Pyruvate dehydrogenase E1 component (P0AFG8)

Identification
Name:Pyruvate dehydrogenase E1 component
Synonyms:Not Available
Gene Name:aceE
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase 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)
Cellular Location:Not Available
SMPDB Pathways:
  • pyruvate decarboxylation to acetyl CoA PW002083
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Enzyme N6-(lipoyl)lysine ↔ 1.0[Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine+1.0Thumb+1.0[Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine
1.0Pyruvic acid + 1.0Enzyme N6-(lipoyl)lysine ↔ 1.0[Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + 1.0Carbon dioxide + 1.0[Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine+1.0Thumb → 1.0a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine+1.0Thumb
1.0Pyruvic acid + 1.0a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + 1.0Hydrogen ion → 1.0a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + 1.0Carbon dioxide
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
Complex Reactions:
1.0Thumb+1.0[dihydrolipoyllysine-residue acetyltransferase] lipoyllysine → 1.0[dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine+1.0Thumb
1.0Pyruvic acid + 1.0[dihydrolipoyllysine-residue acetyltransferase] lipoyllysine → 1.0[dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + 1.0Carbon dioxide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01206Acetyl-CoAMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB01372Thiamine pyrophosphateMetaboCard
GO Classification:
Function
catalytic activity
oxidoreductase activity
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b0114
Gene OrientationClockwise
Centisome Percentage:2.65
Left Sequence End123017
Right Sequence End125680
Gene Sequence:
>2664 bp
ATGTCAGAACGTTTCCCAAATGACGTGGATCCGATCGAAACTCGCGACTGGCTCCAGGCG
ATCGAATCGGTCATCCGTGAAGAAGGTGTTGAGCGTGCTCAGTATCTGATCGACCAACTG
CTTGCTGAAGCCCGCAAAGGCGGTGTAAACGTAGCCGCAGGCACAGGTATCAGCAACTAC
ATCAACACCATCCCCGTTGAAGAACAACCGGAGTATCCGGGTAATCTGGAACTGGAACGC
CGTATTCGTTCAGCTATCCGCTGGAACGCCATCATGACGGTGCTGCGTGCGTCGAAAAAA
GACCTCGAACTGGGCGGCCATATGGCGTCCTTCCAGTCTTCCGCAACCATTTATGATGTG
TGCTTTAACCACTTCTTCCGTGCACGCAACGAGCAGGATGGCGGCGACCTGGTTTACTTC
CAGGGCCACATCTCCCCGGGCGTGTACGCTCGTGCTTTCCTGGAAGGTCGTCTGACTCAG
GAGCAGCTGGATAACTTCCGTCAGGAAGTTCACGGCAATGGCCTCTCTTCCTATCCGCAC
CCGAAACTGATGCCGGAATTCTGGCAGTTCCCGACCGTATCTATGGGTCTGGGTCCGATT
GGTGCTATTTACCAGGCTAAATTCCTGAAATATCTGGAACACCGTGGCCTGAAAGATACC
TCTAAACAAACCGTTTACGCGTTCCTCGGTGACGGTGAAATGGACGAACCGGAATCCAAA
GGTGCGATCACCATCGCTACCCGTGAAAAACTGGATAACCTGGTCTTCGTTATCAACTGT
AACCTGCAGCGTCTTGACGGCCCGGTCACCGGTAACGGCAAGATCATCAACGAACTGGAA
GGCATCTTCGAAGGTGCTGGCTGGAACGTGATCAAAGTGATGTGGGGTAGCCGTTGGGAT
GAACTGCTGCGTAAGGATACCAGCGGTAAACTGATCCAGCTGATGAACGAAACCGTTGAC
GGCGACTACCAGACCTTCAAATCGAAAGATGGTGCGTACGTTCGTGAACACTTCTTCGGT
AAATATCCTGAAACCGCAGCACTGGTTGCAGACTGGACTGACGAGCAGATCTGGGCACTG
AACCGTGGTGGTCACGATCCGAAGAAAATCTACGCTGCATTCAAGAAAGCGCAGGAAACC
AAAGGCAAAGCGACAGTAATCCTTGCTCATACCATTAAAGGTTACGGCATGGGCGACGCG
GCTGAAGGTAAAAACATCGCGCACCAGGTTAAGAAAATGAACATGGACGGTGTGCGTCAT
ATCCGCGACCGTTTCAATGTGCCGGTGTCTGATGCAGATATCGAAAAACTGCCGTACATC
ACCTTCCCGGAAGGTTCTGAAGAGCATACCTATCTGCACGCTCAGCGTCAGAAACTGCAC
GGTTATCTGCCAAGCCGTCAGCCGAACTTCACCGAGAAGCTTGAGCTGCCGAGCCTGCAA
GACTTCGGCGCGCTGTTGGAAGAGCAGAGCAAAGAGATCTCTACCACTATCGCTTTCGTT
CGTGCTCTGAACGTGATGCTGAAGAACAAGTCGATCAAAGATCGTCTGGTACCGATCATC
GCCGACGAAGCGCGTACTTTCGGTATGGAAGGTCTGTTCCGTCAGATTGGTATTTACAGC
CCGAACGGTCAGCAGTACACCCCGCAGGACCGCGAGCAGGTTGCTTACTATAAAGAAGAC
GAGAAAGGTCAGATTCTGCAGGAAGGGATCAACGAGCTGGGCGCAGGTTGTTCCTGGCTG
GCAGCGGCGACCTCTTACAGCACCAACAATCTGCCGATGATCCCGTTCTACATCTATTAC
TCGATGTTCGGCTTCCAGCGTATTGGCGATCTGTGCTGGGCGGCTGGCGACCAGCAAGCG
CGTGGCTTCCTGATCGGCGGTACTTCCGGTCGTACCACCCTGAACGGCGAAGGTCTGCAG
CACGAAGATGGTCACAGCCACATTCAGTCGCTGACTATCCCGAACTGTATCTCTTACGAC
CCGGCTTACGCTTACGAAGTTGCTGTCATCATGCATGACGGTCTGGAGCGTATGTACGGT
GAAAAACAAGAGAACGTTTACTACTACATCACTACGCTGAACGAAAACTACCACATGCCG
GCAATGCCGGAAGGTGCTGAGGAAGGTATCCGTAAAGGTATCTACAAACTCGAAACTATT
GAAGGTAGCAAAGGTAAAGTTCAGCTGCTCGGCTCCGGTTCTATCCTGCGTCACGTCCGT
GAAGCAGCTGAGATCCTGGCGAAAGATTACGGCGTAGGTTCTGACGTTTATAGCGTGACC
TCCTTCACCGAGCTGGCGCGTGATGGTCAGGATTGTGAACGCTGGAACATGCTGCACCCG
CTGGAAACTCCGCGCGTTCCGTATATCGCTCAGGTGATGAACGACGCTCCGGCAGTGGCA
TCTACCGACTATATGAAACTGTTCGCTGAGCAGGTCCGTACTTACGTACCGGCTGACGAC
TACCGCGTACTGGGTACTGATGGCTTCGGTCGTTCCGACAGCCGTGAGAACCTGCGTCAC
CACTTCGAAGTTGATGCTTCTTATGTCGTGGTTGCGGCGCTGGGCGAACTGGCTAAACGT
GGCGAAATCGATAAGAAAGTGGTTGCTGACGCAATCGCCAAATTCAACATCGATGCAGAT
AAAGTTAACCCGCGTCTGGCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:887
Protein Molecular Weight:99668
Protein Theoretical pI:5
PDB File:1RP7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Pyruvate dehydrogenase E1 component
MSERFPNDVDPIETRDWLQAIESVIREEGVERAQYLIDQLLAEARKGGVNVAAGTGISNY
INTIPVEEQPEYPGNLELERRIRSAIRWNAIMTVLRASKKDLELGGHMASFQSSATIYDV
CFNHFFRARNEQDGGDLVYFQGHISPGVYARAFLEGRLTQEQLDNFRQEVHGNGLSSYPH
PKLMPEFWQFPTVSMGLGPIGAIYQAKFLKYLEHRGLKDTSKQTVYAFLGDGEMDEPESK
GAITIATREKLDNLVFVINCNLQRLDGPVTGNGKIINELEGIFEGAGWNVIKVMWGSRWD
ELLRKDTSGKLIQLMNETVDGDYQTFKSKDGAYVREHFFGKYPETAALVADWTDEQIWAL
NRGGHDPKKIYAAFKKAQETKGKATVILAHTIKGYGMGDAAEGKNIAHQVKKMNMDGVRH
IRDRFNVPVSDADIEKLPYITFPEGSEEHTYLHAQRQKLHGYLPSRQPNFTEKLELPSLQ
DFGALLEEQSKEISTTIAFVRALNVMLKNKSIKDRLVPIIADEARTFGMEGLFRQIGIYS
PNGQQYTPQDREQVAYYKEDEKGQILQEGINELGAGCSWLAAATSYSTNNLPMIPFYIYY
SMFGFQRIGDLCWAAGDQQARGFLIGGTSGRTTLNGEGLQHEDGHSHIQSLTIPNCISYD
PAYAYEVAVIMHDGLERMYGEKQENVYYYITTLNENYHMPAMPEGAEEGIRKGIYKLETI
EGSKGKVQLLGSGSILRHVREAAEILAKDYGVGSDVYSVTSFTELARDGQDCERWNMLHP
LETPRVPYIAQVMNDAPAVASTDYMKLFAEQVRTYVPADDYRVLGTDGFGRSDSRENLRH
HFEVDASYVVVAALGELAKRGEIDKKVVADAIAKFNIDADKVNPRLA
References
External Links:
ResourceLink
Uniprot ID:P0AFG8
Uniprot Name:ODP1_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674336
PDB ID:1RP7
Ecogene ID:EG10024
Ecocyc:EG10024
ColiBase:b0114
Kegg Gene:b0114
EchoBASE ID:EB0023
CCDB:ODP1_ECOLI
BacMap:16128107
General Reference:
  • Arjunan, P., Nemeria, N., Brunskill, A., Chandrasekhar, K., Sax, M., Yan, Y., Jordan, F., Guest, J. R., Furey, W. (2002). "Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution." Biochemistry 41:5213-5221. Pubmed: 11955070
  • 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
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • 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
  • Haydon, D. J., Quail, M. A., Guest, J. R. (1993). "A mutation causing constitutive synthesis of the pyruvate dehydrogenase complex in Escherichia coli is located within the pdhR gene." FEBS Lett 336:43-47. Pubmed: 8262214
  • 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
  • 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 pyruvate dehydrogenase component." Eur J Biochem 133:155-162. Pubmed: 6343085
  • 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