOI=10.1186/1471-2164-14-636;
RA Gu S.H., Wu K.M., Guo Y.Y., Pickett J.A., Field L.M., Zhou J.J.,
RA Zhang Y.J.;
RT "Identification of genes expressed in the sex pheromone gland of the black
RT cutworm Agrotis ipsilon with putative roles in sex pheromone biosynthesis
RT and transport.";
RL BMC Genomics 14:636-636(2013).
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; JX989169; AGR49328.1; -; mRNA.
DR AlphaFoldDB; U5KFM9; -.
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 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:SF12; 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}; NADP {ECO:0000256|RuleBase:RU363097};
KW Oxidoreductase {ECO:0000256|RuleBase:RU363097}.
FT DOMAIN 21..121
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 194..238
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGR49328.1"
FT NON_TER 238
FT /evidence="ECO:0000313|EMBL:AGR49328.1"
SQ SEQUENCE 238 AA; 26770 MW; 24513ED4C68FCACA CRC64;
EKCHAPPVDP DHVMKLVQWL DNNQLALLTP SLLGPHPNCY TFSKRLAENL VEQAHPHMPV
VIARPSIVCP AVKEPMPGWV DNLNGPVGVM LGAGKGVIRT MLCNGNLIAQ VVPVDIAINA
IIAIGMLEGS RTEKPESLPV YNVNNGHQKP TTWGDVLNVA KAYGRQYPLS WPLWYPNGDI
TTNKFLHEYR RICYHLVPAY LIDLLLFLLG QKRIMVRIQE RVSQGLEVLQ YFTMRPWN
//
