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P0A799 (PGK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. 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:
Phosphoglycerate kinase

EC=2.7.2.3
Gene names
Name:pgk
Ordered Locus Names:b2926, JW2893
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length387 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 + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. HAMAP-Rule MF_00145

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. HAMAP-Rule MF_00145

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00145.

Sequence similarities

Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from direct assay PubMed 4932978. Source: EcoCyc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglycerate kinase activity

Inferred from direct assay PubMed 4932978. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.5 Ref.6
Chain2 – 387386Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_0000145941

Regions

Nucleotide binding340 – 3434ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1131Substrate By similarity
Binding site1461Substrate By similarity
Binding site1971ATP By similarity
Binding site3141ATP By similarity

Amino acid modifications

Modified residue841N6-acetyllysine Ref.7

Secondary structure

....................................................................... 387
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A799 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: FAD7D66D100514B2

FASTA38741,118
        10         20         30         40         50         60 
MSVIKMTDLD LAGKRVFIRA DLNVPVKDGK VTSDARIRAS LPTIELALKQ GAKVMVTSHL 

        70         80         90        100        110        120 
GRPTEGEYNE EFSLLPVVNY LKDKLSNPVR LVKDYLDGVD VAEGELVVLE NVRFNKGEKK 

       130        140        150        160        170        180 
DDETLSKKYA ALCDVFVMDA FGTAHRAQAS THGIGKFADV ACAGPLLAAE LDALGKALKE 

       190        200        210        220        230        240 
PARPMVAIVG GSKVSTKLTV LDSLSKIADQ LIVGGGIANT FIAAQGHDVG KSLYEADLVD 

       250        260        270        280        290        300 
EAKRLLTTCN IPVPSDVRVA TEFSETAPAT LKSVNDVKAD EQILDIGDAS AQELAEILKN 

       310        320        330        340        350        360 
AKTILWNGPV GVFEFPNFRK GTEIVANAIA DSEAFSIAGG GDTLAAIDLF GIADKISYIS 

       370        380 
TGGGAFLEFV EGKVLPAVAM LEERAKK 

« Hide

References

« Hide 'large scale' references
[1]"Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli."
Alefounder P.R., Perham R.N.
Mol. Microbiol. 3:723-732(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / CS520.
[2]"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.
[3]"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.
[4]"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 2-24.
Strain: K12 / EMG2.
[5]Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
Submitted (FEB-1996) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Protein identification with N and C-terminal sequence tags in proteome projects."
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.
J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-5.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"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-84, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14436 Genomic DNA. Translation: CAA32604.1.
U28377 Genomic DNA. Translation: AAA69093.1.
U00096 Genomic DNA. Translation: AAC75963.1.
AP009048 Genomic DNA. Translation: BAE76990.1.
PIRTVECG. S04733.
RefSeqNP_417401.1. NC_000913.3.
YP_491126.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZMRX-ray2.40A1-387[»]
ProteinModelPortalP0A799.
SMRP0A799. Positions 2-387.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36163N.
IntActP0A799. 15 interactions.
MINTMINT-1229247.
STRING511145.b2926.

PTM databases

PhosSiteP0810419.

2D gel databases

SWISS-2DPAGEP0A799.

Proteomic databases

PaxDbP0A799.
PRIDEP0A799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75963; AAC75963; b2926.
BAE76990; BAE76990; BAE76990.
GeneID12933840.
947414.
KEGGecj:Y75_p2857.
eco:b2926.
PATRIC32121266. VBIEscCol129921_3021.

Organism-specific databases

EchoBASEEB0697.
EcoGeneEG10703. pgk.

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAAGHPVGK.
OrthoDBEOG64N9Z0.
PhylomeDBP0A799.

Enzyme and pathway databases

BioCycEcoCyc:PGK.
ECOL316407:JW2893-MONOMER.
MetaCyc:PGK.
SABIO-RKP0A799.
UniPathwayUPA00109; UER00185.

Gene expression databases

GenevestigatorP0A799.

Family and domain databases

Gene3D3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPMF_00145. Phosphoglyc_kinase.
InterProIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERPTHR11406. PTHR11406. 1 hit.
PfamPF00162. PGK. 1 hit.
[Graphical view]
PIRSFPIRSF000724. Pgk. 1 hit.
PRINTSPR00477. PHGLYCKINASE.
SUPFAMSSF53748. SSF53748. 1 hit.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A799.
PROP0A799.

Entry information

Entry namePGK_ECOLI
AccessionPrimary (citable) accession number: P0A799
Secondary accession number(s): P11665, Q2M9R6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 86 of the entry and version 2 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