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Database: UniProt
Entry: A0A0D3DTP9_BRAOL
LinkDB: A0A0D3DTP9_BRAOL
Original site: A0A0D3DTP9_BRAOL 
ID   A0A0D3DTP9_BRAOL        Unreviewed;       544 AA.
AC   A0A0D3DTP9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE            EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo8g091020.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo8g091020.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo8g091020.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0D3DTP9; -.
DR   STRING; 109376.A0A0D3DTP9; -.
DR   EnsemblPlants; Bo8g091020.1; Bo8g091020.1; Bo8g091020.
DR   Gramene; Bo8g091020.1; Bo8g091020.1; Bo8g091020.
DR   eggNOG; KOG1221; Eukaryota.
DR   HOGENOM; CLU_024661_4_1_1; -.
DR   OMA; QMACNIS; -.
DR   Proteomes; UP000032141; Chromosome C8.
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:SF101; 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:UP000032141}.
FT   DOMAIN          81..374
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
FT   DOMAIN          471..539
FT                   /note="Fatty acyl-CoA reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03015"
SQ   SEQUENCE   544 AA;  61342 MW;  9530DEE5F2EA5E8D CRC64;
     MAISNLLATI NAVSFFSGKP DHFLARPLSQ TTPRIQTSCC HREPSFKPWT PIMMSEVETY
     TKSDSHGVGI FRFLQGKSYL ITGATGFLAK VLILKLVRES PEIGNIFILM KTEHQESANK
     RLYDEIISSD LFRLIKQTHG SSYEALMKSK LIPVVGDIGE DNLGIKSQMA YNISDEIDVI
     ISCAGRTTFD YRYDSALNVN ALGPGRLLSF GKGCKKLKLF LHISTAYVTG NKEGKILETP
     LCIGENITSH LNIETEMKLA SEAVRKFYGR EEIKKLKELG MERAQYYGWE NTYTFTKAMG
     ESVIQNQRGD LPVVIIRPSI IESSYKEPFP GWLQGIRMSA PLILAYGKDH IADMWGDYKS
     SCDIIPVDMV ANATIAAMAK HGCGVSETKA YNVTSSSHAN PLRLGESMDF SHQHLCDSPL
     IKTVMELERV KFYNSLEDFT SSVSIRIAKQ EGEMSSGRGE SPTMLSMKGK RKLKYLVSLA
     RTYQPYTFFQ ARFDDTNTRG LIQELSMEER RMFGFNGRDI DWEHYIVNVH LPGLKRELFR
     GRFS
//
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