ID D7LVI8_ARALL Unreviewed; 524 AA.
AC D7LVI8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN ORFNames=ARALYDRAFT_324181 {ECO:0000313|EMBL:EFH54361.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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; GL348717; EFH54361.1; -; Genomic_DNA.
DR RefSeq; XP_002878102.1; XM_002878056.1.
DR AlphaFoldDB; D7LVI8; -.
DR STRING; 81972.D7LVI8; -.
DR EnsemblPlants; fgenesh1_pm.C_scaffold_5001725; fgenesh1_pm.C_scaffold_5001725; fgenesh1_pm.C_scaffold_5001725.
DR Gramene; fgenesh1_pm.C_scaffold_5001725; fgenesh1_pm.C_scaffold_5001725; fgenesh1_pm.C_scaffold_5001725.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_024661_4_1_1; -.
DR Proteomes; UP000008694; 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; 2.
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:SF66; FATTY ACYL-COA REDUCTASE 6, CHLOROPLASTIC; 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:UP000008694}.
FT DOMAIN 87..358
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 457..519
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 524 AA; 58676 MW; 5083435894D81CA4 CRC64;
MAITNLLASS NPVKLDAFSY FSSLSGKQNH YLTCRLTQTT RRVQTSCCNH ETSLKAVTSL
EMHEADTRRN CDGVGILRFL KAKSYLVTGA TGFLAKALIE KLLRASPEIG KIFLLMRSKD
QESANKRPYD EIISSDLFKL LKQTHGSSYE AFMKSKLIPG IGDIGEDNLG IESEIAEMIS
EETDVIINCC GRTTFDDRYD SAINVNALGP AYVTGKKEGI VLETPLCIGE NITSDLNIDS
ELKLASEAVR KFRGSEETKK LKELGFERAQ HYGWENTYTF TKAMGESIIH SKRGDLPVVI
IRPSIIESSY NEPSPGWIQG IRMVDPIIIA YGKGLISGFC ADSTSLMDIT PVDMVANAAI
AVMAKHGSGG VQELKVYNVT SSSHSNPLRF GELMDLSYQH LRNSPLGETV IDLAPMKFHS
SLECFSSSVY NDIRKQERDS HISTLSKKGN RRLDYFVSLA RIYKPYMFFQ ARFDDTNTTT
LIQEMSMEER KMFEFDARGI DWEHYIVNVH IPGLKRQLFQ GRSS
//
