Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0AD61 (KPYK1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate kinase I

EC=2.7.1.40
Alternative name(s):
PK-1
Gene names
Name:pykF
Ordered Locus Names:b1676, JW1666
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length470 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactor

Magnesium.

Potassium.

Enzyme regulation

Belongs to type I PK; fructose 1,6-bisphosphate-activated.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 470470Pyruvate kinase I
PRO_0000112069

Sites

Metal binding341Potassium By similarity
Metal binding361Potassium By similarity
Metal binding661Potassium By similarity
Metal binding671Potassium; via carbonyl oxygen By similarity
Metal binding2221Magnesium By similarity
Metal binding2461Magnesium By similarity
Binding site321Substrate By similarity
Binding site2451Substrate; via amide nitrogen By similarity
Binding site2461Substrate; via amide nitrogen By similarity
Binding site2781Substrate By similarity
Site2201Transition state stabilizer By similarity

Amino acid modifications

Modified residue761N6-acetyllysine Ref.10
Modified residue3191N6-acetyllysine Ref.10

Experimental info

Sequence conflict441G → S AA sequence Ref.6
Sequence conflict3791Q → N AA sequence Ref.8
Sequence conflict4011T → D AA sequence Ref.8
Sequence conflict451 – 47020MVSGA…SVHVL → YGFWCTGTERHY Ref.1
Sequence conflict451 – 47020MVSGA…SVHVL → YGFWCTGTERHY Ref.3

Secondary structure

........................................................................................ 470
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AD61 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: E29BF01B90327D8B

FASTA47050,729
        10         20         30         40         50         60 
MKKTKIVCTI GPKTESEEML AKMLDAGMNV MRLNFSHGDY AEHGQRIQNL RNVMSKTGKT 

        70         80         90        100        110        120 
AAILLDTKGP EIRTMKLEGG NDVSLKAGQT FTFTTDKSVI GNSEMVAVTY EGFTTDLSVG 

       130        140        150        160        170        180 
NTVLVDDGLI GMEVTAIEGN KVICKVLNNG DLGENKGVNL PGVSIALPAL AEKDKQDLIF 

       190        200        210        220        230        240 
GCEQGVDFVA ASFIRKRSDV IEIREHLKAH GGENIHIISK IENQEGLNNF DEILEASDGI 

       250        260        270        280        290        300 
MVARGDLGVE IPVEEVIFAQ KMMIEKCIRA RKVVITATQM LDSMIKNPRP TRAEAGDVAN 

       310        320        330        340        350        360 
AILDGTDAVM LSGESAKGKY PLEAVSIMAT ICERTDRVMN SRLEFNNDNR KLRITEAVCR 

       370        380        390        400        410        420 
GAVETAEKLD APLIVVATQG GKSARAVRKY FPDATILALT TNEKTAHQLV LSKGVVPQLV 

       430        440        450        460        470 
KEITSTDDFY RLGKELALQS GLAHKGDVVV MVSGALVPSG TTNTASVHVL 

« Hide

References

« Hide 'large scale' references
[1]"Direct genomic sequencing of bacterial DNA: the pyruvate kinase I gene of Escherichia coli."
Ohara O., Dorit R.L., Gilbert W.
Proc. Natl. Acad. Sci. U.S.A. 86:6883-6887(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of the boundaries of Salmonella pathogenicity island 2 and the corresponding chromosomal region of Escherichia coli K-12."
Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R., Holden D.W.
J. Bacteriol. 179:1105-1111(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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."
Aiba H., Baba T., Fujita K., 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. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"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.
[5]"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], SEQUENCE REVISION TO 451-470.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"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 1-48.
[7]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-11.
Strain: K12 / EMG2.
[8]"Primary structure of three peptides at the catalytic and allosteric sites of the fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia coli."
Speranza M.L., Valentini G., Iadarola P., Stoppini M., Malcovati M., Ferri G.
Biol. Chem. Hoppe-Seyler 370:211-216(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 293-319; 369-385 AND 389-404.
[9]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[10]"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-76 AND LYS-319, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[11]"Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition."
Mattevi A., Valentini G., Rizzi M., Speranza M.L., Bolognesi M., Coda A.
Structure 3:729-741(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[12]"The allosteric regulation of pyruvate kinase."
Valentini G., Chiarelli L., Fortin R., Speranza M.L., Galizzi A., Mattevi A.
J. Biol. Chem. 275:18145-18152(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24636 Genomic DNA. Translation: AAA24392.1.
U68703 Genomic DNA. Translation: AAB47952.1.
U00096 Genomic DNA. Translation: AAC74746.1.
AP009048 Genomic DNA. Translation: BAA15445.2.
PIRD64925.
RefSeqNP_416191.1. NC_000913.3.
YP_489938.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E0TX-ray1.80A/B/C/D1-470[»]
1E0UX-ray2.80A/B/C/D1-470[»]
1PKYX-ray2.50A/B/C/D1-470[»]
ProteinModelPortalP0AD61.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36221N.
IntActP0AD61. 21 interactions.
STRING511145.b1676.

PTM databases

PhosSiteP0810429.

2D gel databases

SWISS-2DPAGEP0AD61.

Proteomic databases

PaxDbP0AD61.
PRIDEP0AD61.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74746; AAC74746; b1676.
BAA15445; BAA15445; BAA15445.
GeneID12931281.
946179.
KEGGecj:Y75_p1651.
eco:b1676.
PATRIC32118658. VBIEscCol129921_1747.

Organism-specific databases

EchoBASEEB0797.
EcoGeneEG10804. pykF.

Phylogenomic databases

eggNOGCOG0469.
HOGENOMHOG000021559.
KOK00873.
OMACIVENAG.
OrthoDBEOG6GBMB0.
PhylomeDBP0AD61.

Enzyme and pathway databases

BioCycEcoCyc:PKI-MONOMER.
ECOL316407:JW1666-MONOMER.
MetaCyc:PKI-MONOMER.
SABIO-RKP0AD61.
UniPathwayUPA00109; UER00188.

Gene expression databases

GenevestigatorP0AD61.

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

EvolutionaryTraceP0AD61.
PROP0AD61.

Entry information

Entry nameKPYK1_ECOLI
AccessionPrimary (citable) accession number: P0AD61
Secondary accession number(s): P14178 expand/collapse secondary AC list , P76921, P78165, P78231
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: June 11, 2014
This is version 89 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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