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P21599 (KPYK2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate kinase II

EC=2.7.1.40
Alternative name(s):
PK-2
Gene names
Name:pykA
Ordered Locus Names:b1854, JW1843
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactor

Magnesium.

Potassium.

Enzyme regulation

Allosterically activated by AMP and by several sugar phosphates. Belongs to type II PK.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the pyruvate kinase family.

Sequence caution

The sequence AAA96707.1 differs from that shown. Reason: Frameshift at position 441.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 480479Pyruvate kinase II
PRO_0000112073

Sites

Metal binding381Potassium By similarity
Metal binding401Potassium By similarity
Metal binding701Potassium By similarity
Metal binding2251Magnesium By similarity
Metal binding2521Magnesium By similarity
Binding site361Substrate By similarity
Binding site2511Substrate; via amide nitrogen By similarity
Binding site2521Substrate; via amide nitrogen By similarity
Binding site2841Substrate By similarity
Site2231Transition state stabilizer By similarity

Amino acid modifications

Modified residue3511N6-acetyllysine Ref.9

Experimental info

Sequence conflict201R → C AA sequence Ref.7
Sequence conflict431S → G AA sequence Ref.7
Sequence conflict3231A → R in AAA96707. Ref.6
Sequence conflict3831Missing in AAA96707. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P21599 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C37F004C374D27E9

FASTA48051,357
        10         20         30         40         50         60 
MSRRLRRTKI VTTLGPATDR DNNLEKVIAA GANVVRMNFS HGSPEDHKMR ADKVREIAAK 

        70         80         90        100        110        120 
LGRHVAILGD LQGPKIRVST FKEGKVFLNI GDKFLLDANL GKGEGDKEKV GIDYKGLPAD 

       130        140        150        160        170        180 
VVPGDILLLD DGRVQLKVLE VQGMKVFTEV TVGGPLSNNK GINKLGGGLS AEALTEKDKA 

       190        200        210        220        230        240 
DIKTAALIGV DYLAVSFPRC GEDLNYARRL ARDAGCDAKI VAKVERAEAV CSQDAMDDII 

       250        260        270        280        290        300 
LASDVVMVAR GDLGVEIGDP ELVGIQKALI RRARQLNRAV ITATQMMESM ITNPMPTRAE 

       310        320        330        340        350        360 
VMDVANAVLD GTDAVMLSAE TAAGQYPSET VAAMARVCLG AEKIPSINVS KHRLDVQFDN 

       370        380        390        400        410        420 
VEEAIAMSAM YAANHLKGVT AIITMTESGR TALMTSRISS GLPIFAMSRH ERTLNLTALY 

       430        440        450        460        470        480 
RGVTPVHFDS ANDGVAAASE AVNLLRDKGY LMSGDLVIVT QGDVMSTVGS TNTTRILTVE 

« Hide

References

« Hide 'large scale' references
[1]Bledig S.A., Fotheringham I.G., Hunter M.G.
Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"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."
Itoh T., Aiba H., Baba T., Fujita K., 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. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, 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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Isolation and characterization of the Escherichia coli msbB gene, a multicopy suppressor of null mutations in the high-temperature requirement gene htrB."
Karow M.L., Georgopoulos C.
J. Bacteriol. 174:702-710(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 319-480.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]Engel H., Smink A.J., Keck W.
Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 323-480.
Strain: K12.
[7]"Bacterial pyruvate kinases have a shorter N-terminal domain."
Valentini G., Stoppini M., Speranza M.L., Malcovati M., Ferri G.
Biol. Chem. Hoppe-Seyler 372:91-93(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-44.
[8]"Divergent binding sites in pyruvate kinases I and II from Escherichia coli."
Valentini G., Stoppini M., Iadarola P., Malcovati M., Ferri G., Speranza M.L.
Biol. Chem. Hoppe-Seyler 374:69-74(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 64-77; 83-107; 251-272 AND 337-353.
[9]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-351, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63703 Genomic DNA. Translation: AAA24473.1.
U00096 Genomic DNA. Translation: AAC74924.1.
AP009048 Genomic DNA. Translation: BAA15662.1.
M77039 Genomic DNA. No translation available.
M87660 Genomic DNA. Translation: AAA96707.1. Frameshift.
PIRS29790.
RefSeqNP_416368.1. NC_000913.3.
YP_490116.1. NC_007779.1.

3D structure databases

ProteinModelPortalP21599.
SMRP21599. Positions 4-479.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10622N.
IntActP21599. 15 interactions.
MINTMINT-1238649.
STRING511145.b1854.

Proteomic databases

PaxDbP21599.
PRIDEP21599.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74924; AAC74924; b1854.
BAA15662; BAA15662; BAA15662.
GeneID12934211.
946527.
KEGGecj:Y75_p1830.
eco:b1854.
PATRIC32119031. VBIEscCol129921_1933.

Organism-specific databases

EchoBASEEB0796.
EcoGeneEG10803. pykA.

Phylogenomic databases

eggNOGCOG0469.
HOGENOMHOG000021558.
KOK00873.
OMATPVYFDS.
OrthoDBEOG6GBMB0.
PhylomeDBP21599.
ProtClustDBPRK05826.

Enzyme and pathway databases

BioCycEcoCyc:PKII-MONOMER.
ECOL316407:JW1843-MONOMER.
MetaCyc:PKII-MONOMER.
UniPathwayUPA00109; UER00188.

Gene expression databases

GenevestigatorP21599.

Family and domain databases

Gene3D2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERPTHR11817. PTHR11817. 1 hit.
PfamPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSPR01050. PYRUVTKNASE.
SUPFAMSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsTIGR01064. pyruv_kin. 1 hit.
PROSITEPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP21599.

Entry information

Entry nameKPYK2_ECOLI
AccessionPrimary (citable) accession number: P21599
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene