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P59461 (PGK_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 68. 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:bbp_400
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length393 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 – 393393Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_0000145920

Regions

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

Sites

Binding site361Substrate By similarity
Binding site1141Substrate By similarity
Binding site1471Substrate By similarity
Binding site1981ATP By similarity
Binding site3141ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P59461 [UniParc].

Last modified March 28, 2003. Version 1.
Checksum: 9DCBD57CCDE00530

FASTA39343,647
        10         20         30         40         50         60 
MSIIKITDLN LLNKKVLIRS DLNVPIKNNK ISSYARIHAS LPTIKFALKN LAKVIVTSHL 

        70         80         90        100        110        120 
GRPTEGIYKK KFSLFPVFKY FKKILPETNI YFSQNLTECS SIKSGELIIL ENVRFNQGEK 

       130        140        150        160        170        180 
ENSKILSKKY ATLCDIFVMD AFGAIHRNEA STNGIIKYAK LACSGLLLES ELKTLNSALT 

       190        200        210        220        230        240 
NPVRPMVAIV GGAKVSTKFK TLTTLAKISD TLIVGGGIAN TFISIDHNIG KSLHDPKFIE 

       250        260        270        280        290        300 
QAKILKEKYN IFIPTDSRVS TTFTYDSIAT IKSTSDIHAN EEIMDFGDIS IKNMINIIKK 

       310        320        330        340        350        360 
AKTILWNGPI GVFEFKNFSK GTEQLSKAIA SSDAFSIAGG GDTLSVVEMF KVQNNISYLS 

       370        380        390 
TGGGSFLKFL EGNKFRIIEL LEKHFNKFKN NNF 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO27112.1.
RefSeqNP_778007.1. NC_004545.1.

3D structure databases

ProteinModelPortalP59461.
SMRP59461. Positions 2-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp400.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO27112; AAO27112; bbp_400.
GeneID1058371.
KEGGbab:bbp400.
PATRIC21245603. VBIBucAph80364_0395.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
KOK00927.
OMAAGHPVGK.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-400-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_BUCBP
AccessionPrimary (citable) accession number: P59461
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 28, 2003
Last modified: June 11, 2014
This is version 68 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