Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Details
- Name
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Synonyms
- 2.3.1.12
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- E2
- Gene Name
- Not Available
- Organism
- Azotobacter vinelandii
- Amino acid sequence
>lcl|BSEQ0002579|Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex MSEIIRVPDIGGDGEVIELLVKTGDLIEVEQGLVVLESAKASMEVPSPKAGVVKSVSVKL GDKLKEGDAIIELEPAAGAAAAPAEAAAVPAAPTQAVDEAEAPSPGASATPAPAAASQEV RVPDIGSAGKARVIEVLVKAGDQVQAEQSLIVLESDKASMEIPSPASGVVESVAIQLNAE VGTGDLILTLRTTGAQAQPTAPAAAAAASPAPAPLAPAAAGPQEVKVPDIGSAGKARVIE VLVKAGDQVQAEQSLIVLESDKASMEIPSPAAGVVESVAVQLNAEVGTGDQILTLRVAGA APSGPRARGSPGQAAAAPGAAPAPAPVGAPSRNGAKVHAGPAVRQLAREFGVELAAINST GPRGRILKEDVQAYVKAMMQKAKEAPAAGAASGAGIPPIPPVDFAKYGEIEEVPMTRLMQ IGATNLHRSWLNVPHVTQFESADITELEAFRVAQKAVAEKAGVKLTVLPLLLKACAYLLK ELPDFNSSLAPSGQALIRKKYVHIGFAVDTPDGLLVPVIRNVDQKSLLQLAAEAAELAEK ARSKKLGADAMQGACFTISSLGHIGGTAFTPIVNAPEVAILGVSKASMQPVWDGKAFQPR LMLPLSLSYDHRVINGAAAARFTKRLGDLLADIRAILL
- Number of residues
- 638
- Molecular Weight
- 65044.135
- Theoretical pI
- 5.12
- GO Classification
- Functionsdihydrolipoyllysine-residue acetyltransferase activityProcessesglycolytic processComponentspyruvate dehydrogenase complex
- General Function
- Dihydrolipoyllysine-residue acetyltransferase activity
- 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
- Not Available
- Gene sequence
>lcl|BSEQ0002578|1917 bp GTGAGCGAAATCATCCGCGTACCCGATATCGGCGGCGATGGGGAAGTCATCGAATTGCTG GTCAAGACCGGCGACCTCATCGAGGTCGAGCAGGGGCTGGTGGTGCTGGAGTCCGCCAAG GCGAGCATGGAAGTTCCCAGTCCCAAGGCCGGAGTGGTCAAGAGCGTGAGCGTCAAGCTG GGCGACAAGCTCAAGGAAGGCGACGCGATCATCGAGCTGGAACCTGCCGCCGGTGCCGCG GCGGCACCTGCCGAAGCGGCGGCCGTGCCCGCCGCGCCGACCCAGGCCGTCGACGAGGCC GAGGCGCCCTCTCCCGGCGCCTCCGCCACGCCCGCGCCGGCCGCCGCCAGCCAGGAGGTC CGGGTTCCCGACATCGGCTCGGCCGGCAAGGCACGGGTCATCGAGGTGCTGGTCAAGGCC GGCGACCAGGTCCAGGCCGAGCAGTCGCTGATCGTGCTGGAGTCCGACAAGGCCAGCATG GAGATCCCCTCCCCGGCTTCCGGAGTGGTGGAAAGCGTCGCCATCCAGTTGAACGCCGAG GTCGGCACCGGCGACCTGATCCTCACCCTGCGCACCACCGGCGCCCAGGCCCAGCCTACG GCGCCCGCCGCGGCCGCGGCCGCGAGCCCGGCACCCGCTCCGCTGGCTCCGGCCGCCGCC GGTCCCCAGGAAGTCAAGGTCCCGGACATCGGCTCGGCCGGCAAGGCACGGGTCATCGAG GTGCTGGTCAAGGCCGGCGACCAGGTCCAGGCCGAACAGTCGCTGATCGTGCTGGAATCC GACAAGGCCAGCATGGAGATCCCCTCCCCGGCCGCCGGGGTGGTGGAAAGCGTCGCCGTC CAGTTGAACGCCGAGGTCGGCACCGGCGATCAGATCCTCACCCTGCGCGTCGCCGGCGCC GCGCCGAGCGGCCCCCGCGCCCGCGGCAGCCCCGGCCAAGCCGCCGCCGCTGCGGCCGCT GCCCCGGCTCCGGCCCCGGTCGGCGCACCGAGCCGCAACGGCGCCAAGGTGCATGCCGGC CCCGCCGTGCGCCAACTGGCCCGCGAGTTCGGCGTCGAACTGGCGGCGATCAACAGCACC GGTCCGCGCGGGCGCATCCTCAAGGAGGACGTGCAGGCCTACGTCAAGGCGATGATGCAG AAGGCCAAGGAGGCGCCGGCCGCCGGCGCGGCCAGCGGCGCCGGCATCCCGCCGATTCCG CCGGTCGACTTCGCCAAGTACGGCGAAATCGAAGAAGTGCCGATGACTCGCCTGATGCAG ATCGGCGCGACCAACCTGCACCGCAGTTGGCTGAACGTGCCGCACGTGACCCAGTTCGAG TCGGCCGATATCACCGAGCTGGAAGCCTTCCGCGTCGCGCAGAAGGCCGTCGCCGAGAAG GCCGGGGTCAAGCTGACCGTGCTGCCGCTGCTGCTCAAGGCCTGCGCCTACCTGCTCAAG GAGCTGCCGGACTTCAACAGCTCCCTGGCACCCAGCGGCCAGGCGCTGATCCGCAAGAAG TACGTGCACATCGGCTTCGCCGTGGACACCCCGGACGGCCTGCTGGTGCCGGTAATCCGC AACGTCGACCAGAAGAGCCTGCTGCAACTGGCCGCCGAGGCCGCCGAACTGGCGGAGAAG GCGCGCAGCAAGAAGCTCGGCGCCGACGCCATGCAGGGTGCCTGCTTCACCATCTCCAGC CTCGGCCACATCGGCGGCACGGCCTTCACGCCGATCGTCAACGCCCCGGAAGTGGCGATC CTCGGCGTGTCCAAGGCCAGCATGCAGCCGGTATGGGACGGCAAGGCCTTCCAGCCGCGC CTGATGCTGCCGCTGTCGCTGTCCTACGATCACCGGGTGATCAACGGCGCCGCCGCGGCG CGCTTCACCAAGCGTCTCGGCGACCTGCTGGCGGATATCCGCGCCATCCTGCTGTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P10802 UniProtKB Entry Name ODP2_AZOVI GenBank Protein ID 580740 GenBank Gene ID X12455 - General References
- Hanemaaijer R, Janssen A, de Kok A, Veeger C: The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Molecular cloning and sequence analysis. Eur J Biochem. 1988 Jul 1;174(4):593-9. [Article]
- Hanemaaijer R, de Kok A, Jolles J, Veeger C: The domain structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Eur J Biochem. 1987 Dec 1;169(2):245-52. [Article]
- Hanemaaijer R, Vervoort J, Westphal AH, de Kok A, Veeger C: Mobile sequences in the pyruvate dehydrogenase complex, the E2 component, the catalytic domain and the 2-oxoglutarate dehydrogenase complex of Azotobacter vinelandii, as detected by 600 MHz 1H-NMR spectroscopy. FEBS Lett. 1988 Nov 21;240(1-2):205-10. [Article]
- Mattevi A, Obmolova G, Schulze E, Kalk KH, Westphal AH, de Kok A, Hol WG: Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex. Science. 1992 Mar 20;255(5051):1544-50. [Article]
- Berg A, de Kok A, Vervoort J: Sequential 1H and 15N nuclear magnetic resonance assignments and secondary structure of the N-terminal lipoyl domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Eur J Biochem. 1994 Apr 1;221(1):87-100. [Article]
- Berg A, Vervoort J, de Kok A: Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Eur J Biochem. 1997 Mar 1;244(2):352-60. [Article]