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Identification
HMDB Protein ID HMDBP03078
Secondary Accession Numbers
  • 8614
Name Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
Synonyms
  1. BCKAD-E2
  2. BCKADE2
  3. Branched-chain alpha-keto acid dehydrogenase complex component E2
  4. Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex
  5. Dihydrolipoamide branched chain transacylase
  6. Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
Gene Name DBT
Protein Type Enzyme
Biological Properties
General Function Involved in acyltransferase activity
Specific Function The 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).
Pathways
  • 2-Methyl-3-Hydroxybutryl CoA Dehydrogenase Deficiency
  • 3-Hydroxy-3-Methylglutaryl-CoA Lyase Deficiency
  • 3-hydroxyisobutyric acid dehydrogenase deficiency
  • 3-hydroxyisobutyric aciduria
  • 3-Methylcrotonyl Coa Carboxylase Deficiency Type I
  • 3-Methylglutaconic Aciduria Type I
  • 3-Methylglutaconic Aciduria Type III
  • 3-Methylglutaconic Aciduria Type IV
  • Beta-Ketothiolase Deficiency
  • Isobutyryl-coa dehydrogenase deficiency
  • Isovaleric acidemia
  • Isovaleric Aciduria
  • Maple Syrup Urine Disease
  • Methylmalonate Semialdehyde Dehydrogenase Deficiency
  • Methylmalonic Aciduria
  • Propionic Acidemia
  • Threonine and 2-Oxobutanoate Degradation
  • Valine, Leucine and Isoleucine Degradation
  • Valine, leucine and isoleucine degradation
Reactions
Isobutyryl-CoA + enzyme N(6)-(dihydrolipoyl)lysine → Coenzyme A + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine details
GO Classification
Biological Process
branched-chain amino acid catabolic process
cellular nitrogen compound metabolic process
fatty-acyl-CoA biosynthetic process
Cellular Component
microtubule cytoskeleton
mitochondrial alpha-ketoglutarate dehydrogenase complex
mitochondrial nucleoid
Function
binding
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
acyltransferase activity
protein binding
cofactor binding
dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity
Molecular Function
dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity
cofactor binding
Process
acyl-coa metabolic process
metabolic process
cellular metabolic process
fatty-acyl-coa metabolic process
fatty-acyl-coa biosynthetic process
cofactor metabolic process
coenzyme metabolic process
Cellular Location
  1. Mitochondrion matrix
Gene Properties
Chromosome Location 1
Locus 1p31
SNPs DBT
Gene Sequence
>1449 bp
ATGGCTGCAGTCCGTATGCTGAGAACCTGGAGCAGGAATGCGGGGAAGCTGATTTGTGTT
CGCTATTTTCAAACATGTGGTAATGTTCATGTTTTGAAGCCAAATTATGTGTGTTTCTTT
GGTTATCCTTCATTCAAGTATAGTCATCCACATCACTTCCTGAAAACAACTGCTGCTCTC
CGTGGACAGGTTGTTCAGTTCAAGCTCTCAGACATTGGAGAAGGGATTAGAGAAGTAACT
GTTAAAGAATGGTATGTAAAAGAAGGAGATACAGTGTCTCAGTTTGATAGCATCTGTGAA
GTTCAAAGTGATAAAGCTTCTGTTACCATCACTAGTCGTTATGATGGAGTCATTAAAAAA
CTCTATTATAATCTAGACGATATTGCCTATGTGGGGAAGCCATTAGTAGACATAGAAACG
GAAGCTTTAAAAGATTCAGAAGAAGATGTTGTTGAAACTCCTGCAGTGTCTCATGATGAA
CATACACACCAAGAGATAAAGGGCCGAAAAACACTGGCAACTCCTGCAGTTCGCCGTCTG
GCAATGGAAAACAATATTAAGCTGAGTGAAGTTGTTGGCTCAGGAAAAGATGGCAGAATA
CTTAAAGAAGATATCCTCAACTATTTGGAAAAGCAGACAGGAGCTATATTGCCTCCTTCA
CCCAAAGTTGAAATTATGCCACCTCCACCAAAGCCAAAAGACATGACTGTTCCTATACTA
GTATCAAAACCTCCGGTATTCACAGGCAAAGACAAAACAGAACCCATAAAAGGCTTTCAA
AAAGCAATGGTCAAGACTATGTCTGCAGCCCTGAAGATACCTCATTTTGGTTATTGTGAT
GAGATTGACCTTACTGAACTGGTTAAGCTCCGAGAAGAATTAAAACCCATTGCATTTGCT
CGTGGAATTAAACTCTCCTTTATGCCTTTCTTCTTAAAGGCTGCTTCCTTGGGATTACTA
CAGTTTCCTATCCTTAACGCTTCTGTGGATGAAAACTGCCAGAATATAACATATAAGGCT
TCTCATAACATTGGGATAGCAATGGATACTGAGCAGGGTTTGATTGTCCCTAATGTGAAA
AATGTTCAGATCTGCTCTATATTTGACATCGCCACTGAACTGAACCGCCTCCAGAAATTG
GGCTCTGTGGGTCAGCTCAGCACCACTGATCTTACAGGAGGAACATTTACTCTTTCCAAC
ATTGGATCAATTGGTGGTACCTTTGCCAAACCAGTGATAATGCCACCTGAAGTAGCCATT
GGGGCCCTTGGATCAATTAAGGCCATTCCCCGATTTAACCAGAAAGGAGAAGTATATAAG
GCACAGATAATGAATGTGAGCTGGTCAGCTGATCACAGAGTTATTGATGGTGCTACAATG
TCACGCTTCTCCAATTTGTGGAAATCCTATTTAGAAAACCCAGCTTTTATGCTACTAGAT
CTGAAATGA
Protein Properties
Number of Residues 482
Molecular Weight 53486.635
Theoretical pI 8.518
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
MAAVRMLRTWSRNAGKLICVRYFQTCGNVHVLKPNYVCFFGYPSFKYSHPHHFLKTTAAL
RGQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKK
LYYNLDDIAYVGKPLVDIETEALKDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRL
AMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKVEIMPPPPKPKDMTVPIL
VSKPPVFTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEIDLTELVKLREELKPIAFA
RGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVK
NVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTFAKPVIMPPEVAI
GALGSIKAIPRFNQKGEVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLD
LK
GenBank ID Protein 189053756
UniProtKB/Swiss-Prot ID P11182
UniProtKB/Swiss-Prot Entry Name ODB2_HUMAN
PDB IDs
GenBank Gene ID AK313191
GeneCard ID DBT
GenAtlas ID DBT
HGNC ID HGNC:2698
References
General References
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  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  5. Wynn RM, Kochi H, Cox RP, Chuang DT: Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence. Biochim Biophys Acta. 1994 Sep 28;1201(1):125-8. [PubMed:7918575 ]
  6. Lau KS, Chuang JL, Herring WJ, Danner DJ, Cox RP, Chuang DT: The complete cDNA sequence for dihydrolipoyl transacylase (E2) of human branched-chain alpha-keto acid dehydrogenase complex. Biochim Biophys Acta. 1992 Oct 20;1132(3):319-21. [PubMed:1420314 ]
  7. Hummel KB, Litwer S, Bradford AP, Aitken A, Danner DJ, Yeaman SJ: Nucleotide sequence of a cDNA for branched chain acyltransferase with analysis of the deduced protein structure. J Biol Chem. 1988 May 5;263(13):6165-8. [PubMed:3245861 ]
  8. Danner DJ, Litwer S, Herring WJ, Pruckler J: Construction and nucleotide sequence of a cDNA encoding the full-length preprotein for human branched chain acyltransferase. J Biol Chem. 1989 May 5;264(13):7742-6. [PubMed:2708389 ]
  9. Nobukuni Y, Mitsubuchi H, Endo F, Matsuda I: Complete primary structure of the transacylase (E2b) subunit of the human branched chain alpha-keto acid dehydrogenase complex. Biochem Biophys Res Commun. 1989 Jun 30;161(3):1035-41. [PubMed:2742576 ]
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