ID   A0A182UMX9_ANOME        Unreviewed;       940 AA.
AC   A0A182UMX9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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:AMEM000627-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:AMEM000627-PA}
RP   IDENTIFICATION.
RC   STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM000627-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; A0A182UMX9; -.
DR   STRING; 30066.A0A182UMX9; -.
DR   EnsemblMetazoa; AMEM000627-RA; AMEM000627-PA; AMEM000627.
DR   VEuPathDB; VectorBase:AMEM000627; -.
DR   VEuPathDB; VectorBase:AMEM21_000162; -.
DR   VEuPathDB; VectorBase:AMEM21_005578; -.
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; 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   PANTHER; PTHR11011:SF60; FATTY ACYL-COA REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR11011; MALE STERILITY PROTEIN 2-RELATED; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF03015; Sterile; 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          24..72
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
FT   DOMAIN          149..241
FT                   /note="Fatty acyl-CoA reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03015"
FT   REGION          910..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   940 AA;  106612 MW;  3C19C54C8E05E9E5 CRC64;
     MVAGTILSSD TMAYAHELLI ATYQEPVPGW IDNFYGPTGV IAGAGTGVLR TLRADPTKVA
     NMVPVDLCVN GIISSAWDIA ERFRTEILPD PEIPIYNFCT EPNNCITWGD FTHTTIKFGS
     MYPTMKAIWY LCYASNPNIV LHYLSIIFLH YAPAVVCDII AVLIGRKPRL LRSYKKIHRF
     MDVIEYFSMR EWEFKMDNMN GLWRKLSSAD QKLFFFDMRQ INWDYFLEQY FCGIRRYLLN
     DPMETVPQAV VRWNRLYWVH QATKVVVLLL LYKLIMSVWE KVEEAAILLK STKRRYRRVH
     LDVQYEPEAD SIEHMQAILD KQLLQQLAVL KLDLPALSGN LAVLLSNVVA KMDCLLELDI
     CYRHQLTNVN LPLSSDLNLI NRSLHKLSLD CAWPARIDCP NMQSLAVKGP FDIEAIVGKQ
     YALHGVREPY WKLKHIKELL IFFIFDHLNL ESLKAVSLTC HRLEEMFADY SARRFVLSTR
     KKTNRKEDLP PLRHVLETME EAVILLQRTK RAYRRFHLDV RCHPKPDSLD DVQAAHEKLL
     ATRLIQQLVV LKLDLGYELH KIAVKLSGVV TKMESLQELY IGHEATDNPY PFSQLTLVNR
     SLQKLLLRNV WPGRIDCPKM GSLNVSVLEI DLGSIIGKQY VQHGGQEPYW KLKQLSELIR
     PRASIAQDST QISPGGMNLP ERAHRDPIIP ASTRAVPICS RGRGGSFDDS SAPYPSSAPK
     YRPITSTHTY RVLQHETNET PILSTGQHTT AFAGRLLERQ YSFDLLPHFS IALIVSVRSS
     VANSRSAGFR AGRLVRFRLL VGGLNGLLSC CVFLCPLLAA DPSSDVLKVV GPQQWLVLDV
     LVELEELHPV GALRLHQPEA AALEKVEQIF HRPTVERALA ALGLEVAVAA PVQPFVRRHA
     QTDDLVALAD GQHGHPGHVQ QRVAHHPADP RIAGTDRLQC
//