Dihydrolipoyl dehydrogenase
Details
- Name
- Dihydrolipoyl dehydrogenase
- Synonyms
- 1.8.1.4
- Dihydrolipoamide dehydrogenase
- E3 component of pyruvate complex
- Gene Name
- Not Available
- Organism
- Azotobacter vinelandii
- Amino acid sequence
>lcl|BSEQ0016943|Dihydrolipoyl dehydrogenase MSQKFDVIVIGAGPGGYVAAIKSAQLGLKTALIEKYKGKEGKTALGGTCLNVGCIPSKAL LDSSYKFHEAHESFKLHGISTGEVAIDVPTMIARKDQIVRNLTGGVASLIKANGVTLFEG HGKLLAGKKVEVTAADGSSQVLDTENVILASGSKPVEIPPAPVDQDVIVDSTGALDFQNV PGKLGVIGAGVIGLELGSVWARLGAEVTVLEAMDKFLPAVDEQVAKEAQKILTKQGLKIL LGARVTGTEVKNKQVTVKFVDAEGEKSQAFDKLIVAVGRRPVTTDLLAADSGVTLDERGF IYVDDYCATSVPGVYAIGDVVRGAMLAHKASEEGVVVAERIAGHKAQMNYDLIPAVIYTH PEIAGVGKTEQALKAEGVAINVGVFPFAASGRAMAANDTAGFVKVIADAKTDRVLGVHVI GPSAAELVQQGAIAMEFGTSAEDLGMMVFAHPALSEALHEAALAVSGHAIHVANRKK
- Number of residues
- 477
- Molecular Weight
- 49566.78
- Theoretical pI
- 6.38
- GO Classification
- Functionsdihydrolipoyl dehydrogenase activity / flavin adenine dinucleotide bindingProcessescell redox homeostasis / glycolytic processComponentscytoplasm
- General Function
- Flavin adenine dinucleotide binding
- Specific Function
- The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0005794|1434 bp ATGAGCCAGAAGTTCGACGTGATTGTGATTGGTGCAGGCCCCGGCGGCTACGTGGCTGCC ATCAAGTCTGCCCAGCTTGGCCTCAAGACCGCCCTGATCGAGAAGTACAAGGGCAAGGAA GGCAAGACCGCGCTTGGCGGTACCTGCCTGAACGTGGGCTGCATTCCCTCCAAGGCGCTG CTGGACAGCTCCTACAAGTTCCACGAGGCACACGAGAGCTTCAAGCTCCACGGCATCAGC ACCGGCGAAGTCGCCATCGACGTGCCGACCATGATCGCCCGCAAGGACCAGATCGTCAGA AACCTCACCGGCGGGGTCGCCTCGCTGATCAAGGCCAATGGCGTCACCCTGTTCGAAGGT CATGGCAAGCTGCTGGCCGGCAAGAAGGTCGAAGTCACCGCTGCCGACGGCAGCAGCCAG GTACTCGACACCGAGAACGTCATCCTCGCTTCCGGTTCCAAGCCGGTGGAAATTCCGCCG GCTCCGGTCGATCAGGATGTCATCGTCGACTCCACCGGCGCCCTGGACTTCCAGAACGTT CCGGGCAAACTCGGCGTGATCGGCGCCGGCGTGATCGGCCTGGAGCTGGGTTCGGTCTGG GCTCGCCTGGGTGCCGAGGTCACCGTGCTCGAGGCCATGGACAAGTTCCTGCCGGCCGTC GATGAACAGGTCGCCAAGGAAGCCCAGAAGATTCTCACCAAGCAAGGCCTGAAGATCCTG CTGGGTGCCCGCGTCACCGGCACCGAGGTCAAGAACAAGCAGGTCACCGTCAAGTTCGTC GATGCCGAAGGCGAGAAGTCGCAGGCCTTCGACAAGCTGATCGTCGCGGTCGGCCGCCGC CCGGTGACTACCGACCTGCTGGCCGCCGACAGCGGCGTGACCCTGGACGAGCGTGGCTTC ATCTATGTCGACGACTACTGCGCCACCAGCGTGCCGGGCGTCTATGCCATCGGTGACGTG GTCCGCGGTGCCATGCTGGCCCACAAGGCCTCGGAAGAAGGTGTGGTGGTCGCCGAGCGC ATCGCCGGTCACAAGGCCCAGATGAACTATGACCTGATCCCGGCCGTCATCTACACCCAC CCGGAAATCGCCGGCGTGGGCAAGACCGAGCAGGCTCTGAAGGCCGAAGGCGTGGCCATC AACGTCGGCGTCTTCCCCTTCGCTGCCAGCGGCCGCGCCATGGCCGCCAACGATACCGCA GGCTTCGTCAAGGTCATCGCCGATGCCAAGACCGACCGCGTGCTGGGCGTCCATGTGATC GGCCCGAGCGCCGCCGAACTGGTCCAGCAGGGCGCTATCGCCATGGAGTTCGGCACCAGC GCCGAAGACCTGGGCATGATGGTTTTTGCCCACCCGGCGCTGTCCGAAGCGCTGCACGAG GCCGCCCTGGCGGTCAGCGGCCACGCGATTCACGTTGCCAACCGCAAGAAGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P18925 UniProtKB Entry Name DLDH_AZOVI GenBank Gene ID M37307 - General References
- Westphal AH, de Kok A: Lipoamide dehydrogenase from Azotobacter vinelandii. Molecular cloning, organization and sequence analysis of the gene. Eur J Biochem. 1988 Mar 1;172(2):299-305. [Article]
- Westphal AH, de Kok A: The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component. Eur J Biochem. 1990 Jan 12;187(1):235-9. [Article]
- Mattevi A, Schierbeek AJ, Hol WG: Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 A resolution. A comparison with the structure of glutathione reductase. J Mol Biol. 1991 Aug 20;220(4):975-94. [Article]