ID   A0A182FRU3_ANOAL        Unreviewed;       509 AA.
AC   A0A182FRU3;
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 albimanus (New world malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7167 {ECO:0000313|EnsemblMetazoa:AALB009269-PA, ECO:0000313|Proteomes:UP000069272};
RN   [1] {ECO:0000313|EnsemblMetazoa:AALB009269-PA}
RP   IDENTIFICATION.
RC   STRAIN=STECLA/ALBI9_A {ECO:0000313|EnsemblMetazoa:AALB009269-PA};
RG   EnsemblMetazoa;
RL   Submitted (AUG-2022) 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; A0A182FRU3; -.
DR   STRING; 7167.A0A182FRU3; -.
DR   EnsemblMetazoa; AALB009269-RA; AALB009269-PA; AALB009269.
DR   VEuPathDB; VectorBase:AALB009269; -.
DR   VEuPathDB; VectorBase:AALB20_026355; -.
DR   OrthoDB; 1434498at2759; -.
DR   Proteomes; UP000069272; Chromosome 2R.
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:SF27; FATTY ACYL-COA REDUCTASE CG8306-RELATED; 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        349..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363097"
FT   TRANSMEM        464..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363097"
FT   DOMAIN          16..286
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
FT   DOMAIN          359..450
FT                   /note="Fatty acyl-CoA reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03015"
SQ   SEQUENCE   509 AA;  57741 MW;  AA95CDD98D83B91D CRC64;
     MASEVQSFYK DKYIFLTGGT GFLGVAIIDK ILRSTPEIAG IYLLMRPKKG KAVQERLQDL
     TKNSVFEQLL ETQSADIFKK LIPVAGDVGE DFLGLSQADQ ELIIANTNVV IHSAATLDFQ
     ATLRPTVNIN LLGTKRVLDL CTRMKNLKSM VHISSAYVNS YLTEAEEKLY PCTETSQKVI
     DLVDTLSDTA LDDLLPKLLK DHPNAYTFTK QLAEHEVNKH ASQFPCAIIR PSMITGAWKE
     PTPGWTISKN GPQGFLMGAS KGVIRRLPVG VDLVYDYIPV DAVVNQALCL GWYVATNGFR
     EVKVFHCTSS TTNPFRWRSV IDSMNDYLHK YPLKSAIWYP RLKFVSSLWV YKLSSIFVHI
     LPALVLDFIL RMTGGRPMLM RLHTNVWDSL NRLEKFIFTE WKYYNPATQQ LAQSLSEKDK
     VLFNFNISQL QWPEYFVFLT QGVRRYLNNE HPKSLDAARK KDKILFVVDV VFQVLVFALF
     GALLASLFGS SSSYFWLYGG ISYLLFSLL
//