ID   FAR_SIMCH               Reviewed;         493 AA.
AC   Q9XGY7;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Alcohol-forming fatty acyl-CoA reductase;
DE            EC=1.2.1.84;
OS   Simmondsia chinensis (Jojoba) (Buxus chinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Simmondsiaceae; Simmondsia.
OX   NCBI_TaxID=3999;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10712526; DOI=10.1104/pp.122.3.635;
RA   Metz J.G., Pollard M.R., Anderson L., Hayes T.R., Lassner M.W.;
RT   "Purification of a jojoba embryo fatty acyl-coenzyme A reductase and
RT   expression of its cDNA in high erucic acid rapeseed.";
RL   Plant Physiol. 122:635-644(2000).
CC   -!- FUNCTION: NADPH-dependent alcohol-forming fatty acyl-coenzyme A
CC       reductase that catalyzes the reduction of fatty acyl-CoA to fatty
CC       alcohols. The recombinant enzyme accepts saturated and mono-unsaturated
CC       fatty acyl-CoAs of 16 to 22 carbons. {ECO:0000269|PubMed:10712526}.
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:0000269|PubMed:10712526};
CC   -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AF149917; AAD38039.1; -; mRNA.
DR   AlphaFoldDB; Q9XGY7; -.
DR   PRIDE; Q9XGY7; -.
DR   KEGG; ag:AAD38039; -.
DR   BioCyc; MetaCyc:MON-13889; -.
DR   BRENDA; 1.2.1.84; 5733.
DR   GO; GO:0102965; F:alcohol-forming fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0080019; F:fatty-acyl-CoA reductase (alcohol-forming) activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd09071; FAR_C; 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; PTHR11011; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF03015; Sterile; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase.
FT   CHAIN           1..493
FT                   /note="Alcohol-forming fatty acyl-CoA reductase"
FT                   /id="PRO_0000421755"
SQ   SEQUENCE   493 AA;  56167 MW;  F2978E0D763A5C13 CRC64;
     MEEMGSILEF LDNKAILVTG ATGSLAKIFV EKVLRSQPNV KKLYLLLRAT DDETAALRLQ
     NEVFGKELFK VLKQNLGANF YSFVSEKVTV VPGDITGEDL CLKDVNLKEE MWREIDVVVN
     LAATINFIER YDVSLLINTY GAKYVLDFAK KCNKLKIFVH VSTAYVSGEK NGLILEKPYY
     MGESLNGRLG LDINVEKKLV EAKINELQAA GATEKSIKST MKDMGIERAR HWGWPNVYVF
     TKALGEMLLM QYKGDIPLTI IRPTIITSTF KEPFPGWVEG VRTIDNVPVY YGKGRLRCML
     CGPSTIIDLI PADMVVNATI VAMVAHANQR YVEPVTYHVG SSAANPMKLS ALPEMAHRYF
     TKNPWINPDR NPVHVGRAMV FSSFSTFHLY LTLNFLLPLK VLEIANTIFC QWFKGKYMDL
     KRKTRLLLRL VDIYKPYLFF QGIFDDMNTE KLRIAAKESI VEADMFYFDP RAINWEDYFL
     KTHFPGVVEH VLN