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P21599

- KPYK2_ECOLI

UniProt

P21599 - KPYK2_ECOLI

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Protein

Pyruvate kinase II

Gene

pykA

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

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Magnesium.
Potassium.

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361SubstrateBy similarity
Metal bindingi38 – 381PotassiumBy similarity
Metal bindingi40 – 401PotassiumBy similarity
Metal bindingi70 – 701PotassiumBy similarity
Sitei223 – 2231Transition state stabilizerBy similarity
Metal bindingi225 – 2251MagnesiumBy similarity
Binding sitei251 – 2511Substrate; via amide nitrogenBy similarity
Metal bindingi252 – 2521MagnesiumBy similarity
Binding sitei252 – 2521Substrate; via amide nitrogenBy similarity
Binding sitei284 – 2841SubstrateBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. magnesium ion binding Source: InterPro
  4. potassium ion binding Source: InterPro
  5. pyruvate kinase activity Source: EcoCyc

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
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:PKII-MONOMER.
ECOL316407:JW1843-MONOMER.
MetaCyc:PKII-MONOMER.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase II (EC:2.7.1.40)
Alternative name(s):
PK-2
Gene namesi
Name:pykA
Ordered Locus Names:b1854, JW1843
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10803. pykA.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 480479Pyruvate kinase IIPRO_0000112073Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei351 – 3511N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP21599.
PRIDEiP21599.

Expressioni

Gene expression databases

GenevestigatoriP21599.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-368956,EBI-368956
malXP196423EBI-368956,EBI-556578
yggRP520523EBI-368956,EBI-552531

Protein-protein interaction databases

DIPiDIP-10622N.
IntActiP21599. 15 interactions.
MINTiMINT-1238649.
STRINGi511145.b1854.

Structurei

3D structure databases

ProteinModelPortaliP21599.
SMRiP21599. Positions 4-476.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021558.
InParanoidiP21599.
KOiK00873.
OMAiTPVYFDS.
OrthoDBiEOG6GBMB0.
PhylomeDBiP21599.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21599-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRRLRRTKI VTTLGPATDR DNNLEKVIAA GANVVRMNFS HGSPEDHKMR
60 70 80 90 100
ADKVREIAAK LGRHVAILGD LQGPKIRVST FKEGKVFLNI GDKFLLDANL
110 120 130 140 150
GKGEGDKEKV GIDYKGLPAD VVPGDILLLD DGRVQLKVLE VQGMKVFTEV
160 170 180 190 200
TVGGPLSNNK GINKLGGGLS AEALTEKDKA DIKTAALIGV DYLAVSFPRC
210 220 230 240 250
GEDLNYARRL ARDAGCDAKI VAKVERAEAV CSQDAMDDII LASDVVMVAR
260 270 280 290 300
GDLGVEIGDP ELVGIQKALI RRARQLNRAV ITATQMMESM ITNPMPTRAE
310 320 330 340 350
VMDVANAVLD GTDAVMLSAE TAAGQYPSET VAAMARVCLG AEKIPSINVS
360 370 380 390 400
KHRLDVQFDN VEEAIAMSAM YAANHLKGVT AIITMTESGR TALMTSRISS
410 420 430 440 450
GLPIFAMSRH ERTLNLTALY RGVTPVHFDS ANDGVAAASE AVNLLRDKGY
460 470 480
LMSGDLVIVT QGDVMSTVGS TNTTRILTVE
Length:480
Mass (Da):51,357
Last modified:January 23, 2007 - v3
Checksum:iC37F004C374D27E9
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201R → C AA sequence (PubMed:1859631)Curated
Sequence conflicti43 – 431S → G AA sequence (PubMed:1859631)Curated
Sequence conflicti323 – 3231A → R in AAA96707. 1 PublicationCurated
Sequence conflicti383 – 3831Missing in AAA96707. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS29790.
RefSeqiNP_416368.1. NC_000913.3.
YP_490116.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74924; AAC74924; b1854.
BAA15662; BAA15662; BAA15662.
GeneIDi12934211.
946527.
KEGGiecj:Y75_p1830.
eco:b1854.
PATRICi32119031. VBIEscCol129921_1933.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRi S29790.
RefSeqi NP_416368.1. NC_000913.3.
YP_490116.1. NC_007779.1.

3D structure databases

ProteinModelPortali P21599.
SMRi P21599. Positions 4-476.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10622N.
IntActi P21599. 15 interactions.
MINTi MINT-1238649.
STRINGi 511145.b1854.

Proteomic databases

PaxDbi P21599.
PRIDEi P21599.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74924 ; AAC74924 ; b1854 .
BAA15662 ; BAA15662 ; BAA15662 .
GeneIDi 12934211.
946527.
KEGGi ecj:Y75_p1830.
eco:b1854.
PATRICi 32119031. VBIEscCol129921_1933.

Organism-specific databases

EchoBASEi EB0796.
EcoGenei EG10803. pykA.

Phylogenomic databases

eggNOGi COG0469.
HOGENOMi HOG000021558.
InParanoidi P21599.
KOi K00873.
OMAi TPVYFDS.
OrthoDBi EOG6GBMB0.
PhylomeDBi P21599.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .
BioCyci EcoCyc:PKII-MONOMER.
ECOL316407:JW1843-MONOMER.
MetaCyc:PKII-MONOMER.

Miscellaneous databases

PROi P21599.

Gene expression databases

Genevestigatori P21599.

Family and domain databases

Gene3Di 2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProi IPR001697. 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 ]
PANTHERi PTHR11817. PTHR11817. 1 hit.
Pfami PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view ]
PRINTSi PR01050. PYRUVTKNASE.
SUPFAMi SSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
PROSITEi PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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.

Entry informationi

Entry nameiKPYK2_ECOLI
AccessioniPrimary (citable) accession number: P21599
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3