ID A0A182WR01_9DIPT Unreviewed; 506 AA.
AC A0A182WR01;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 03-MAY-2023, entry version 27.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN015637-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA 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 minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN015637-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN015637-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; A0A182WR01; -.
DR STRING; 112268.A0A182WR01; -.
DR EnsemblMetazoa; AMIN015637-RA; AMIN015637-PA; AMIN015637.
DR VEuPathDB; VectorBase:AMIN015637; -.
DR OrthoDB; 1434498at2759; -.
DR Proteomes; UP000075920; 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:SF61; 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 362..384
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT TRANSMEM 484..505
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 23..295
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 367..459
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 506 AA; 57775 MW; 3F59B8C986D0EAE3 CRC64;
MDVDMNGGRD RIAPMFKDRH VLITGGTGFL GKALIEKLLR CCPEIGQIYL LVRAKKGKSP
RQRLEDIFAN PLFETVKGMR GLDTLISQCT VIGGDVTEPE LAISPEDRKL IAENVSIIYH
CAATIRFDET LKKAVMLNTR GTKYMIDLAK QCKKLDMFGY VSTSYCHLNE KLLLEKPYPP
PADPHKVIKA VEWLEEGVVD GMTKKILGDC PNTYAYTKAL AEALVVESMD EIPAVIFRPS
IVIPTWREPI PGWTDNINGP VGLLIGAGKG VIRSMYCNSD GYGDYLPVDF AVSAMCVCTW
NYVGNQDHKR NIYHLVSSAE IKVSWEGIIE RGKWIVSNKI PLNGVLWYPG GSMKRSRWEH
NLSAFFFHWI PAFLIDCLLY CFGYKPILWR IHQRIAKGFE VFEYYANNQW DFDNATVLYL
RTIINEEEKV KFKIDAGGVE IQEYFENCIR AARWYILKET DDTIPAARRH MRVMWWVDKI
CKTLIYGGLI YYIGKALYSM LFASVF
//
