ID A0A0T6AZY6_9SCAR Unreviewed; 434 AA.
AC A0A0T6AZY6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 03-MAY-2023, entry version 26.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
DE Flags: Fragment;
GN ORFNames=AMK59_7287 {ECO:0000313|EMBL:KRT80507.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT80507.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT80507.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT80507.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT80507.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRT80507.1}.
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DR EMBL; LJIG01022455; KRT80507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6AZY6; -.
DR OrthoDB; 1434498at2759; -.
DR Proteomes; UP000051574; Unassembled WGS sequence.
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:SF107; 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}; NADP {ECO:0000256|RuleBase:RU363097};
KW Oxidoreductase {ECO:0000256|RuleBase:RU363097};
KW Reference proteome {ECO:0000313|Proteomes:UP000051574}.
FT DOMAIN 3..248
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 321..416
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRT80507.1"
FT NON_TER 434
FT /evidence="ECO:0000313|EMBL:KRT80507.1"
SQ SEQUENCE 434 AA; 49858 MW; 1646836A23FBCCCA CRC64;
IDSLYLLIRP KRGMGSEQRL KELFKNPVFN KIRETNPNAL TKVRIIEGDV SQPNLGMSEI
DREKLAEKIN VVFHSAATVR FDENIRNAVI LNTLGTKRVL DFASELKNLK SLVHVSTAYS
NADRREVEEQ VYDPPFDPKS LLNCIDILPD EALDILITKV MGKHPNTYTL TKSMAEYIVF
EYSGKLPVAI VRPSIVTAAW KEPFPGWVDN ISGITGIMME IGRGSIKSIL CKDNMIMDLI
PVDIVANMLV TAAWHTTAYR SNSMRVYNCT SGQINKVSWK DFGSLTQNYA RQYPTKYLSW
YPGFSYRTNR VAHWIHSLVC QTLPACMFDL ILYCTKRKPM MYKISRKFDK ALEIGSFFSL
NEWDFHTTTV KELHEAVDSA EDGENFNIDI SSERGFDWNP YVKDFMLGIR QYVLKDDLSS
LPKARVKMNW FYWA
//
