Pyruvate kinase II - Escherichia coli (strain K12)

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P21599 (KPYK2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Pyruvate kinase II
EC=2.7.1.40

Alternative name(s):
PK-2

Gene names

Name:	pykA
Ordered Locus Names:	b1854, JW1843

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro potassium ion binding Inferred from electronic annotation. Source: InterPro pyruvate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.7

Chain

2 – 480

479

Pyruvate kinase II

PRO_0000112073

Sites

Metal binding

Potassium By similarity

Metal binding

Potassium By similarity

Metal binding

Potassium By similarity

Metal binding

225

Magnesium By similarity

Metal binding

252

Magnesium By similarity

Binding site

Substrate By similarity

Binding site

251

Substrate; via amide nitrogen By similarity

Binding site

252

Substrate; via amide nitrogen By similarity

Binding site

284

Substrate By similarity

Site

223

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

351

N6-acetyllysine Ref.9

Experimental info

Sequence conflict

R → C AA sequence Ref.7

Sequence conflict

S → G AA sequence Ref.7

Sequence conflict

323

A → R in AAA96707. Ref.6

Sequence conflict

383

Missing in AAA96707. Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P21599 [UniParc].

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

FASTA

480

51,357

        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' referencesShow '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. Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 1732206] [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: 1859631] [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: 8439398] [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: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-351, 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.
PIR	S29790.
RefSeq	NP_416368.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P21599.
SMR	P21599. Positions 5-479.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10622N.
IntAct	P21599. 17 interactions.
MINT	MINT-1238649.
Proteomic databases
PRIDE	P21599.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000004674; EBESCP00000004674; EBESCG00000003816. EBESCT00000014499; EBESCP00000013790; EBESCG00000013560.
GeneID	946527.
GenomeReviews	Gene locus JW1843 in contig AP009048_GR. Gene locus b1854 in contig U00096_GR.
KEGG	ecj:JW1843. eco:b1854.
PATRIC	32119031. VBIEscCol129921_1933.
Organism-specific databases
EchoBASE	EB0796.
EcoGene	EG10803. pykA.
Phylogenomic databases
eggNOG	COG0469.
GeneTree	EBGT00050000009296.
HOGENOM	HBG734376.
OMA	SRSRQLN.
PhylomeDB	P21599.
ProtClustDB	PRK05826.
Enzyme and pathway databases
BioCyc	EcoCyc:PKII-MONOMER. MetaCyc:PKII-MONOMER.
Gene expression databases
Genevestigator	P21599.
Family and domain databases
InterPro	IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase. 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]
Gene3D	G3DSA:2.40.33.10. PK_B_barrel_like. 1 hit. G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 2 hits. G3DSA:3.40.1380.20. Pyrv_Knase_a/b. 1 hit.
KO	K00873.
PANTHER	PTHR11817. Pyruvate_kinase. 1 hit.
Pfam	PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view]
PRINTS	PR01050. PYRUVTKNASE.
SUPFAM	SSF50800. PK_B_barrel_like. 1 hit. SSF52935. Pyruvate_kinase. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMs	TIGR01064. Pyruv_kin. 1 hit.
PROSITE	PS00110. PYRUVATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPYK2_ECOLI

Accession

Primary (citable) accession number: P21599

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents