Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pyruvate kinase I

Gene

pykF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei32 – 321SubstrateBy similarity
Metal bindingi34 – 341PotassiumBy similarity
Metal bindingi36 – 361PotassiumBy similarity
Metal bindingi66 – 661PotassiumBy similarity
Metal bindingi67 – 671Potassium; via carbonyl oxygenBy similarity
Sitei220 – 2201Transition state stabilizerBy similarity
Metal bindingi222 – 2221MagnesiumBy similarity
Binding sitei245 – 2451Substrate; via amide nitrogenBy similarity
Metal bindingi246 – 2461MagnesiumBy similarity
Binding sitei246 – 2461Substrate; via amide nitrogenBy similarity
Binding sitei278 – 2781SubstrateBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. potassium ion binding Source: InterPro
  4. pyruvate kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
  2. response to heat Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

BioCyciEcoCyc:PKI-MONOMER.
ECOL316407:JW1666-MONOMER.
MetaCyc:PKI-MONOMER.
SABIO-RKP0AD61.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase I (EC:2.7.1.40)
Alternative name(s):
PK-1
Gene namesi
Name:pykF
Ordered Locus Names:b1676, JW1666
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10804. pykF.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Pyruvate kinase IPRO_0000112069Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761N6-acetyllysine1 Publication
Modified residuei319 – 3191N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0AD61.
PRIDEiP0AD61.

2D gel databases

SWISS-2DPAGEP0AD61.

PTM databases

PhosSiteiP0810429.

Expressioni

Gene expression databases

GenevestigatoriP0AD61.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

DIPiDIP-36221N.
IntActiP0AD61. 21 interactions.
STRINGi511145.b1676.

Structurei

Secondary structure

1
470
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Turni12 – 143Combined sources
Helixi17 – 2610Combined sources
Beta strandi30 – 345Combined sources
Helixi40 – 5718Combined sources
Beta strandi62 – 665Combined sources
Helixi78 – 803Combined sources
Beta strandi83 – 853Combined sources
Beta strandi90 – 956Combined sources
Beta strandi105 – 1095Combined sources
Helixi113 – 1164Combined sources
Beta strandi122 – 1254Combined sources
Turni126 – 1294Combined sources
Beta strandi130 – 1389Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi157 – 1593Combined sources
Helixi172 – 18312Combined sources
Beta strandi187 – 1937Combined sources
Helixi197 – 20812Combined sources
Turni209 – 2113Combined sources
Helixi212 – 2143Combined sources
Beta strandi215 – 2217Combined sources
Helixi224 – 2285Combined sources
Helixi230 – 2367Combined sources
Beta strandi237 – 2437Combined sources
Helixi244 – 2507Combined sources
Turni253 – 2553Combined sources
Helixi256 – 26914Combined sources
Beta strandi273 – 2775Combined sources
Beta strandi278 – 2814Combined sources
Helixi282 – 2854Combined sources
Helixi292 – 30413Combined sources
Beta strandi307 – 3115Combined sources
Helixi313 – 3164Combined sources
Helixi322 – 33615Combined sources
Helixi355 – 36814Combined sources
Beta strandi372 – 3776Combined sources
Beta strandi379 – 3813Combined sources
Helixi382 – 3898Combined sources
Beta strandi393 – 4019Combined sources
Helixi403 – 4086Combined sources
Helixi409 – 4113Combined sources
Beta strandi415 – 4195Combined sources
Helixi426 – 43914Combined sources
Beta strandi448 – 4536Combined sources
Beta strandi455 – 4573Combined sources
Beta strandi464 – 4696Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E0TX-ray1.80A/B/C/D1-470[»]
1E0UX-ray2.80A/B/C/D1-470[»]
1PKYX-ray2.50A/B/C/D1-470[»]
ProteinModelPortaliP0AD61.
SMRiP0AD61. Positions 1-470.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AD61.

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021559.
InParanoidiP0AD61.
KOiK00873.
OMAiDRVMKSR.
OrthoDBiEOG6GBMB0.
PhylomeDBiP0AD61.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. 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]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AD61-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKTKIVCTI GPKTESEEML AKMLDAGMNV MRLNFSHGDY AEHGQRIQNL
60 70 80 90 100
RNVMSKTGKT AAILLDTKGP EIRTMKLEGG NDVSLKAGQT FTFTTDKSVI
110 120 130 140 150
GNSEMVAVTY EGFTTDLSVG NTVLVDDGLI GMEVTAIEGN KVICKVLNNG
160 170 180 190 200
DLGENKGVNL PGVSIALPAL AEKDKQDLIF GCEQGVDFVA ASFIRKRSDV
210 220 230 240 250
IEIREHLKAH GGENIHIISK IENQEGLNNF DEILEASDGI MVARGDLGVE
260 270 280 290 300
IPVEEVIFAQ KMMIEKCIRA RKVVITATQM LDSMIKNPRP TRAEAGDVAN
310 320 330 340 350
AILDGTDAVM LSGESAKGKY PLEAVSIMAT ICERTDRVMN SRLEFNNDNR
360 370 380 390 400
KLRITEAVCR GAVETAEKLD APLIVVATQG GKSARAVRKY FPDATILALT
410 420 430 440 450
TNEKTAHQLV LSKGVVPQLV KEITSTDDFY RLGKELALQS GLAHKGDVVV
460 470
MVSGALVPSG TTNTASVHVL
Length:470
Mass (Da):50,729
Last modified:December 6, 2005 - v1
Checksum:iE29BF01B90327D8B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441G → S AA sequence (PubMed:1859631)Curated
Sequence conflicti379 – 3791Q → N AA sequence (PubMed:2653362)Curated
Sequence conflicti401 – 4011T → D AA sequence (PubMed:2653362)Curated
Sequence conflicti451 – 47020MVSGA…SVHVL → YGFWCTGTERHY(PubMed:2674937)CuratedAdd
BLAST
Sequence conflicti451 – 47020MVSGA…SVHVL → YGFWCTGTERHY(PubMed:9097039)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24636 Genomic DNA. Translation: AAA24392.1.
U68703 Genomic DNA. Translation: AAB47952.1.
U00096 Genomic DNA. Translation: AAC74746.1.
AP009048 Genomic DNA. Translation: BAA15445.2.
PIRiD64925.
RefSeqiNP_416191.1. NC_000913.3.
YP_489938.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74746; AAC74746; b1676.
BAA15445; BAA15445; BAA15445.
GeneIDi12931281.
946179.
KEGGiecj:Y75_p1651.
eco:b1676.
PATRICi32118658. VBIEscCol129921_1747.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24636 Genomic DNA. Translation: AAA24392.1.
U68703 Genomic DNA. Translation: AAB47952.1.
U00096 Genomic DNA. Translation: AAC74746.1.
AP009048 Genomic DNA. Translation: BAA15445.2.
PIRiD64925.
RefSeqiNP_416191.1. NC_000913.3.
YP_489938.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E0TX-ray1.80A/B/C/D1-470[»]
1E0UX-ray2.80A/B/C/D1-470[»]
1PKYX-ray2.50A/B/C/D1-470[»]
ProteinModelPortaliP0AD61.
SMRiP0AD61. Positions 1-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36221N.
IntActiP0AD61. 21 interactions.
STRINGi511145.b1676.

PTM databases

PhosSiteiP0810429.

2D gel databases

SWISS-2DPAGEP0AD61.

Proteomic databases

PaxDbiP0AD61.
PRIDEiP0AD61.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74746; AAC74746; b1676.
BAA15445; BAA15445; BAA15445.
GeneIDi12931281.
946179.
KEGGiecj:Y75_p1651.
eco:b1676.
PATRICi32118658. VBIEscCol129921_1747.

Organism-specific databases

EchoBASEiEB0797.
EcoGeneiEG10804. pykF.

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021559.
InParanoidiP0AD61.
KOiK00873.
OMAiDRVMKSR.
OrthoDBiEOG6GBMB0.
PhylomeDBiP0AD61.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
BioCyciEcoCyc:PKI-MONOMER.
ECOL316407:JW1666-MONOMER.
MetaCyc:PKI-MONOMER.
SABIO-RKP0AD61.

Miscellaneous databases

EvolutionaryTraceiP0AD61.
PROiP0AD61.

Gene expression databases

GenevestigatoriP0AD61.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. 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]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. 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. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Entry informationi

Entry nameiKPYK1_ECOLI
AccessioniPrimary (citable) accession number: P0AD61
Secondary accession number(s): P14178
, P76921, P78165, P78231
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: February 4, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.