Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (P06959)

Identification
Name:Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Synonyms:
  • Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
  • E2
Gene Name:aceF
Enzyme Class:
Biological Properties
General Function:Involved in transferase activity, transferring acyl groups
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)
Cellular Location:Not Available
SMPDB Pathways:
  • glycolysis and pyruvate dehydrogenase PW000785
  • pyruvate decarboxylation to acetyl CoA PW002083
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Enzyme N6-(dihydrolipoyl)lysine+1.0Thumb ↔ 1.0Thumb+1.0[Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine
1.0Acetyl-CoA + 1.0Enzyme N6-(dihydrolipoyl)lysine + 1.0Enzyme N6-(dihydrolipoyl)lysine ↔ 1.0Coenzyme A + 1.0[Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Dihydrolipoamide+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Dihydrolipoamide + 1.0Dihydrolipoamide ↔ 1.0Coenzyme A + 1.0S-Acetyldihydrolipoamide
ReactionCard
1.0Succinyl-CoA+1.0Dihydrolipoamide+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Succinyl-CoA + 1.0Dihydrolipoamide + 1.0Succinyl-CoA + 1.0Dihydrolipoamide → 1.0Coenzyme A + 1.0(S)-Succinyldihydrolipoamide
ReactionCard
1.0a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine+1.0Thumb → 1.0a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine+1.0Thumb
1.0a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + 1.0Coenzyme A → 1.0a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + 1.0Acetyl-CoA
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Coenzyme A + 1.0NAD + 1.0Pyruvic acid → 1.0Acetyl-CoA + 1.0Carbon dioxide + 1.0NADH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB23731(S)-SuccinyldihydrolipoamideMetaboCard
ECMDB01206Acetyl-CoAMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB00985DihydrolipoamideMetaboCard
ECMDB23785Enzyme N6-(dihydrolipoyl)lysineMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB01526S-AcetyldihydrolipoamideMetaboCard
ECMDB01022Succinyl-CoAMetaboCard
GO Classification:
Component
macromolecular complex
protein complex
pyruvate dehydrogenase complex
Function
acetyltransferase activity
acyltransferase activity
binding
catalytic activity
dihydrolipoyllysine-residue acetyltransferase activity
protein binding
S-acetyltransferase activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
Process
alcohol metabolic process
glucose catabolic process
glucose metabolic process
glycolysis
hexose metabolic process
metabolic process
monosaccharide metabolic process
small molecule metabolic process
Gene Properties
Blattner:b0115
Gene OrientationClockwise
Centisome Percentage:2.71
Left Sequence End125695
Right Sequence End127587
Gene Sequence:
>1893 bp
ATGGCTATCGAAATCAAAGTACCGGACATCGGGGCTGATGAAGTTGAAATCACCGAGATC
CTGGTCAAAGTGGGCGACAAAGTTGAAGCCGAACAGTCGCTGATCACCGTAGAAGGCGAC
AAAGCCTCTATGGAAGTTCCGTCTCCGCAGGCGGGTATCGTTAAAGAGATCAAAGTCTCT
GTTGGCGATAAAACCCAGACCGGCGCACTGATTATGATTTTCGATTCCGCCGACGGTGCA
GCAGACGCTGCACCTGCTCAGGCAGAAGAGAAGAAAGAAGCAGCTCCGGCAGCAGCACCA
GCGGCTGCGGCGGCAAAAGACGTTAACGTTCCGGATATCGGCAGCGACGAAGTTGAAGTG
ACCGAAATCCTGGTGAAAGTTGGCGATAAAGTTGAAGCTGAACAGTCGCTGATCACCGTA
GAAGGCGACAAGGCTTCTATGGAAGTTCCGGCTCCGTTTGCTGGCACCGTGAAAGAGATC
AAAGTGAACGTGGGTGACAAAGTGTCTACCGGCTCGCTGATTATGGTCTTCGAAGTCGCG
GGTGAAGCAGGCGCGGCAGCTCCGGCCGCTAAACAGGAAGCAGCTCCGGCAGCGGCCCCT
GCACCAGCGGCTGGCGTGAAAGAAGTTAACGTTCCGGATATCGGCGGTGACGAAGTTGAA
GTGACTGAAGTGATGGTGAAAGTGGGCGACAAAGTTGCCGCTGAACAGTCACTGATCACC
GTAGAAGGCGACAAAGCTTCTATGGAAGTTCCGGCGCCGTTTGCAGGCGTCGTGAAGGAA
CTGAAAGTCAACGTTGGCGATAAAGTGAAAACTGGCTCGCTGATTATGATCTTCGAAGTT
GAAGGCGCAGCGCCTGCGGCAGCTCCTGCGAAACAGGAAGCGGCAGCGCCGGCACCGGCA
GCAAAAGCTGAAGCCCCGGCAGCAGCACCAGCTGCGAAAGCGGAAGGCAAATCTGAATTT
GCTGAAAACGACGCTTATGTTCACGCGACTCCGCTGATCCGCCGTCTGGCACGCGAGTTT
GGTGTTAACCTTGCGAAAGTGAAGGGCACTGGCCGTAAAGGTCGTATCCTGCGCGAAGAC
GTTCAGGCTTACGTGAAAGAAGCTATCAAACGTGCAGAAGCAGCTCCGGCAGCGACTGGC
GGTGGTATCCCTGGCATGCTGCCGTGGCCGAAGGTGGACTTCAGCAAGTTTGGTGAAATC
GAAGAAGTGGAACTGGGCCGCATCCAGAAAATCTCTGGTGCGAACCTGAGCCGTAACTGG
GTAATGATCCCGCATGTTACTCACTTCGACAAAACCGATATCACCGAGTTGGAAGCGTTC
CGTAAACAGCAGAACGAAGAAGCGGCGAAACGTAAGCTGGATGTGAAGATCACCCCGGTT
GTCTTCATCATGAAAGCCGTTGCTGCAGCTCTTGAGCAGATGCCTCGCTTCAATAGTTCG
CTGTCGGAAGACGGTCAGCGTCTGACCCTGAAGAAATACATCAACATCGGTGTGGCGGTG
GATACCCCGAACGGTCTGGTTGTTCCGGTATTCAAAGACGTCAACAAGAAAGGCATCATC
GAGCTGTCTCGCGAGCTGATGACTATTTCTAAGAAAGCGCGTGACGGTAAGCTGACTGCG
GGCGAAATGCAGGGCGGTTGCTTCACCATCTCCAGCATCGGCGGCCTGGGTACTACCCAC
TTCGCGCCGATTGTGAACGCGCCGGAAGTGGCTATCCTCGGCGTTTCCAAGTCCGCGATG
GAGCCGGTGTGGAATGGTAAAGAGTTCGTGCCGCGTCTGATGCTGCCGATTTCTCTCTCC
TTCGACCACCGCGTGATCGACGGTGCTGATGGTGCCCGTTTCATTACCATCATTAACAAC
ACGCTGTCTGACATTCGCCGTCTGGTGATGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:630
Protein Molecular Weight:66096
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
MAIEIKVPDIGADEVEITEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGIVKEIKVS
VGDKTQTGALIMIFDSADGAADAAPAQAEEKKEAAPAAAPAAAAAKDVNVPDIGSDEVEV
TEILVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFEVA
GEAGAAAPAAKQEAAPAAAPAPAAGVKEVNVPDIGGDEVEVTEVMVKVGDKVAAEQSLIT
VEGDKASMEVPAPFAGVVKELKVNVGDKVKTGSLIMIFEVEGAAPAAAPAKQEAAAPAPA
AKAEAPAAAPAAKAEGKSEFAENDAYVHATPLIRRLAREFGVNLAKVKGTGRKGRILRED
VQAYVKEAIKRAEAAPAATGGGIPGMLPWPKVDFSKFGEIEEVELGRIQKISGANLSRNW
VMIPHVTHFDKTDITELEAFRKQQNEEAAKRKLDVKITPVVFIMKAVAAALEQMPRFNSS
LSEDGQRLTLKKYINIGVAVDTPNGLVVPVFKDVNKKGIIELSRELMTISKKARDGKLTA
GEMQGGCFTISSIGGLGTTHFAPIVNAPEVAILGVSKSAMEPVWNGKEFVPRLMLPISLS
FDHRVIDGADGARFITIINNTLSDIRRLVM
References
External Links:
ResourceLink
Uniprot ID:P06959
Uniprot Name:ODP2_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21238964
Ecogene ID:EG10025
Ecocyc:EG10025
ColiBase:b0115
Kegg Gene:b0115
EchoBASE ID:EB0024
CCDB:ODP2_ECOLI
BacMap:16128108
General Reference:
  • Ali, S. T., Guest, J. R. (1990). "Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli." Biochem J 271:139-145. Pubmed: 2121129
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hale, G., Perham, R. N. (1980). "Amino acid sequence around lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli." Biochem J 187:905-908. Pubmed: 6821375
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Russell, G. C., Guest, J. R. (1990). "Overexpression of restructured pyruvate dehydrogenase complexes and site-directed mutagenesis of a potential active-site histidine residue." Biochem J 269:443-450. Pubmed: 2201286
  • Stephens, P. E., Darlison, M. G., Lewis, H. M., Guest, J. R. (1983). "The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component." Eur J Biochem 133:481-489. Pubmed: 6345153
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842