ID A0A182VNQ1_ANOME Unreviewed; 481 AA.
AC A0A182VNQ1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
OS Anopheles merus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM018082-PA, ECO:0000313|Proteomes:UP000075903};
RN [1] {ECO:0000313|Proteomes:UP000075903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAF {ECO:0000313|Proteomes:UP000075903};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles merus MAF (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMEM018082-PA}
RP IDENTIFICATION.
RC STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM018082-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 AlphaFoldDB; A0A182VNQ1; -.
DR STRING; 30066.A0A182VNQ1; -.
DR EnsemblMetazoa; AMEM018082-RA; AMEM018082-PA; AMEM018082.
DR VEuPathDB; VectorBase:AMEM018082; -.
DR VEuPathDB; VectorBase:AMEM21_001684; -.
DR OrthoDB; 3416210at2759; -.
DR Proteomes; UP000075903; Unassembled WGS sequence.
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:SF81; 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 3: Inferred from homology;
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 29..300
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 377..466
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 481 AA; 54735 MW; 9B88AF442F4F37E0 CRC64;
MNTETIDTGP VLEGALNVAE FYRGATVLVT GGTGFIGKVL VEKLLRCFEV KKIFLLIRRK
GNVSATDRLQ QMLEGPIFDT IRSTAPDAKE RFAKVVAMDA AFDREDIVDD VDKTKLCNEV
QIVFHVMASI RFNEVLDEAI AINVTSAQRL YALASSMAEL RSIVHVSTFY ANCDRPYIEE
RIYDDVPYGG LEHIQLFFKS LSVEEKERMT RVVLGDMPNS YVFSKKCAEA MVGREFGHLP
IGIFRPPIVI SSYREPEPGW VDCFHGATGL CVPVVLGKTM WYYGKPEVKP FMSPVDHTVS
GMLAAACDIY RRQCTILPVE KPVPVYNFTF EKNRFAYGDM VELVCSGLPN VLDRWLSRIK
CRISPWKIFP QMLLWLMTLQ ARIADEILAW FGKRGSNVKI VSAITTLSNA VEYFRCHMWT
MDNSNVKRML SLLSRDDAKR LDFDGEQIDW RDYHKSYAKG IAMELMRKND RRKSSKAANR
A
//
