LIPID MAPS® Gene/Proteome Database (LMPD)

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LMP010553

UniProt Annotations

Entry Information
Gene Namedihydrolipoamide branched chain acyltransferase
Protein EntryODB2_ARATH
UniProt IDQ9M7Z1
SpeciesArabidopsis
Comments
Comment typeDescription
Catalytic Activity2-methylpropanoyl-CoA + enzyme N(6)- (dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2- methylpropanoyl)dihydrolipoyl)lysine.
CofactorName=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250}; Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
Developmental StageBarely detected in non senescent green leaves, accumulated slightly at the early stage of leaf senescence and strongly expressed at the late stage of leaf senescence. {ECO:0000269|PubMed:10681595}.
FunctionThe branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component (By similarity). Required during sugar starvation and acts under the control of a sugar-sensing mechanism involving Ser/Thr kinases and phosphatases. {ECO:0000250, ECO:0000269|PubMed:11080291, ECO:0000269|PubMed:11917081}.
InductionBy dark treatment (at the protein level). Induced by the calmodulin antagonists trifluoperazine and fluphenazine in darkness. Down-regulated by sucrose in a hexokinase dependent manner (at protein level). Up-regulated by Leucine and its derivative alpha-keto acid (KIC). {ECO:0000269|PubMed:10681595, ECO:0000269|PubMed:11080291, ECO:0000269|PubMed:11418132, ECO:0000269|PubMed:11917081, ECO:0000269|PubMed:16100230}.
SimilarityBelongs to the 2-oxoacid dehydrogenase family. {ECO:0000305}.
SimilarityContains 1 E3-binding domain. {ECO:0000305}.
SimilarityContains 1 lipoyl-binding domain. {ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000305}.
Subcellular LocationMitochondrion matrix {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:14764908}.
SubunitForms a 24-polypeptide structural core with octahedral symmetry. {ECO:0000269|PubMed:10933498}.
Tissue SpecificityExpressed in the non-photosynthetic organs such as siliques, flowers and roots. {ECO:0000269|PubMed:10681595}.