ID M8A2M7_TRIUA Unreviewed; 510 AA.
AC M8A2M7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN ORFNames=TRIUR3_32321 {ECO:0000313|EMBL:EMS54669.1};
OS Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS54669.1};
RN [1] {ECO:0000313|EMBL:EMS54669.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23535596; DOI=10.1038/nature11997;
RA Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D.,
RA Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., Wang B.,
RA Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., Zhang X.,
RA Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., Tang D.,
RA Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., An X., Dong Z.,
RA Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., Wang J., Yang H., Li Z.,
RA Wang D., Zhang A., Wang J.;
RT "Draft genome of the wheat A-genome progenitor Triticum urartu.";
RL Nature 496:87-90(2013).
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; KD179285; EMS54669.1; -; Genomic_DNA.
DR AlphaFoldDB; M8A2M7; -.
DR STRING; 4572.M8A2M7; -.
DR eggNOG; KOG1221; Eukaryota.
DR OMA; NCVTEHI; -.
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}.
FT DOMAIN 17..333
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 408..508
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 510 AA; 58250 MW; D4EB2C817264AD14 CRC64;
MDADMVVGYF GGKSMLITGS TGFLGKADQL RELYSGCFDA RAVLVEKILR VQPDVKKLFL
LVRAPDIESA KLRIQTEVTG REIFLVLKEK HGMGFDDFIE EKICPLAGDI MYENFGLDTA
NLRELSKDID IIVNIAATTN FSERYDVAFD ANVLGAKHVC AFARKCTKLK MLLHVSTAYV
AGELEGLILE KPFLMGETLK EGTHLDIESE LNLIRETRRE LKANCSLEKA ERRTMKELGL
KRARQFGWPN TYVFTKAMGE MLLGHLRGEL PVVILRPSII TSILKEPLPG WMEGIRTIDA
VVIGYAKQTL PFFLVDLSLI MDVIPGDMVV NAMMVAMAAH SEERAQTIYH VTSSLRNPAP
YAILADTGHR YFYDNPPRTG RKGEPARLNK MRFFSTVARL SLYMAVRYRL PLEMLRLVNI
ALCGVFSRRY DDLRRKYRFI VQLIELYAPY SLFKGCFDDM NTERLRMAMK KEQDENGAEE
YYFDFDPKSI NWDSYFYGVH IPGVLKYMRD
//