Pyruvate kinase I (P0AD61)

Identification
Name:Pyruvate kinase I
Synonyms:
  • PK-1
Gene Name:pykF
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
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyruvic acid → 1.0ADP + 1.0Phosphoenolpyruvic 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:b1676
Gene OrientationClockwise
Centisome Percentage:37.80
Left Sequence End1753722
Right Sequence End1755134
Gene Sequence:
>1413 bp
ATGAAAAAGACCAAAATTGTTTGCACCATCGGACCGAAAACCGAATCTGAAGAGATGTTA
GCTAAAATGCTGGACGCTGGCATGAACGTTATGCGTCTGAACTTCTCTCATGGTGACTAT
GCAGAACACGGTCAGCGCATTCAGAATCTGCGCAACGTGATGAGCAAAACTGGTAAAACC
GCCGCTATCCTGCTTGATACCAAAGGTCCGGAAATCCGCACCATGAAACTGGAAGGCGGT
AACGACGTTTCTCTGAAAGCTGGTCAGACCTTTACTTTCACCACTGATAAATCTGTTATC
GGCAACAGCGAAATGGTTGCGGTAACGTATGAAGGTTTCACTACTGACCTGTCTGTTGGC
AACACCGTACTGGTTGACGATGGTCTGATCGGTATGGAAGTTACCGCCATTGAAGGTAAC
AAAGTTATCTGTAAAGTGCTGAACAACGGTGACCTGGGCGAAAACAAAGGTGTGAACCTG
CCTGGCGTTTCCATTGCTCTGCCAGCACTGGCTGAAAAAGACAAACAGGACCTGATCTTT
GGTTGCGAACAAGGCGTAGACTTTGTTGCTGCTTCCTTTATTCGTAAGCGTTCTGACGTT
ATCGAAATCCGTGAGCACCTGAAAGCGCACGGCGGCGAAAACATCCACATCATCTCCAAA
ATCGAAAACCAGGAAGGCCTCAACAACTTCGACGAAATCCTCGAAGCCTCTGACGGCATC
ATGGTTGCGCGTGGCGACCTGGGTGTAGAAATCCCGGTAGAAGAAGTTATCTTCGCCCAG
AAGATGATGATCGAAAAATGTATCCGTGCACGTAAAGTCGTTATCACTGCGACCCAGATG
CTGGATTCCATGATCAAAAACCCACGCCCGACTCGCGCAGAAGCCGGTGACGTTGCAAAC
GCCATCCTCGACGGTACTGACGCAGTGATGCTGTCTGGTGAATCCGCAAAAGGTAAATAC
CCGCTGGAAGCGGTTTCTATCATGGCGACCATCTGCGAACGTACCGACCGCGTGATGAAC
AGCCGTCTCGAGTTCAACAATGACAACCGTAAACTGCGCATTACCGAAGCGGTATGCCGT
GGTGCCGTTGAAACTGCTGAAAAACTGGATGCTCCGCTGATCGTGGTTGCTACTCAGGGC
GGTAAATCTGCTCGCGCAGTACGTAAATACTTCCCGGATGCCACCATCCTGGCACTGACC
ACCAACGAAAAAACGGCTCATCAGTTGGTACTGAGCAAAGGCGTTGTGCCGCAGCTTGTT
AAAGAGATCACTTCTACTGATGATTTCTACCGTCTGGGTAAAGAACTGGCTCTGCAGAGC
GGTCTGGCACACAAAGGTGACGTTGTAGTTATGGTTTCTGGTGCACTGGTACCGAGCGGC
ACTACTAACACCGCATCTGTTCACGTCCTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:470
Protein Molecular Weight:50729
Protein Theoretical pI:6
PDB File:1PKY
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Pyruvate kinase I
MKKTKIVCTIGPKTESEEMLAKMLDAGMNVMRLNFSHGDYAEHGQRIQNLRNVMSKTGKT
AAILLDTKGPEIRTMKLEGGNDVSLKAGQTFTFTTDKSVIGNSEMVAVTYEGFTTDLSVG
NTVLVDDGLIGMEVTAIEGNKVICKVLNNGDLGENKGVNLPGVSIALPALAEKDKQDLIF
GCEQGVDFVAASFIRKRSDVIEIREHLKAHGGENIHIISKIENQEGLNNFDEILEASDGI
MVARGDLGVEIPVEEVIFAQKMMIEKCIRARKVVITATQMLDSMIKNPRPTRAEAGDVAN
AILDGTDAVMLSGESAKGKYPLEAVSIMATICERTDRVMNSRLEFNNDNRKLRITEAVCR
GAVETAEKLDAPLIVVATQGGKSARAVRKYFPDATILALTTNEKTAHQLVLSKGVVPQLV
KEITSTDDFYRLGKELALQSGLAHKGDVVVMVSGALVPSGTTNTASVHVL
References
External Links:
ResourceLink
Uniprot ID:P0AD61
Uniprot Name:KPYK1_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675072
PDB ID:1PKY
Ecogene ID:EG10804
Ecocyc:EG10804
ColiBase:b1676
Kegg Gene:b1676
EchoBASE ID:EB0797
CCDB:KPYK1_ECOLI
BacMap:16129632
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
  • 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
  • Hensel, M., Shea, J. E., Baumler, A. J., Gleeson, C., Blattner, F., Holden, D. W. (1997). "Analysis of the boundaries of Salmonella pathogenicity island 2 and the corresponding chromosomal region of Escherichia coli K-12." J Bacteriol 179:1105-1111. Pubmed: 9023191
  • 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
  • Mattevi, A., Valentini, G., Rizzi, M., Speranza, M. L., Bolognesi, M., Coda, A. (1995). "Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition." Structure 3:729-741. Pubmed: 8591049
  • Ohara, O., Dorit, R. L., Gilbert, W. (1989). "Direct genomic sequencing of bacterial DNA: the pyruvate kinase I gene of Escherichia coli." Proc Natl Acad Sci U S A 86:6883-6887. Pubmed: 2674937
  • Speranza, M. L., Valentini, G., Iadarola, P., Stoppini, M., Malcovati, M., Ferri, G. (1989). "Primary structure of three peptides at the catalytic and allosteric sites of the fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia coli." Biol Chem Hoppe Seyler 370:211-216. Pubmed: 2653362
  • Valentini, G., Chiarelli, L., Fortin, R., Speranza, M. L., Galizzi, A., Mattevi, A. (2000). "The allosteric regulation of pyruvate kinase." J Biol Chem 275:18145-18152. Pubmed: 10751408
  • 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