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Q0BVE2 (PGK_GRABC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 56. 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:GbCGDNIH1_0312
OrganismGranulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1) [Complete proteome] [HAMAP]
Taxonomic identifier391165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGranulibacter

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_1000057998

Regions

Nucleotide binding353 – 3564ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1181Substrate By similarity
Binding site1511Substrate By similarity
Binding site2011ATP By similarity
Binding site3231ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0BVE2 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 38560639196FAF65

FASTA39641,837
        10         20         30         40         50         60 
MSFRTLDGLD VRGRRVLVRL DLNVPMRDGR VSDLTRIERQ APTVRELAEG GARVIVMSHF 

        70         80         90        100        110        120 
DRPKGKRVQE MSLRPIAEAL GAALGQPVAF VDDCIGGTVE EAVAGMKDGD VLVLENTRFH 

       130        140        150        160        170        180 
AAEEKNDPEF SRLLASLAEV YVNDAFSAAH RAHASTHGVT AHLPAYAGRL MQREVEALEL 

       190        200        210        220        230        240 
ALGSPTRPVA AIVGGAKVST KLDLLGNLST KVDVLVIGGA MANTFLAAQG IKVGKSLQEA 

       250        260        270        280        290        300 
EMHDTARAIL ETAKKAGCEI LLPVDAVTAT EFRADPPTRT VSINEIPDDA MMLDVGPETV 

       310        320        330        340        350        360 
RLLTERLSGV KTLVWNGPLG AFEISPFDKA TVALAQSVAG LTETAGLVSV AGGGDTVAAL 

       370        380        390 
KHAGVVERLT YVSAAGGAFL EWMEGKELPG VAVLRA 

« Hide

References

[1]"Genome sequence analysis of the emerging human pathogenic acetic acid bacterium Granulibacter bethesdensis."
Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.
J. Bacteriol. 189:8727-8736(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1260 / CGDNIH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000394 Genomic DNA. Translation: ABI61210.1.
RefSeqYP_744133.1. NC_008343.1.

3D structure databases

ProteinModelPortalQ0BVE2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391165.GbCGDNIH1_0312.

Proteomic databases

PRIDEQ0BVE2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI61210; ABI61210; GbCGDNIH1_0312.
GeneID4276352.
KEGGgbe:GbCGDNIH1_0312.
PATRIC22076667. VBIGraBet83793_0329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAHASVYDI.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycGBET391165:GHON-319-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_GRABC
AccessionPrimary (citable) accession number: Q0BVE2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 17, 2006
Last modified: June 11, 2014
This is version 56 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