Pyruvate kinase II (P21599)

Identification
Name:Pyruvate kinase II
Synonyms:
  • PK-2
Gene Name:pykA
Enzyme Class:
Biological Properties
General Function:Involved in magnesium ion binding
Specific Function:ATP + pyruvate = ADP + phosphoenolpyruvate
Cellular Location:Not Available
SMPDB Pathways:
  • 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+1.0Thumb
1.0ADP + 1.0Hydrogen ion + 1.0Phosphoenolpyruvic acid ↔ 1.0Adenosine triphosphate + 1.0Pyruvic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyruvic acid ↔ 1.0ADP + 1.0Phosphoenolpyruvic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Guanosine triphosphate + 1.0Pyruvic acid ↔ 1.0Guanosine diphosphate + 1.0Phosphoenolpyruvic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0dATP + 1.0Pyruvic acid ↔ 1.0dADP + 1.0Phosphoenolpyruvic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0dGDP+1.0Thumb
1.0dGTP + 1.0Pyruvic acid ↔ 1.0dGDP + 1.0Phosphoenolpyruvic acid
ReactionCard
1.0Nucleoside triphosphate+1.0Thumb ↔ 1.0NDP+1.0Thumb
1.0Nucleoside triphosphate + 1.0Pyruvic acid ↔ 1.0NDP + 1.0Phosphoenolpyruvic acid
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Adenosine diphosphate+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Phosphoenolpyruvic acid + 1.0Adenosine diphosphate + 1.0Hydrogen ion + 1.0ADP → 1.0Adenosine triphosphate + 1.0Pyruvic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0ADP + 1.0Hydrogen ion + 1.0Phosphoenolpyruvic acid ↔ 1.0Adenosine triphosphate + 1.0Pyruvic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21326dADPMetaboCard
ECMDB01532dATPMetaboCard
ECMDB00960dGDPMetaboCard
ECMDB01440dGTPMetaboCard
ECMDB01201Guanosine diphosphateMetaboCard
ECMDB01273Guanosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00263Phosphoenolpyruvic acidMetaboCard
ECMDB00243Pyruvic acidMetaboCard
GO Classification:
Function
alkali metal ion binding
binding
catalytic activity
cation binding
ion binding
kinase activity
magnesium ion binding
metal ion binding
potassium ion binding
pyruvate kinase activity
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
alcohol metabolic process
glucose catabolic process
glucose metabolic process
glycolysis
hexose metabolic process
metabolic process
monosaccharide metabolic process
small molecule metabolic process
Gene Properties
Blattner:b1854
Gene OrientationClockwise
Centisome Percentage:41.72
Left Sequence End1935673
Right Sequence End1937115
Gene Sequence:
>1443 bp
ATGTCCAGAAGGCTTCGCAGAACAAAAATCGTTACCACGTTAGGCCCAGCAACAGATCGC
GATAATAATCTTGAAAAAGTTATCGCGGCGGGTGCCAACGTTGTACGTATGAACTTTTCT
CACGGCTCGCCTGAAGATCACAAAATGCGCGCGGATAAAGTTCGTGAGATTGCCGCAAAA
CTGGGGCGTCATGTGGCTATTCTGGGTGACCTCCAGGGGCCCAAAATCCGTGTATCCACC
TTTAAAGAAGGCAAAGTTTTCCTCAATATTGGGGATAAATTCCTGCTCGACGCCAACCTG
GGTAAAGGTGAAGGCGACAAAGAAAAAGTCGGTATCGACTACAAAGGCCTGCCTGCTGAC
GTCGTGCCTGGTGACATCCTGCTGCTGGACGATGGTCGCGTCCAGTTAAAAGTACTGGAA
GTTCAGGGCATGAAAGTGTTCACCGAAGTCACCGTCGGTGGTCCCCTCTCCAACAATAAA
GGTATCAACAAACTTGGCGGCGGTTTGTCGGCTGAAGCGCTGACCGAAAAAGACAAAGCA
GACATTAAGACTGCGGCGTTGATTGGCGTAGATTACCTGGCTGTCTCCTTCCCACGCTGT
GGCGAAGATCTGAACTATGCCCGTCGCCTGGCACGCGATGCAGGATGTGATGCGAAAATT
GTTGCCAAGGTTGAACGTGCGGAAGCCGTTTGCAGCCAGGATGCAATGGATGACATCATC
CTCGCCTCTGACGTGGTAATGGTTGCACGTGGCGACCTCGGTGTGGAAATTGGCGACCCG
GAACTGGTCGGCATTCAGAAAGCGTTGATCCGTCGTGCGCGTCAGCTAAACCGAGCGGTA
ATCACGGCGACCCAGATGATGGAGTCAATGATTACTAACCCGATGCCGACGCGTGCAGAA
GTCATGGACGTAGCAAACGCCGTTCTGGATGGTACTGACGCTGTGATGCTGTCTGCAGAA
ACTGCCGCTGGGCAGTATCCGTCAGAAACCGTTGCAGCCATGGCGCGCGTTTGCCTGGGT
GCGGAAAAAATCCCGAGCATCAACGTTTCTAAACACCGTCTGGACGTTCAGTTCGACAAT
GTGGAAGAAGCTATTGCCATGTCAGCAATGTACGCAGCTAACCACCTGAAAGGCGTTACG
GCGATCATCACCATGACCGAATCGGGTCGTACCGCGCTGATGACCTCCCGTATCAGCTCT
GGTCTGCCAATTTTCGCCATGTCGCGCCATGAACGTACGCTGAACCTGACTGCTCTCTAT
CGTGGCGTTACGCCGGTGCACTTTGATAGCGCTAATGACGGCGTAGCAGCTGCCAGCGAA
GCGGTTAATCTGCTGCGCGATAAAGGTTACTTGATGTCTGGTGACCTGGTGATTGTCACC
CAGGGCGACGTGATGAGTACCGTGGGTTCTACTAATACCACGCGTATTTTAACGGTAGAG
TAA
Protein Properties
Pfam Domain Function:
Protein Residues:480
Protein Molecular Weight:51357
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Pyruvate kinase II
MSRRLRRTKIVTTLGPATDRDNNLEKVIAAGANVVRMNFSHGSPEDHKMRADKVREIAAK
LGRHVAILGDLQGPKIRVSTFKEGKVFLNIGDKFLLDANLGKGEGDKEKVGIDYKGLPAD
VVPGDILLLDDGRVQLKVLEVQGMKVFTEVTVGGPLSNNKGINKLGGGLSAEALTEKDKA
DIKTAALIGVDYLAVSFPRCGEDLNYARRLARDAGCDAKIVAKVERAEAVCSQDAMDDII
LASDVVMVARGDLGVEIGDPELVGIQKALIRRARQLNRAVITATQMMESMITNPMPTRAE
VMDVANAVLDGTDAVMLSAETAAGQYPSETVAAMARVCLGAEKIPSINVSKHRLDVQFDN
VEEAIAMSAMYAANHLKGVTAIITMTESGRTALMTSRISSGLPIFAMSRHERTLNLTALY
RGVTPVHFDSANDGVAAASEAVNLLRDKGYLMSGDLVIVTQGDVMSTVGSTNTTRILTVE
References
External Links:
ResourceLink
Uniprot ID:P21599
Uniprot Name:KPYK2_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1736497
Ecogene ID:EG10803
Ecocyc:EG10803
ColiBase:b1854
Kegg Gene:b1854
EchoBASE ID:EB0796
CCDB:KPYK2_ECOLI
BacMap:16129807
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
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., 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., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040
  • Karow, M., Georgopoulos, C. (1992). "Isolation and characterization of the Escherichia coli msbB gene, a multicopy suppressor of null mutations in the high-temperature requirement gene htrB." J Bacteriol 174:702-710. Pubmed: 1732206
  • Valentini, G., Stoppini, M., Iadarola, P., Malcovati, M., Ferri, G., Speranza, M. L. (1993). "Divergent binding sites in pyruvate kinases I and II from Escherichia coli." Biol Chem Hoppe Seyler 374:69-74. Pubmed: 8439398
  • Valentini, G., Stoppini, M., Speranza, M. L., Malcovati, M., Ferri, G. (1991). "Bacterial pyruvate kinases have a shorter N-terminal domain." Biol Chem Hoppe Seyler 372:91-93. Pubmed: 1859631
  • 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