ID B0WYI0_CULQU Unreviewed; 453 AA.
AC B0WYI0;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN Name=6045033 {ECO:0000313|EnsemblMetazoa:CPIJ012073-PA};
GN ORFNames=CpipJ_CPIJ012073 {ECO:0000313|EMBL:EDS37057.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS37057.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS37057.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ012073-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ012073-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) 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; DS232189; EDS37057.1; -; Genomic_DNA.
DR RefSeq; XP_001862452.1; XM_001862417.1.
DR AlphaFoldDB; B0WYI0; -.
DR STRING; 7176.B0WYI0; -.
DR EnsemblMetazoa; CPIJ012073-RA; CPIJ012073-PA; CPIJ012073.
DR KEGG; cqu:CpipJ_CPIJ012073; -.
DR VEuPathDB; VectorBase:CPIJ012073; -.
DR VEuPathDB; VectorBase:CQUJHB004476; -.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_024661_0_1_1; -.
DR InParanoid; B0WYI0; -.
DR OMA; REWTIAN; -.
DR OrthoDB; 3469512at2759; -.
DR Proteomes; UP000002320; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320}.
FT DOMAIN 37..224
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 308..398
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 453 AA; 52385 MW; F8489704B14E4966 CRC64;
MDALYAKVEA VQIDLNNGTT LFPRDDMGDD DTSPIEERLL AETEIIFNVL ASVKFNESIR
NALATNVGGT GKVLQLAKRM PRLRSVVHVS TLYSNCHRTD IEERVYDDIP MDHGMILQLT
NALSEQEMDR FQHCFLGPMP NTYTFSKKCA EVMIQKDYSQ LPIGIFRPPI VISTYQEPMP
GWTDNLNGPS GVCMWTVKGL IHTIWGGAGK RANLVPVDYC VNGIIVAAYD IWRRSRRRVA
GTAKAVDEEN SQLLPTYNYM YPAFSLTWGK YMDMVHLGFE SRLHQMVWNY SYIITSYGPL
FRALSFCFHT VPAFVLDVVQ RIRRKKPIYR KAMQKTGRFL ELMSYFGTRE WTIANENVRR
LRGLLSADES RLLEFDMGTI NWAEYFRTYI PGIRRYCFLE GAVRGDRWKP AANRRFQFMK
RLVQKLVWIW VCLRMTRVTS KFVAENLFAL LIA
//
