ID A0A2G5ET82_AQUCA Unreviewed; 483 AA.
AC A0A2G5ET82;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN ORFNames=AQUCO_00400069v1 {ECO:0000313|EMBL:PIA58953.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA58953.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA58953.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) 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; KZ305021; PIA58953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5ET82; -.
DR STRING; 218851.A0A2G5ET82; -.
DR InParanoid; A0A2G5ET82; -.
DR OrthoDB; 3060211at2759; -.
DR Proteomes; UP000230069; 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 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:SF99; FATTY ACYL-COA REDUCTASE 3; 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:UP000230069}.
FT DOMAIN 11..312
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 386..483
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 483 AA; 54799 MW; 96B65D0547173D33 CRC64;
MESLENKSIL ITGSTGFLAK IFVEKVLRIQ PNVKKLYLVV RAEDIKSAKQ RLHDEVIGKD
LFRVLKEKHG TNFNSFISNK VTPVVGDISC ENLGVKDSDL KEQLWNEVDI IVNIAATVNF
DERYDIALGI NTMGAKHVLD FAKNCVKHEM LLHVSTAYVC GEKSGLILEK PFKMGETLNG
ISGLDIQTEL KLAKEKRNEL QAKQATKEEE STAMKEFGMQ RARFYGWPNT YSFTKAMGEM
LLGDLRGNVP LAIIRPTIIT STYKEPFPGW VEGVRTIDSL AVGYGKGKLT CFLGDFDLIL
DLIPGDMVVN AMIAAMVTHA NQPNEFIYQV GSSLGNPIKC STFKDLAYCY FSKNPWIDKD
GKQVIVTRPI LFTSAASFQR YMAVRYLLPL KGLQVVNAAL CNYFRHTYSS TNRKIKFVLR
LVELYMPYIF FKGIFDDANL EKLRTTVTKP SEANTYYFDP KIIDWEDYFM NVHFPGIVRY
VFK
//
