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Q6FYN4 (PGK_BARQU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:BQ11990
OrganismBartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier283165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length397 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_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 – 397397Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000057970

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
Q6FYN4 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 1915DDEE408EC57D

FASTA39742,820
        10         20         30         40         50         60 
MGFRTLDDVD VTGKRVLVRV DFNVPMSQGK VCDETRLKRH KETLLELQKR GAKLILLSHC 

        70         80         90        100        110        120 
GRPKGQGEPE FSLRPVVRVL EKIINQPVAF APDCVGVAAQ TAIEALQNGG LLLLENVRFH 

       130        140        150        160        170        180 
PGEEKNDCSF AEALAHNGDL YVNDAFSVSH RAHASVEGIT HLLPSYAGRS LQCELQALEK 

       190        200        210        220        230        240 
GLDNPKRPVV ALVGGAKVSS KLFVLNHLVE KVDYLVIGGG MANSFLAAQG VHIGKSLCEH 

       250        260        270        280        290        300 
ALMQTIKKVI EKAQEYQCTL LLPVDAVVGF RFEKGAPHRL YDIGDIPDDG MILDIGTRSI 

       310        320        330        340        350        360 
AHINEVIDKA ATLVWNGPLG VFEMSPFDQG TIAVARHAAE CSLTGKCVSI AGGGDTVFAL 

       370        380        390 
NHAGVANDFT YLSTAGGAFL EWMEGKVLPG IFALRQA 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897700 Genomic DNA. Translation: CAF26658.1.
RefSeqYP_032730.1. NC_005955.1.

3D structure databases

ProteinModelPortalQ6FYN4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283165.BQ11990.

Proteomic databases

PRIDEQ6FYN4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF26658; CAF26658; BQ11990.
GeneID2867045.
KEGGbqu:BQ11990.
PATRIC31953825. VBIBarQui58630_1310.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAFGLADKM.
OrthoDBEOG64N9Z0.
ProtClustDBPRK00073.

Enzyme and pathway databases

BioCycBQUI283165:GHZA-1197-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_BARQU
AccessionPrimary (citable) accession number: Q6FYN4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 19, 2004
Last modified: February 19, 2014
This is version 60 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