Identification
Name:Phosphoenolpyruvate carboxykinase [ATP]
Synonyms:
  • PEP carboxykinase
  • PEPCK
  • Phosphoenolpyruvate carboxylase
Gene Name:pckA
Enzyme Class:
Biological Properties
General Function:Involved in phosphoenolpyruvate carboxykinase (ATP) activity
Specific Function:ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO(2)
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
SMPDB Reactions:
Thumb+ThumbAdenosine diphosphate+Thumb+Thumb+Thumb
EcoCyc Reactions:
Thumb+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
Complex Reactions:
Thumb+ThumbThumb+Thumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB00223Oxalacetic acidMetaboCard
ECMDB00263Phosphoenolpyruvic acidMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
carbon-carbon lyase activity
carboxy-lyase activity
catalytic activity
lyase activity
nucleoside binding
nucleotide binding
phosphoenolpyruvate carboxykinase (ATP) activity
phosphoenolpyruvate carboxykinase activity
purine nucleoside binding
purine nucleotide binding
Process
alcohol metabolic process
gluconeogenesis
glucose metabolic process
hexose metabolic process
metabolic process
monosaccharide metabolic process
small molecule metabolic process
Gene Properties
Blattner:b3403
Gene OrientationClockwise
Centisome Percentage:76.10
Left Sequence End3530840
Right Sequence End3532462
Gene Sequence:
>1623 bp
ATGAATACTCTCCCTGAACATTCATGTGACGTGTTGATTATCGGTAGCGGCGCAGCCGGA
CTTTCACTGGCGCTACGCCTGGCTGACCAGCATCAGGTCATCGTTCTAAGTAAAGGCCCG
GTAACGGAAGGTTCAACATTTTATGCCCAGGGCGGTATTGCCGCCGTGTTTGATGAAACT
GACAGCATTGACTCGCATGTGGAAGACACATTGATTGCCGGGGCTGGTATTTGCGATCGC
CATGCAGTTGAATTTGTCGCCAGCAATGCACGATCCTGTGTGCAATGGCTAATCGACCAG
GGGGTGTTGTTTGATACCCACATTCAACCGAATGGCGAAGAAAGTTACCATCTGACCCGT
GAAGGTGGACATAGTCACCGTCGTATTCTTCATGCCGCCGACGCCACCGGTAGAGAAGTA
GAAACCACGCTGGTGAGCAAGGCGCTGAACCATCCGAATATTCGCGTGCTGGAGCGCAGC
AACGCGGTTGATCTGATTGTTTCTGACAAAATTGGCCTGCCGGGCACGCGACGGGTTGTT
GGCGCGTGGGTATGGAACCGTAATAAAGAAACGGTGGAAACCTGCCACGCAAAAGCGGTG
GTGCTGGCAACCGGCGGTGCGTCGAAGGTTTATCAGTACACCACCAATCCGGATATTTCT
TCTGGCGATGGCATTGCTATGGCGTGGCGCGCAGGCTGCCGGGTTGCCAATCTCGAATTT
AATCAGTTCCACCCTACCGCGCTATATCACCCACAGGCACGCAATTTCCTGTTAACAGAA
GCACTGCGCGGCGAAGGCGCTTATCTCAAGCGCCCGGATGGTACGCGTTTTATGCCCGAT
TTTGATGAGCGCGGCGAACTGGCCCCGCGCGATATTGTCGCCCGCGCCATTGACCATGAA
ATGAAACGCCTCGGCGCAGATTGTATGTTCCTTGATATCAGCCATAAGCCCGCCGATTTT
ATTCGCCAGCATTTCCCGATGATTTATGAAAAGCTGCTCGGGCTGGGGATTGATCTCACA
CAAGAACCGGTACCGATTGTGCCTGCTGCACATTATACCTGCGGTGGTGTAATGGTTGAT
GATCATGGGCGTACGGACGTCGAGGGCTTGTATGCCATTGGCGAGGTGAGTTATACCGGC
TTACACGGCGCTAACCGCATGGCCTCGAATTCATTGCTGGAGTGTCTGGTCTATGGCTGG
TCGGCGGCGGAAGATATCACCAGACGTATGCCTTATGCCCACGACATCAGTACGTTACCG
CCGTGGGATGAAAGCCGCGTTGAGAACCCTGACGAACGGGTAGTAATTCAGCATAACTGG
CACGAGCTACGTCTGTTTATGTGGGATTACGTTGGCATTGTGCGCACAACGAAGCGCCTG
GAACGCGCCCTGCGGCGGATAACCATGCTCCAACAAGAAATAGACGAATATTACGCCCAT
TTCCGCGTCTCAAATAATTTGCTGGAGCTGCGTAATCTGGTACAGGTTGCCGAGTTGATT
GTTCGCTGTGCAATGATGCGTAAAGAGAGTCGGGGGTTGCATTTCACGCTGGATTATCCG
GAACTGCTCACCCATTCCGGTCCGTCGATCCTTTCCCCCGGCAATCATTACATAAACAGA
TAA
Protein Properties
Pfam Domain Function:
Protein Residues:540
Protein Molecular Weight:59643
Protein Theoretical pI:5
PDB File:1OS1
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Phosphoenolpyruvate carboxykinase [ATP]
MRVNNGLTPQELEAYGISDVHDIVYNPSYDLLYQEELDPSLTGYERGVLTNLGAVAVDTG
IFTGRSPKDKYIVRDDTTRDTFWWADKGKGKNDNKPLSPETWQHLKGLVTRQLSGKRLFV
VDAFCGANPDTRLSVRFITEVAWQAHFVKNMFIRPSDEELAGFKPDFIVMNGAKCTNPQW
KEQGLNSENFVAFNLTERMQLIGGTWYGGEMKKGMFSMMNYLLPLKGIASMHCSANVGEK
GDVAVFFGLSGTGKTTLSTDPKRRLIGDDEHGWDDDGVFNFEGGCYAKTIKLSKEAEPEI
YNAIRRDALLENVTVREDGTIDFDDGSKTENTRVSYPIYHIDNIVKPVSKAGHATKVIFL
TADAFGVLPPVSRLTADQTQYHFLSGFTAKLAGTERGITEPTPTFSACFGAAFLSLHPTQ
YAEVLVKRMQAAGAQAYLVNTGWNGTGKRISIKDTRAIIDAILNGSLDNAETFTLPMFNL
AIPTELPGVDTKILDPRNTYASPEQWQEKAETLAKLFIDNFDKYTDTPAGAALVAAGPKL
References
External Links:
ResourceLink
Uniprot ID:P22259
Uniprot Name:PCKA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675465
PDB ID:1OS1
Ecogene ID:EG10688
Ecocyc:EG10688
ColiBase:b3403
Kegg Gene:b3403
EchoBASE ID:EB0682
CCDB:PCKA_ECOLI
BacMap:16131280
General Reference:
  • 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
  • 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
  • Hou, S. Y., Chao, Y. P., Liao, J. C. (1995). "A mutant phosphoenolpyruvate carboxykinase in Escherichia coli conferring oxaloacetate decarboxylase activity." J Bacteriol 177:1620-1623. Pubmed: 7883719
  • 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
  • Matte, A., Goldie, H., Sweet, R. M., Delbaere, L. T. (1996). "Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold." J Mol Biol 256:126-143. Pubmed: 8609605
  • Medina, V., Pontarollo, R., Glaeske, D., Tabel, H., Goldie, H. (1990). "Sequence of the pckA gene of Escherichia coli K-12: relevance to genetic and allosteric regulation and homology of E. coli phosphoenolpyruvate carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces cerevisiae." J Bacteriol 172:7151-7156. Pubmed: 1701430
  • Mizuno, T., Wurtzel, E. T., Inouye, M. (1982). "Osmoregulation of gene expression. II. DNA sequence of the envZ gene of the ompB operon of Escherichia coli and characterization of its gene product." J Biol Chem 257:13692-13698. Pubmed: 6292200
  • Ramseier, T. M., Bledig, S., Michotey, V., Feghali, R., Saier, M. H. Jr (1995). "The global regulatory protein FruR modulates the direction of carbon flow in Escherichia coli." Mol Microbiol 16:1157-1169. Pubmed: 8577250
  • Tari, L. W., Matte, A., Goldie, H., Delbaere, L. T. (1997). "Mg(2+)-Mn2+ clusters in enzyme-catalyzed phosphoryl-transfer reactions." Nat Struct Biol 4:990-994. Pubmed: 9406547
  • Tari, L. W., Matte, A., Pugazhenthi, U., Goldie, H., Delbaere, L. T. (1996). "Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase." Nat Struct Biol 3:355-363. Pubmed: 8599762
  • 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