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Q4L4K4 (PGK_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 64. 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:SH2112
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length396 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
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

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 – 396396Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000009651

Regions

Nucleotide binding352 – 3554ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1191Substrate By similarity
Binding site1561Substrate By similarity
Binding site2061ATP By similarity
Binding site3251ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4L4K4 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: D74F11EEF00A6CDC

FASTA39642,432
        10         20         30         40         50         60 
MAKKIVSDLD LKGKVVLERA DFNVPLKDGK ITNDNRIVQA LPTIKYIIEQ GGKLVLFSHL 

        70         80         90        100        110        120 
GKVKQESDKE GLTLKPVADA LSEKLGKEVT FVPETRGKKL ESAIKNLSEG DVLLVENTRF 

       130        140        150        160        170        180 
EDLDGKKESK NDPELGKYWA SLGDVFVNDA FGTAHREHAS NVGISTHLET AAGYLMEKEI 

       190        200        210        220        230        240 
KFIGGVVNDP HKPVVAILGG AKVSDKIGVI KNLVNIADKI LIGGGMAYTF LKAQGKEIGL 

       250        260        270        280        290        300 
SLLEEDKIDF AKELLESNGD QIVLPVDAKV AKEFSNDAEI TEVSIDNIPS DQEAMDVGPK 

       310        320        330        340        350        360 
TVELFSKELE GAHTVVWNGP MGVFEFSNFA QGTIGVCKAI ANLKDATTII GGGDSAAAAI 

       370        380        390 
SLGFEDDFTH ISTGGGASLE YLEGIELPGI KAINDK 

« Hide

References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC1435.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006716 Genomic DNA. Translation: BAE05421.1.
RefSeqYP_254027.1. NC_007168.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279808.SH2112.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE05421; BAE05421; SH2112.
GeneID3481993.
KEGGsha:SH2112.
PATRIC19620321. VBIStaHae67511_2081.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAAGHPVGK.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycSHAE279808:GJX7-2170-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.
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.
ProtoNetSearch...

Entry information

Entry namePGK_STAHJ
AccessionPrimary (citable) accession number: Q4L4K4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 2, 2005
Last modified: June 11, 2014
This is version 64 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