Phosphoenolpyruvate synthase (P23538)

Identification
Name:Phosphoenolpyruvate synthase
Synonyms:
  • PEP synthase
  • Pyruvate, water dikinase
Gene Name:ppsA
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate
Cellular Location:Not Available
SMPDB Pathways:
  • Gluconeogenesis from L-malic acid PW000819
  • fructose metabolism PW000913
  • glycerol metabolism PW000914
  • glycerol metabolism II PW000915
  • glycerol metabolism III (sn-glycero-3-phosphoethanolamine) PW000916
  • glycerol metabolism IV (glycerophosphoglycerol) PW000917
  • glycerol metabolism V (glycerophosphoserine) PW000918
  • glycolysis and pyruvate dehydrogenase PW000785
  • superpathway of D-glucarate and D-galactarate degradation PW000795
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+2.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0Pyruvic acid ↔ 1.0Adenosine monophosphate + 2.0Hydrogen ion + 1.0Phosphoenolpyruvic acid + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyruvic acid + 1.0Water ↔ 1.0Adenosine monophosphate + 1.0Phosphoenolpyruvic acid + 1.0Phosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+2.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Phosphoenolpyruvic acid + 1.0Adenosine monophosphate + 1.0Phosphate + 2.0Hydrogen ion → 1.0Adenosine triphosphate + 1.0Water + 1.0Pyruvic acid
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb
1.0Water + 1.0Adenosine triphosphate + 1.0Pyruvic acid → 1.0Adenosine monophosphate + 1.0Phosphate + 2.0Hydrogen ion + 1.0Phosphoenolpyruvic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+2.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0Pyruvic acid ↔ 1.0Adenosine monophosphate + 2.0Hydrogen ion + 1.0Phosphoenolpyruvic acid + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyruvic acid + 1.0Water ↔ 1.0Adenosine monophosphate + 1.0Phosphoenolpyruvic acid + 1.0Phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyruvic acid + 1.0Water → 1.0Adenosine monophosphate + 1.0Phosphoenolpyruvic acid + 1.0Inorganic phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00263Phosphoenolpyruvic acidMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
kinase activity
nucleoside binding
purine nucleoside binding
pyruvate, water dikinase activity
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
alcohol metabolic process
cellular metabolic process
gluconeogenesis
glucose metabolic process
hexose metabolic process
metabolic process
monosaccharide metabolic process
phosphate metabolic process
phosphorus metabolic process
phosphorylation
small molecule metabolic process
Gene Properties
Blattner:b1702
Gene OrientationCounterclockwise
Centisome Percentage:38.42
Left Sequence End1782758
Right Sequence End1785136
Gene Sequence:
>2379 bp
ATGTCCAACAATGGCTCGTCACCGCTGGTGCTTTGGTATAACCAACTCGGCATGAATGAT
GTAGACAGGGTTGGGGGCAAAAATGCCTCCCTGGGTGAAATGATTACTAATCTTTCCGGA
ATGGGTGTTTCCGTTCCGAATGGTTTCGCCACAACCGCCGACGCGTTTAACCAGTTTCTG
GACCAAAGCGGCGTAAACCAGCGCATTTATGAACTGCTGGATAAAACGGATATTGACGAT
GTTACTCAGCTTGCGAAAGCGGGCGCGCAAATCCGCCAGTGGATTATCGACACTCCCTTC
CAGCCTGAGCTGGAAAACGCCATCCGCGAAGCCTATGCACAGCTTTCCGCCGATGACGAA
AACGCCTCTTTTGCGGTGCGCTCCTCCGCCACCGCAGAAGATATGCCGGACGCTTCTTTT
GCCGGTCAGCAGGAAACCTTCCTCAACGTTCAGGGTTTTGACGCCGTTCTCGTGGCAGTG
AAACATGTATTTGCTTCTCTGTTTAACGATCGCGCCATCTCTTATCGTGTGCACCAGGGT
TACGATCACCGTGGTGTGGCGCTCTCCGCCGGTGTTCAACGGATGGTGCGCTCTGACCTC
GCATCATCTGGCGTGATGTTCTCCATTGATACCGAATCCGGCTTTGACCAGGTGGTGTTT
ATCACTTCCGCATGGGGCCTTGGTGAGATGGTCGTGCAGGGTGCGGTTAACCCGGATGAG
TTTTACGTGCATAAACCGACACTGGCGGCGAATCGCCCGGCTATCGTGCGCCGCACCATG
GGGTCGAAAAAAATCCGCATGGTTTACGCGCCGACCCAGGAGCACGGCAAGCAGGTTAAA
ATCGAAGACGTACCGCAGGAACAGCGTGACATCTTCTCGCTGACCAACGAAGAAGTGCAG
GAACTGGCAAAACAGGCCGTACAAATTGAGAAACACTACGGTCGCCCGATGGATATTGAG
TGGGCGAAAGATGGCCACACCGGTAAACTGTTCATTGTGCAGGCGCGTCCGGAAACCGTG
CGCTCACGCGGTCAGGTCATGGAGCGTTATACGCTGCATTCACAGGGTAAGATTATCGCC
GAAGGCCGTGCTATCGGTCATCGCATCGGTGCGGGTCCGGTGAAAGTCATCCATGACATC
AGCGAAATGAACCGCATCGAACCTGGCGACGTGCTGGTTACTGACATGACCGACCCGGAC
TGGGAACCGATCATGAAGAAAGCATCTGCCATCGTCACCAACCGTGGCGGTCGTACCTGT
CACGCGGCGATCATCGCTCGTGAACTGGGCATTCCGGCGGTAGTGGGCTGTGGAGATGCA
ACAGAACGGATGAAAGACGGTGAGAACGTCACTGTTTCTTGTGCCGAAGGTGATACCGGT
TACGTCTATGCGGAGTTGCTGGAATTTAGCGTGAAAAGCTCCAGCGTAGAAACGATGCCG
GATCTGCCGTTGAAAGTGATGATGAACGTCGGTAACCCGGACCGTGCTTTCGACTTCGCC
TGCCTACCGAACGAAGGCGTGGGCCTTGCGCGTCTGGAATTTATCATCAACCGTATGATT
GGCGTCCACCCACGCGCACTGCTTGAGTTTGACGATCAGGAACCGCAGTTGCAAAACGAA
ATCCGCGAGATGATGAAAGGTTTTGATTCTCCGCGTGAATTTTACGTTGGTCGTCTGACT
GAAGGGATCGCGACGCTGGGTGCCGCGTTTTATCCGAAGCGCGTCATTGTCCGTCTCTCT
GATTTTAAATCGAACGAATATGCCAACCTGGTCGGTGGTGAGCGTTACGAGCCAGATGAA
GAGAACCCGATGCTCGGCTTCCGTGGCGCGGGCCGCTATGTTTCCGACAGCTTCCGCGAC
TGTTTCGCGCTGGAGTGTGAAGCAGTGAAACGTGTGCGCAACGACATGGGACTGACCAAC
GTTGAGATCATGATCCCGTTCGTGCGTACCGTAGATCAGGCGAAAGCGGTGGTTGAAGAA
CTGGCGCGTCAGGGGCTGAAACGTGGCGAGAACGGGCTGAAAATCATCATGATGTGTGAA
ATCCCGTCCAACGCCTTGCTGGCCGAGCAGTTCCTCGAATATTTCGACGGCTTCTCAATT
GGCTCAAACGATATGACGCAGCTGGCGCTCGGTCTGGACCGTGACTCCGGCGTGGTGTCT
GAATTGTTCGATGAGCGCAACGATGCGGTGAAAGCACTGCTGTCGATGGCTATCCGTGCC
GCGAAGAAACAGGGCAAATATGTCGGGATTTGCGGTCAGGGTCCGTCCGACCACGAAGAC
TTTGCCGCATGGTTGATGGAAGAGGGGATCGATAGCCTGTCTCTGAACCCGGACACCGTG
GTGCAAACCTGGTTAAGCCTGGCTGAACTGAAGAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:792
Protein Molecular Weight:87434
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Phosphoenolpyruvate synthase
MSNNGSSPLVLWYNQLGMNDVDRVGGKNASLGEMITNLSGMGVSVPNGFATTADAFNQFL
DQSGVNQRIYELLDKTDIDDVTQLAKAGAQIRQWIIDTPFQPELENAIREAYAQLSADDE
NASFAVRSSATAEDMPDASFAGQQETFLNVQGFDAVLVAVKHVFASLFNDRAISYRVHQG
YDHRGVALSAGVQRMVRSDLASSGVMFSIDTESGFDQVVFITSAWGLGEMVVQGAVNPDE
FYVHKPTLAANRPAIVRRTMGSKKIRMVYAPTQEHGKQVKIEDVPQEQRDIFSLTNEEVQ
ELAKQAVQIEKHYGRPMDIEWAKDGHTGKLFIVQARPETVRSRGQVMERYTLHSQGKIIA
EGRAIGHRIGAGPVKVIHDISEMNRIEPGDVLVTDMTDPDWEPIMKKASAIVTNRGGRTC
HAAIIARELGIPAVVGCGDATERMKDGENVTVSCAEGDTGYVYAELLEFSVKSSSVETMP
DLPLKVMMNVGNPDRAFDFACLPNEGVGLARLEFIINRMIGVHPRALLEFDDQEPQLQNE
IREMMKGFDSPREFYVGRLTEGIATLGAAFYPKRVIVRLSDFKSNEYANLVGGERYEPDE
ENPMLGFRGAGRYVSDSFRDCFALECEAVKRVRNDMGLTNVEIMIPFVRTVDQAKAVVEE
LARQGLKRGENGLKIIMMCEIPSNALLAEQFLEYFDGFSIGSNDMTQLALGLDRDSGVVS
ELFDERNDAVKALLSMAIRAAKKQGKYVGICGQGPSDHEDFAAWLMEEGIDSLSLNPDTV
VQTWLSLAELKK
References
External Links:
ResourceLink
Uniprot ID:P23538
Uniprot Name:PPSA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742783
Ecogene ID:EG10759
Ecocyc:EG10759
ColiBase:b1702
Kegg Gene:b1702
EchoBASE ID:EB0752
CCDB:PPSA_ECOLI
BacMap:16129658
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • Berman, K. M., Cohn, M. (1970). "Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent metal ions." J Biol Chem 245:5309-5318. Pubmed: 4319237
  • 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
  • Cooper, R. A., Kornberg, H. L. (1967). "The mechanism of the phosphoenolpyruvate synthase reaction." Biochim Biophys Acta 141:211-213. Pubmed: 4293109
  • 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
  • Narindrasorasak, S., Bridger, W. A. (1977). "Phosphoenolypyruvate synthetase of Escherichia coli: molecular weight, subunit composition, and identification of phosphohistidine in phosphoenzyme intermediate." J Biol Chem 252:3121-3127. Pubmed: 16880
  • Niersbach, M., Kreuzaler, F., Geerse, R. H., Postma, P. W., Hirsch, H. J. (1992). "Cloning and nucleotide sequence of the Escherichia coli K-12 ppsA gene, encoding PEP synthase." Mol Gen Genet 231:332-336. Pubmed: 1310524