ID A0A182UTX1_ANOME Unreviewed; 502 AA.
AC A0A182UTX1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 03-MAY-2023, 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 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:AMEM003574-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:AMEM003574-PA}
RP IDENTIFICATION.
RC STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM003574-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; A0A182UTX1; -.
DR STRING; 30066.A0A182UTX1; -.
DR EnsemblMetazoa; AMEM003574-RA; AMEM003574-PA; AMEM003574.
DR VEuPathDB; VectorBase:AMEM003574; -.
DR VEuPathDB; VectorBase:AMEM21_003940; -.
DR OrthoDB; 1434498at2759; -.
DR Proteomes; UP000075903; Unassembled WGS sequence.
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:SF24; 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}; 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 359..379
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT TRANSMEM 476..494
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 22..292
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 368..459
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 502 AA; 57886 MW; 98BFFE3FBD5D2E27 CRC64;
MTTQSGCYES VTDFYANKDV FLTGGTGFLG KVLIEKLLRS CPDIGRIFVL MRNKRGKSIE
TRVTELAACP LFDRLKEENK SALNKVVPVF GDITQLRLGM YEEDIQRLSN VSVAFHLAAS
VRFDDPLRDA IKTNICSTQE LFEMLKATAP QLRAVVHVST AYSNPENRYV EEKLYPPKFD
WKKLVQAVDR YEPETLDALM QKLSQNSPNT YTYTKGLAEQ VCNDYSTELP LAIVRPSVVL
FTIAEPMSGW VDNFNGPTGM LVSAGLGITR TAYLRPKNRI NIIPVDVVVK TIILAAWKRG
TIERACGPKH LPIYNSAVTY EQSLEYQEML DRGKEYLYAV PFSRMLWVPR GYPTDWKTLY
YFKLIFTMLL PSFLLDLLIR MFGHKPFLMK LQSRIYGSEV SLRYFVRNEW EFETKQTDNL
PSLLDEKDRN TFGWYMPRKL TGKYLENAYP TIRRYLMKDP DETIPYAKRK LARMILADRI
ISIIVCCLTL VAIYRRMFAE SL
//
