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A8A466 (PGK_ECOHS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:EcHS_A3084
OrganismEscherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]
Taxonomic identifier331112 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length387 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_00145

Subcellular location

Cytoplasm Potential 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 termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglycerate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 387387Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000057983

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 By similarity

Sequences

Sequence LengthMass (Da)Tools
A8A466 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: FAD7D36D43DE4269

FASTA38741,104
        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 
EAKRLLSTCN IPVPSDVRVA TEFSETAPAT LKSVNDVKAD EQILDIGDAS AQELAEILKN 

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

       370        380 
TGGGAFLEFV EGKVLPAVAM LEERAKK 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000802 Genomic DNA. Translation: ABV07320.1.
RefSeqYP_001459703.1. NC_009800.1.

3D structure databases

ProteinModelPortalA8A466.
SMRA8A466. Positions 2-387.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING331112.EcHS_A3084.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV07320; ABV07320; EcHS_A3084.
GeneID5593968.
KEGGecx:EcHS_A3084.
PATRIC18316149. VBIEscCol77814_3014.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMADMIFDIG.
OrthoDBEOG64N9Z0.
ProtClustDBPRK00073.

Enzyme and pathway databases

BioCycECOL331112:GHHI-3075-MONOMER.
UniPathwayUPA00109; UER00185.

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...

Entry information

Entry namePGK_ECOHS
AccessionPrimary (citable) accession number: A8A466
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: February 19, 2014
This is version 39 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

PATHWAY comments

Index of metabolic and biosynthesis pathways