Phosphoenolpyruvate carboxylase (P00864)

Identification
Name:Phosphoenolpyruvate carboxylase
Synonyms:
  • PEPC
  • PEPCase
Gene Name:ppc
Enzyme Class:
Biological Properties
General Function:Involved in phosphoenolpyruvate carboxylase activity
Specific Function:Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Carbon dioxide + 1.0Water + 1.0Phosphoenolpyruvic acid ↔ 1.0Hydrogen ion + 1.0Oxalacetic acid + 1.0Phosphate + 1.0Hydrogen carbonate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Phosphate + 1.0Oxalacetic acid ↔ 1.0Water + 1.0Phosphoenolpyruvic acid + 1.0Carbon dioxide
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Inorganic phosphate + 1.0Oxalacetic acid → 1.0Water + 1.0Phosphoenolpyruvic acid + 1.0Carbonic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB04030Carbon dioxideMetaboCard
ECMDB03538Carbonic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00223Oxalacetic acidMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00263Phosphoenolpyruvic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
carbon-carbon lyase activity
carboxy-lyase activity
catalytic activity
lyase activity
phosphoenolpyruvate carboxykinase activity
phosphoenolpyruvate carboxylase activity
Process
acetyl-CoA catabolic process
acetyl-CoA metabolic process
carbon fixation
cellular metabolic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
organic substance metabolic process
tricarboxylic acid cycle
Gene Properties
Blattner:b3956
Gene OrientationCounterclockwise
Centisome Percentage:89.41
Left Sequence End4148470
Right Sequence End4151121
Gene Sequence:
>2652 bp
ATGAACGAACAATATTCCGCATTGCGTAGTAATGTCAGTATGCTCGGCAAAGTGCTGGGA
GAAACCATCAAGGATGCGTTGGGAGAACACATTCTTGAACGCGTAGAAACTATCCGTAAG
TTGTCGAAATCTTCACGCGCTGGCAATGATGCTAACCGCCAGGAGTTGCTCACCACCTTA
CAAAATTTGTCGAACGACGAGCTGCTGCCCGTTGCGCGTGCGTTTAGTCAGTTCCTGAAC
CTGGCCAACACCGCCGAGCAATACCACAGCATTTCGCCGAAAGGCGAAGCTGCCAGCAAC
CCGGAAGTGATCGCCCGCACCCTGCGTAAACTGAAAAACCAGCCGGAACTGAGCGAAGAC
ACCATCAAAAAAGCAGTGGAATCGCTGTCGCTGGAACTGGTCCTCACGGCTCACCCAACC
GAAATTACCCGTCGTACACTGATCCACAAAATGGTGGAAGTGAACGCCTGTTTAAAACAG
CTCGATAACAAAGATATCGCTGACTACGAACACAACCAGCTGATGCGTCGCCTGCGCCAG
TTGATCGCCCAGTCATGGCATACCGATGAAATCCGTAAGCTGCGTCCAAGCCCGGTAGAT
GAAGCCAAATGGGGCTTTGCCGTAGTGGAAAACAGCCTGTGGCAAGGCGTACCAAATTAC
CTGCGCGAACTGAACGAACAACTGGAAGAGAACCTCGGCTACAAACTGCCCGTCGAATTT
GTTCCGGTCCGTTTTACTTCGTGGATGGGCGGCGACCGCGACGGCAACCCGAACGTCACT
GCCGATATCACCCGCCACGTCCTGCTACTCAGCCGCTGGAAAGCCACCGATTTGTTCCTG
AAAGATATTCAGGTGCTGGTTTCTGAACTGTCGATGGTTGAAGCGACCCCTGAACTGCTG
GCGCTGGTTGGCGAAGAAGGTGCCGCAGAACCGTATCGCTATCTGATGAAAAACCTGCGT
TCTCGCCTGATGGCGACACAGGCATGGCTGGAAGCGCGCCTGAAAGGCGAAGAACTGCCA
AAACCAGAAGGCCTGCTGACACAAAACGAAGAACTGTGGGAACCGCTCTACGCTTGCTAC
CAGTCACTTCAGGCGTGTGGCATGGGTATTATCGCCAACGGCGATCTGCTCGACACCCTG
CGCCGCGTGAAATGTTTCGGCGTACCGCTGGTCCGTATTGATATCCGTCAGGAGAGCACG
CGTCATACCGAAGCGCTGGGCGAGCTGACCCGCTACCTCGGTATCGGCGACTACGAAAGC
TGGTCAGAGGCCGACAAACAGGCGTTCCTGATCCGCGAACTGAACTCCAAACGTCCGCTT
CTGCCGCGCAACTGGCAACCAAGCGCCGAAACGCGCGAAGTGCTCGATACCTGCCAGGTG
ATTGCCGAAGCACCGCAAGGCTCCATTGCCGCCTACGTGATCTCGATGGCGAAAACGCCG
TCCGACGTACTGGCTGTCCACCTGCTGCTGAAAGAAGCGGGTATCGGGTTTGCGATGCCG
GTTGCTCCGCTGTTTGAAACCCTCGATGATCTGAACAACGCCAACGATGTCATGACCCAG
CTGCTCAATATTGACTGGTATCGTGGCCTGATTCAGGGCAAACAGATGGTGATGATTGGC
TATTCCGACTCAGCAAAAGATGCGGGAGTGATGGCAGCTTCCTGGGCGCAATATCAGGCA
CAGGATGCATTAATCAAAACCTGCGAAAAAGCGGGTATTGAGCTGACGTTGTTCCACGGT
CGCGGCGGTTCCATTGGTCGCGGCGGCGCACCTGCTCATGCGGCGCTGCTGTCACAACCG
CCAGGAAGCCTGAAAGGCGGCCTGCGCGTAACCGAACAGGGCGAGATGATCCGCTTTAAA
TATGGTCTGCCAGAAATCACCGTCAGCAGCCTGTCGCTTTATACCGGGGCGATTCTGGAA
GCCAACCTGCTGCCACCGCCGGAGCCGAAAGAGAGCTGGCGTCGCATTATGGATGAACTG
TCAGTCATCTCCTGCGATGTCTACCGCGGCTACGTACGTGAAAACAAAGATTTTGTGCCT
TACTTCCGCTCCGCTACGCCGGAACAAGAACTGGGCAAACTGCCGTTGGGTTCACGTCCG
GCGAAACGTCGCCCAACCGGCGGCGTCGAGTCACTACGCGCCATTCCGTGGATCTTCGCC
TGGACGCAAAACCGTCTGATGCTCCCCGCCTGGCTGGGTGCAGGTACGGCGCTGCAAAAA
GTGGTCGAAGACGGCAAACAGAGCGAGCTGGAGGCTATGTGCCGCGATTGGCCATTCTTC
TCGACGCGTCTCGGCATGCTGGAGATGGTCTTCGCCAAAGCAGACCTGTGGCTGGCGGAA
TACTATGACCAACGCCTGGTAGACAAAGCACTGTGGCCGTTAGGTAAAGAGTTACGCAAC
CTGCAAGAAGAAGACATCAAAGTGGTGCTGGCGATTGCCAACGATTCCCATCTGATGGCC
GATCTGCCGTGGATTGCAGAGTCTATTCAGCTACGGAATATTTACACCGACCCGCTGAAC
GTATTGCAGGCCGAGTTGCTGCACCGCTCCCGCCAGGCAGAAAAAGAAGGCCAGGAACCG
GATCCTCGCGTCGAACAAGCGTTAATGGTCACTATTGCCGGGATTGCGGCAGGTATGCGT
AATACCGGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:883
Protein Molecular Weight:99062
Protein Theoretical pI:5
PDB File:1JQN
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Phosphoenolpyruvate carboxylase
MNEQYSALRSNVSMLGKVLGETIKDALGEHILERVETIRKLSKSSRAGNDANRQELLTTL
QNLSNDELLPVARAFSQFLNLANTAEQYHSISPKGEAASNPEVIARTLRKLKNQPELSED
TIKKAVESLSLELVLTAHPTEITRRTLIHKMVEVNACLKQLDNKDIADYEHNQLMRRLRQ
LIAQSWHTDEIRKLRPSPVDEAKWGFAVVENSLWQGVPNYLRELNEQLEENLGYKLPVEF
VPVRFTSWMGGDRDGNPNVTADITRHVLLLSRWKATDLFLKDIQVLVSELSMVEATPELL
ALVGEEGAAEPYRYLMKNLRSRLMATQAWLEARLKGEELPKPEGLLTQNEELWEPLYACY
QSLQACGMGIIANGDLLDTLRRVKCFGVPLVRIDIRQESTRHTEALGELTRYLGIGDYES
WSEADKQAFLIRELNSKRPLLPRNWQPSAETREVLDTCQVIAEAPQGSIAAYVISMAKTP
SDVLAVHLLLKEAGIGFAMPVAPLFETLDDLNNANDVMTQLLNIDWYRGLIQGKQMVMIG
YSDSAKDAGVMAASWAQYQAQDALIKTCEKAGIELTLFHGRGGSIGRGGAPAHAALLSQP
PGSLKGGLRVTEQGEMIRFKYGLPEITVSSLSLYTGAILEANLLPPPEPKESWRRIMDEL
SVISCDVYRGYVRENKDFVPYFRSATPEQELGKLPLGSRPAKRRPTGGVESLRAIPWIFA
WTQNRLMLPAWLGAGTALQKVVEDGKQSELEAMCRDWPFFSTRLGMLEMVFAKADLWLAE
YYDQRLVDKALWPLGKELRNLQEEDIKVVLAIANDSHLMADLPWIAESIQLRNIYTDPLN
VLQAELLHRSRQAEKEGQEPDPRVEQALMVTIAGIAAGMRNTG
References
External Links:
ResourceLink
Uniprot ID:P00864
Uniprot Name:CAPP_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676105
PDB ID:1JQN
Ecogene ID:EG10756
Ecocyc:EG10756
ColiBase:b3956
Kegg Gene:b3956
EchoBASE ID:EB0749
CCDB:CAPP_ECOLI
BacMap:16131794
General Reference:
  • Blattner, F. R., Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L. (1993). "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Nucleic Acids Res 21:5408-5417. Pubmed: 8265357
  • 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., Miwa, T., Ishijima, S., Izui, K., Katsuki, H. (1984). "The primary structure of phosphoenolpyruvate carboxylase of Escherichia coli. Nucleotide sequence of the ppc gene and deduced amino acid sequence." J Biochem 95:909-916. Pubmed: 6086598
  • 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
  • Inoue, M., Hayashi, M., Sugimoto, M., Harada, S., Kai, Y., Kasai, N., Terada, K., Izui, K. (1989). "First crystallization of a phosphoenolpyruvate carboxylase from Escherichia coli." J Mol Biol 208:509-510. Pubmed: 2677392
  • Izui, K., Miwa, T., Kajitani, M., Fujita, N., Sabe, H., Ishihama, A., Katsuki, H. (1985). "Promoter analysis of the phosphoenolpyruvate carboxylase gene of Escherichia coli." Nucleic Acids Res 13:59-71. Pubmed: 3889833
  • Kai, Y., Matsumura, H., Inoue, T., Terada, K., Nagara, Y., Yoshinaga, T., Kihara, A., Tsumura, K., Izui, K. (1999). "Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition." Proc Natl Acad Sci U S A 96:823-828. Pubmed: 9927652
  • Meinnel, T., Schmitt, E., Mechulam, Y., Blanquet, S. (1992). "Structural and biochemical characterization of the Escherichia coli argE gene product." J Bacteriol 174:2323-2331. Pubmed: 1551850
  • Terada, K., Izui, K. (1991). "Site-directed mutagenesis of the conserved histidine residue of phosphoenolpyruvate carboxylase. His138 is essential for the second partial reaction." Eur J Biochem 202:797-803. Pubmed: 1765093
  • Terada, K., Murata, T., Izui, K. (1991). "Site-directed mutagenesis of phosphoenolpyruvate carboxylase from E. coli: the role of His579 in the catalytic and regulatory functions." J Biochem 109:49-54. Pubmed: 2016273
  • Yano, M., Terada, K., Umiji, K., Izui, K. (1995). "Catalytic role of an arginine residue in the highly conserved and unique sequence of phosphoenolpyruvate carboxylase." J Biochem 117:1196-1200. Pubmed: 7490260