Pyruvate dehydrogenase E1 component

Details

Name
Pyruvate dehydrogenase E1 component
Synonyms
  • 1.2.4.1
  • PDH E1 component
Gene Name
aceE
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0016641|Pyruvate dehydrogenase E1 component
MSERFPNDVDPIETRDWLQAIESVIREEGVERAQYLIDQLLAEARKGGVNVAAGTGISNY
INTIPVEEQPEYPGNLELERRIRSAIRWNAIMTVLRASKKDLELGGHMASFQSSATIYDV
CFNHFFRARNEQDGGDLVYFQGHISPGVYARAFLEGRLTQEQLDNFRQEVHGNGLSSYPH
PKLMPEFWQFPTVSMGLGPIGAIYQAKFLKYLEHRGLKDTSKQTVYAFLGDGEMDEPESK
GAITIATREKLDNLVFVINCNLQRLDGPVTGNGKIINELEGIFEGAGWNVIKVMWGSRWD
ELLRKDTSGKLIQLMNETVDGDYQTFKSKDGAYVREHFFGKYPETAALVADWTDEQIWAL
NRGGHDPKKIYAAFKKAQETKGKATVILAHTIKGYGMGDAAEGKNIAHQVKKMNMDGVRH
IRDRFNVPVSDADIEKLPYITFPEGSEEHTYLHAQRQKLHGYLPSRQPNFTEKLELPSLQ
DFGALLEEQSKEISTTIAFVRALNVMLKNKSIKDRLVPIIADEARTFGMEGLFRQIGIYS
PNGQQYTPQDREQVAYYKEDEKGQILQEGINELGAGCSWLAAATSYSTNNLPMIPFYIYY
SMFGFQRIGDLCWAAGDQQARGFLIGGTSGRTTLNGEGLQHEDGHSHIQSLTIPNCISYD
PAYAYEVAVIMHDGLERMYGEKQENVYYYITTLNENYHMPAMPEGAEEGIRKGIYKLETI
EGSKGKVQLLGSGSILRHVREAAEILAKDYGVGSDVYSVTSFTELARDGQDCERWNMLHP
LETPRVPYIAQVMNDAPAVASTDYMKLFAEQVRTYVPADDYRVLGTDGFGRSDSRENLRH
HFEVDASYVVVAALGELAKRGEIDKKVVADAIAKFNIDADKVNPRLA
Number of residues
887
Molecular Weight
99667.78
Theoretical pI
5.42
GO Classification
Functions
identical protein binding / metal ion binding / pyruvate dehydrogenase (acetyl-transferring) activity / pyruvate dehydrogenase activity
Processes
glycolytic process
Components
cytosol / membrane
General Function
Pyruvate dehydrogenase activity
Specific Function
Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0016642|Pyruvate dehydrogenase E1 component (aceE)
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
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AFG8
UniProtKB Entry NameODP1_ECOLI
GenBank Gene IDV01498
General References
  1. Stephens PE, Darlison MG, Lewis HM, Guest JR: The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the pyruvate dehydrogenase component. Eur J Biochem. 1983 Jun 1;133(1):155-62. [Article]
  2. Fujita N, Mori H, Yura T, Ishihama A: Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region. Nucleic Acids Res. 1994 May 11;22(9):1637-9. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Haydon DJ, Quail MA, Guest JR: A mutation causing constitutive synthesis of the pyruvate dehydrogenase complex in Escherichia coli is located within the pdhR gene. FEBS Lett. 1993 Dec 20;336(1):43-7. [Article]
  6. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
  7. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  8. Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y: Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics. 2009 Feb;8(2):215-25. doi: 10.1074/mcp.M800187-MCP200. Epub 2008 Aug 23. [Article]
  9. Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W: Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. Biochemistry. 2002 Apr 23;41(16):5213-21. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01987Cocarboxylaseapproved, experimentalunknownDetails