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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//