ECMDB: Pyruvate kinase I (P0AD61)

Identification

Name:

Pyruvate kinase I

Synonyms:

PK-1

Gene Name:

pykF

Enzyme Class:

2.7.1.40

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:

Carbon fixation in photosynthetic organisms ec00710
Glycolysis / Gluconeogenesis ec00010
Metabolic pathways eco01100
Microbial metabolism in diverse environments ec01120
Purine metabolism ec00230
Pyruvate metabolism ec00620

KEGG Reactions:

1.0

↔

1.0

1.0ADP + 1.0Hydrogen ion + 1.0Phosphoenolpyruvic acid ↔ 1.0Adenosine triphosphate + 1.0Pyruvic acid
ReactionCard

1.0

↔

1.0

1.0Adenosine triphosphate + 1.0Pyruvic acid ↔ 1.0ADP + 1.0Phosphoenolpyruvic acid
ReactionCard

1.0

↔

1.0

1.0Guanosine triphosphate + 1.0Pyruvic acid ↔ 1.0Guanosine diphosphate + 1.0Phosphoenolpyruvic acid
ReactionCard

1.0

↔

1.0

1.0dATP + 1.0Pyruvic acid ↔ 1.0dADP + 1.0Phosphoenolpyruvic acid
ReactionCard

1.0

↔

1.0dGDP

1.0

1.0dGTP + 1.0Pyruvic acid ↔ 1.0dGDP + 1.0Phosphoenolpyruvic acid
ReactionCard

1.0Nucleoside triphosphate

1.0

↔

1.0NDP

1.0

1.0Nucleoside triphosphate + 1.0Pyruvic acid ↔ 1.0NDP + 1.0Phosphoenolpyruvic acid
ReactionCard

SMPDB Reactions:

1.0

1.0Adenosine diphosphate

1.0

→

1.0

1.0Phosphoenolpyruvic acid + 1.0Adenosine diphosphate + 1.0Hydrogen ion + 1.0ADP → 1.0Adenosine triphosphate + 1.0Pyruvic acid
ReactionCard

EcoCyc Reactions:

1.0

↔

1.0

1.0ADP + 1.0Hydrogen ion + 1.0Phosphoenolpyruvic acid ↔ 1.0Adenosine triphosphate + 1.0Pyruvic acid
ReactionCard

Complex Reactions:

1.0

→

1.0

1.0Adenosine triphosphate + 1.0Pyruvic acid → 1.0ADP + 1.0Phosphoenolpyruvic acid
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB00538	Adenosine triphosphate	MetaboCard
ECMDB01341	ADP	MetaboCard
ECMDB21326	dADP	MetaboCard
ECMDB01532	dATP	MetaboCard
ECMDB00960	dGDP	MetaboCard
ECMDB01440	dGTP	MetaboCard
ECMDB01201	Guanosine diphosphate	MetaboCard
ECMDB01273	Guanosine triphosphate	MetaboCard
ECMDB21225	Hydrogen ion	MetaboCard
ECMDB00263	Phosphoenolpyruvic acid	MetaboCard
ECMDB00243	Pyruvic acid	MetaboCard

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 Orientation

Clockwise

Centisome Percentage:

37.80

Left Sequence End

1753722

Right Sequence End

1755134

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:

PK (PF00224 )
PK_C (PF02887 )

Protein Residues:

470

Protein Molecular Weight:

50729

Protein Theoretical pI:

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:

Resource	Link
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