LIPID MAPS® Gene/Proteome Database (LMPD)

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LMPD Record

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LMP009691

UniProt Annotations

Entry Information
Gene Name3-ketoacyl-CoA synthase 1
Protein EntryKCS1_ARATH
UniProt IDQ9MAM3
SpeciesArabidopsis
Comments
Comment typeDescription
Catalytic ActivityA very-long-chain acyl-CoA + malonyl-CoA = CoA + a very-long-chain 3-oxoacyl-CoA + CO(2).
Catalytic ActivityStearoyl-CoA + malonyl-CoA + 2 NAD(P)H = icosanoyl-CoA + CO(2) + CoA + 2 NAD(P)(+) + H(2)O.
CautionIt is uncertain whether Met-1 or Met-9 is the initiator. {ECO:0000305}.
Disruption PhenotypePlants have thinner stems with an altered wax composition, and are more sensitive to dehydration. {ECO:0000269|PubMed:10074711}.
Enzyme RegulationInhibited by K3 herbicides such as alachlor, allidochlor, anilofos, cafenstrole, fentrazamide and flufenacet. {ECO:0000269|PubMed:15277688}.
FunctionContributes to cuticular wax and suberin biosynthesis. Involved in both decarbonylation and acyl-reduction wax synthesis pathways. Elongase condensing enzyme mostly active with saturated fatty acids, especially with 16:0, 16:1, 18:0, and 20:0. Mediates the synthesis of VLCFAs from 20 to 26 carbons in length (e.g. C20:1, C20, C22, C24 and C26). {ECO:0000269|PubMed:10074711, ECO:0000269|PubMed:15277688, ECO:0000269|PubMed:16765910}.
InductionRepressed by herbicides such as flufenacet and benfuresate. {ECO:0000269|PubMed:12916765}.
PathwayLipid metabolism; fatty acid biosynthesis.
Sequence CautionSequence=BAD95286.1; Type=Erroneous initiation; Evidence={ECO:0000305};
SimilarityBelongs to the chalcone/stilbene synthases family. {ECO:0000305}.
SimilarityContains 1 FAE (fatty acid elongase) domain. {ECO:0000305}.
Subcellular LocationMembrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Tissue SpecificityUbiquitous. {ECO:0000269|PubMed:10074711}.