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Database: UniProt
Entry: A0A0N4SX79_BRUPA
LinkDB: A0A0N4SX79_BRUPA
Original site: A0A0N4SX79_BRUPA 
ID   A0A0N4SX79_BRUPA        Unreviewed;       546 AA.
AC   A0A0N4SX79;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, 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};
GN   ORFNames=BPAG_LOCUS270 {ECO:0000313|EMBL:VDN81456.1};
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000026901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BPAG_0000026901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN81456.1, ECO:0000313|Proteomes:UP000278627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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   EMBL; UZAD01000011; VDN81456.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4SX79; -.
DR   STRING; 6280.A0A0N4SX79; -.
DR   WBParaSite; BPAG_0000026901-mRNA-1; BPAG_0000026901-mRNA-1; BPAG_0000026901.
DR   Proteomes; UP000038020; Unplaced.
DR   Proteomes; UP000278627; 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:SF45; 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   Reference proteome {ECO:0000313|Proteomes:UP000278627};
KW   Transmembrane {ECO:0000256|RuleBase:RU363097};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT   TRANSMEM        483..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363097"
FT   DOMAIN          18..303
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
FT   DOMAIN          375..466
FT                   /note="Fatty acyl-CoA reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03015"
SQ   SEQUENCE   546 AA;  62818 MW;  AD96555271D0BB29 CRC64;
     MGHSQQVTDI YADQSVLVTG ASGFLGKVLI EKLLYSVNSL KNIYLLIRPK NGLGPKQRMD
     TIVQGPLFDR LRRSNPGIFS KLIPIGGDIM EEGLGLNQLD MQTICDEVSI VFHCAATVKF
     DEALRISVEM NVLGTQRLVA LCHMIKNLLV LVHVSTAYAN CDKSKILEII YPPPVPPNKL
     FEAIDWMDDV VIDAITPHLL GKRPNTYTLT KALAEVQLME DARQLPVIIV RPSIIGAMWR
     DPLPGWTDNY NGPTGIFAAV GFISLITGID QRHLCGKGVL TNMCGSSSAK ADIIPVDIVS
     NLMIVAAAHR TYTEYESIPV IHCCSGALNP IQWDFIVNFI EHFFRTYPLN ECYRIPSTHF
     HSSRLLFEFN FYLKHMGPAY LIDLLNTFWG PKIRFTRVYQ KVLRLVETLH YFTTRGWDFD
     SKSLIELWET TSEEDKKIFN FDIRQLDWNS YLFDYLMGVK RYVVKDKLEE LPKARRNLSW
     LKIYAAVFNA LIWWISVRIF ARQRSRRYRW FSGSVGFLLT YIWSNYNFRP PVRLKSLEEY
     KQRATF
//
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