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
- Functionsidentical protein binding / metal ion binding / pyruvate dehydrogenase (acetyl-transferring) activity / pyruvate dehydrogenase activityProcessesglycolytic processComponentscytosol / 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
- Transketolase_N (PF00456)
- 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
Resource Link UniProtKB ID P0AFG8 UniProtKB Entry Name ODP1_ECOLI GenBank Gene ID V01498 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]