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
- Functionsdihydrolipoyl dehydrogenase activity / flavin adenine dinucleotide bindingProcessescell redox homeostasis / glycolytic processComponentscytoplasm
- 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
Resource Link UniProtKB ID P09063 UniProtKB Entry Name DLDH1_PSEPU GenBank Gene ID M57613 - General References
- 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]
- 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]
- 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]