Dihydrolipoyl dehydrogenase

Details

Name
Dihydrolipoyl dehydrogenase
Synonyms
  • 1.8.1.4
  • Dihydrolipoamide dehydrogenase
  • E3 component of branched-chain alpha-keto acid dehydrogenase complex
  • LPD-Val
Gene Name
lpdV
Organism
Pseudomonas putida
Amino acid sequence
>lcl|BSEQ0011858|Dihydrolipoyl dehydrogenase
MQQTIQTTLLIIGGGPGGYVAAIRAGQLGIPTVLVEGQALGGTCLNIGCIPSKALIHVAE
QFHQASRFTEPSPLGISVASPRLDIGQSVAWKDGIVDRLTTGVAALLKKHGVKVVHGWAK
VLDGKQVEVDGQRIQCEHLLLATGSSSVELPMLPLGGPVISSTEALAPKALPQHLVVVGG
GYIGLELGIAYRKLGAQVSVVEARERILPTYDSELTAPVAESLKKLGIALHLGHSVEGYE
NGCLLANDGKGGQLRLEADRVLVAVGRRPRTKGFNLECLDLKMNGAAIAIDERCQTSMHN
VWAIGDVAGEPMLAHRAMAQGEMVAEIIAGKARRFEPAAIAAVCFTDPEVVVVGKTPEQA
SQQGLDCIVAQFPFAANGRAMSLESKSGFVRVVARRDNHLILGWQAVGVAVSELSTAFAQ
SLEMGACLEDVAGTIHAHPTLGEAVQEAALRALGHALHI
Number of residues
459
Molecular Weight
48158.33
Theoretical pI
6.79
GO Classification
Functions
dihydrolipoyl dehydrogenase activity / flavin adenine dinucleotide binding
Processes
cell redox homeostasis / glycolytic process
Components
cytoplasm
General Function
Flavin adenine dinucleotide binding
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 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0005130|1380 bp
ATGCAACAGACTATCCAGACAACCCTGTTGATCATCGGCGGCGGCCCTGGCGGCTATGTG
GCGGCCATCCGCGCCGGGCAACTGGGCATCCCTACCGTGCTGGTGGAAGGCCAGGCGCTG
GGCGGTACCTGCCTGAACATCGGCTGCATTCCGTCCAAGGCGCTGATCCATGTGGCCGAG
CAGTTCCACCAGGCCTCGCGCTTTACCGAACCCTCGCCGCTGGGCATCAGCGTGGCTTCG
CCACGCCTGGACATCGGCCAGAGCGTGGCCTGGAAAGACGGCATCGTCGATCGCCTGACC
ACTGGTGTCGCCGCCCTGCTGAAAAAGCACGGGGTGAAGGTGGTGCACGGCTGGGCCAAG
GTGCTTGATGGCAAGCAGGTCGAGGTGGATGGCCAGCGCATCCAGTGCGAGCACCTGTTG
CTGGCCACGGGCTCCAGCAGTGTCGAACTGCCGATGCTGCCGTTGGGTGGGCCGGTGATT
TCCTCGACCGAGGCCCTGGCACCGAAAGCCCTGCCGCAACACCTGGTGGTGGTGGGCGGT
GGCTACATCGGCCTGGAGCTGGGTATCGCCTACCGCAAGCTCGGCGCGCAGGTCAGCGTG
GTGGAAGCGCGCGAGCGCATCCTGCCGACTTACGACAGCGAACTGACCGCCCCGGTGGCC
GAGTCGCTGAAAAAGCTGGGTATCGCCCTGCACCTTGGCCACAGCGTCGAAGGTTACGAA
AATGGCTGCCTGCTGGCCAACGATGGCAAGGGCGGACAACTGCGCCTGGAAGCCGACCGG
GTGCTGGTGGCCGTGGGCCGCCGCCCACGCACCAAGGGCTTCAACCTGGAATGCCTGGAC
CTGAAGATGAATGGTGCCGCGATTGCCATCGACGAGCGCTGCCAGACCAGCATGCACAAC
GTCTGGGCCATCGGCGACGTGGCCGGCGAACCGATGCTGGCGCACCGGGCCATGGCCCAG
GGCGAGATGGTGGCCGAGATCATCGCCGGCAAGGCACGCCGCTTCGAACCCGCTGCGATA
GCCGCCGTGTGCTTCACCGACCCGGAAGTGGTCGTGGTCGGCAAGACGCCGGAACAGGCC
AGTCAGCAAGGCCTGGACTGCATCGTCGCGCAGTTCCCGTTCGCCGCCAACGGCCGGGCC
ATGAGCCTGGAGTCGAAAAGCGGTTTCGTGCGCGTGGTCGCGCGGCGTGACAACCACCTG
ATCCTGGGCTGGCAAGCGGTTGGCGTGGCGGTTTCCGAGCTGTCCACGGCGTTTGCCCAG
TCGCTGGAGATGGGTGCCTGCCTGGAGGATGTGGCCGGTACCATCCATGCCCACCCGACC
CTGGGTGAAGCGGTACAGGAAGCGGCACTGCGTGCCCTGGGCCACGCCCTGCATATCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP09063
UniProtKB Entry NameDLDH1_PSEPU
GenBank Gene IDM57613
General References
  1. Burns G, Brown T, Hatter K, Sokatch JR: Comparison of the amino acid sequences of the transacylase components of branched chain oxoacid dehydrogenase of Pseudomonas putida, and the pyruvate and 2-oxoglutarate dehydrogenases of Escherichia coli. Eur J Biochem. 1988 Sep 1;176(1):165-9. [Article]
  2. Burns G, Brown T, Hatter K, Sokatch JR: Sequence analysis of the lpdV gene for lipoamide dehydrogenase of branched-chain-oxoacid dehydrogenase of Pseudomonas putida. Eur J Biochem. 1989 Jan 15;179(1):61-9. [Article]
  3. Mattevi A, Obmolova G, Sokatch JR, Betzel C, Hol WG: The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 A resolution. Proteins. 1992 Aug;13(4):336-51. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03147Flavin adenine dinucleotideapprovedunknownDetails