ID A0A182MGT0_9DIPT Unreviewed; 486 AA.
AC A0A182MGT0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
OS Anopheles culicifacies.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; culicifacies species complex.
OX NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA017920-PA, ECO:0000313|Proteomes:UP000075883};
RN [1] {ECO:0000313|Proteomes:UP000075883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
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 culicifacies species A.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACUA017920-PA}
RP IDENTIFICATION.
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA017920-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 EMBL; AXCM01004166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182MGT0; -.
DR STRING; 139723.A0A182MGT0; -.
DR EnsemblMetazoa; ACUA017920-RA; ACUA017920-PA; ACUA017920.
DR VEuPathDB; VectorBase:ACUA017920; -.
DR OrthoDB; 3469512at2759; -.
DR Proteomes; UP000075883; 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 32..294
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 362..432
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 486 AA; 55807 MW; 827D6283A101647A CRC64;
MAACSTDTRR YDVEQSPPDR VLDFYRNTTI LVTGGSGFLG KVLLEKILRC MNVRKVFLAI
RTKDGRTPSE RLQDLLKDAI FDRLRMVTTT EQLLERIEAV EISLEADSSG LGMDGSKEAL
VLQETEVVFN VLASVKFNES IRNAIDTNVG GTRMILQLAR RMHRLKAIVH VSTLYSNCDR
THIEEKVYTD PWLNPDSVLQ LQHCLVGALP NTYTFSKKCA ESLIQQQFAD LPIGIFRPPI
VLSTYREPIA GWTDNLNGPA GLCLWTVKGY VRVILGNGRK KANLVPVDYC VNAMLVAGYD
VADRSIGRQQ KPEHAATGAW ESKQLVPVYN YMYMQPNLTW GRYMSSVSMG FDGWIKRLCC
YRRMVAKTNR FLETMAYFGL REWHIANENV VRLRTLLTPT EASMLEFDLS TVDWDEYFQS
YIPGIRRYFL AEPQLKDRPS RVKSTSWHRR IQFLSQLFHK LIWVYVCLKL GHRLYVVRNL
FSILIS
//
