ID A0A182M7X1_9DIPT Unreviewed; 493 AA.
AC A0A182M7X1;
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 culicifacies.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; culicifacies species complex.
OX NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA011671-PA, ECO:0000313|Proteomes:UP000075883};
RN [1] {ECO:0000313|Proteomes:UP000075883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
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 culicifacies species A.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACUA011671-PA}
RP IDENTIFICATION.
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA011671-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|RuleBase:RU363097}.
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DR EMBL; AXCM01002370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182M7X1; -.
DR STRING; 139723.A0A182M7X1; -.
DR EnsemblMetazoa; ACUA011671-RA; ACUA011671-PA; ACUA011671.
DR VEuPathDB; VectorBase:ACUA011671; -.
DR OrthoDB; 1434498at2759; -.
DR Proteomes; UP000075883; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR026055; FAR.
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 SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU363097};
KW Lipid metabolism {ECO:0000256|RuleBase:RU363097};
KW 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 379..397
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT TRANSMEM 456..480
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 36..305
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
SQ SEQUENCE 493 AA; 56427 MW; 0085DA0C62D6A20E CRC64;
MHTFSNHPIG LLPMEQNYDP AKPSIAEFFS GRDIFVTGGT GFMGKVLIEK LLRSCSELNK
IYILIREKKQ KSIKERILEM QQLPLFDKLR EEQPELLDKM VPVQGDVSLL GLGLSQNDIE
MMRNVSVIFH VAASVRFDDP LKTAILLNTR GTRELVQFAE QLPALRVLMH VSSTYSNPDR
YVIEEEVYPA YADWRDTIRI AETFDEQTLD VLAPKYMGFL PNTYVFTKSL AEQIVNEHKD
RLPMILFRPS IVISSMKDPI PGWMDNFNGP VGLLVGCGIG ICRTMYCDPN NIADFTPVDV
CIKAMIVAAW KRGTEPVPST ANQDLPIYNC CISNLRNSTM SQIVEMGRTL SDEIPLDKCI
WAPGGGITQI RIHNLIRVLL YHILPAILID GIFRLMGQKP FKDFYYRDFI EFDVTLYFRN
CILGARRYLL KEKDENIPRA LTHLKRMKLL DKICKSIIVA VFLYIILIQF DMLGMILYLI
SYKPSYALEV DCK
//
