ID A0A0G4GH09_VITBC Unreviewed; 657 AA.
AC A0A0G4GH09;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN ORFNames=Vbra_6260 {ECO:0000313|EMBL:CEM28889.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM28889.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEM28889.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) 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; CDMY01000664; CEM28889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4GH09; -.
DR STRING; 1169540.A0A0G4GH09; -.
DR VEuPathDB; CryptoDB:Vbra_6260; -.
DR InParanoid; A0A0G4GH09; -.
DR OrthoDB; 1434498at2759; -.
DR PhylomeDB; A0A0G4GH09; -.
DR Proteomes; UP000041254; 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:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; 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; 2.
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:UP000041254}.
FT DOMAIN 16..69
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 147..358
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 453..529
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
FT REGION 75..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 657 AA; 72531 MW; 22B7EA60CCA7E1CC CRC64;
MGERTIEFFR EQSILLTGAT GTVGQVVLER LLRCAPPRRV YLLTRSRPKA SGAQRILDLL
QQPLFSAVHR LWEGEGEGER EAHTGSSGPA ASECTSGSRH SNRFWRGNRG SGAEVCGVSG
CRPAPLSTCR GCARRTPEDE ILHRFGIQVM DGDLQKDNLG LSESDLDTLR ANVTVVVNCA
ASINFDDPFP QLFEQNVSGA LRVLQLARAC DGVRSSGCFV HVSTAYANSN RRGVIEEKLY
ESDIDHEHTF SELNRTTGEE HQRLAEQLRV HYGHPNNYTF TKWLAEHLIG SRHGDLPTLI
IRPSIIGSTY RTPFNGWTSA PQGFGALVAL GAFGAFLRLP SDGKAIGDVI PADYVASASL
RATVQMAGRV GRLEVMHVAS SHANPVTWSE LSRQAVKGFD KLRMYQIPQQ YMISPRCVYT
WCSSSWRYAL MHALDDAALV LAQLLVSLLG VVFPALGKQL SKPVRFLCRR QNVLKLLHHF
ICNQWIFKTD KIRELAHREH DPDFPLDVEN IKWEPWCIDY VEGLCRYSLI PTLERITKRE
KEQATHAPDK PTTTTTTHRD TDRDRDSPSS TSTSATTTSS TSLGMCNPCC QSSNHPPESP
PPSPSPVVES DESSEGKGRS DGAPLMSSRK ISGTTTEGDT MALPSDVSND SIERACC
//
