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Q662V8 (PGK_BORGA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. 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:BG0055
OrganismBorrelia garinii (strain PBi) [Complete proteome] [HAMAP]
Taxonomic identifier290434 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

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_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 – 393393Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000192806

Regions

Nucleotide binding350 – 3534ATP By similarity
Region22 – 243Substrate binding By similarity
Region60 – 634Substrate binding By similarity

Sites

Binding site371Substrate By similarity
Binding site1191Substrate By similarity
Binding site1521Substrate By similarity
Binding site2021ATP By similarity
Binding site2931ATP; via carbonyl oxygen By similarity
Binding site3241ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q662V8 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 21C202189491FE70

FASTA39342,631
        10         20         30         40         50         60 
MSIKTVKDFN SFAGKRALVR CDFNVPLKEG NISDDTRIKA ALPTIEYLKE KGARIVLISH 

        70         80         90        100        110        120 
LGRPEGKKNL KYSLKPVANK LSELLGQDVK MLSDCIGREI VNNTLQMKDG DVVLLENVRF 

       130        140        150        160        170        180 
YAEEEKNDKN FAKKLSENGD VFVNDAFGAA HRAHASTVGV SDYLPSVGGF LMEKEDKFLG 

       190        200        210        220        230        240 
EVLKNPERPF VSIIGGSKVS SKIAVLESLL SKSNVVVIGG GMAYTFLHSK GYSIGKSLLE 

       250        260        270        280        290        300 
SEYIDIASSF LKKAKELDVK VILPLDHIVA DDFNKNSTPE YIDSFDIPEN KIGMDVGGKT 

       310        320        330        340        350        360 
LKEIEKVIKT AKTIIWNGPL GVFEFDSFSK GTAMVAEMVA SCAGLTIVGG GDSVAAVNKF 

       370        380        390 
NLSDKITHVS TGGGASLEYL EGKILPGIKV LEK 

« Hide

References

[1]"Comparative analysis of the Borrelia garinii genome."
Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U., Schilhabel M., Wilske B., Suehnel J., Platzer M.
Nucleic Acids Res. 32:6038-6046(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PBi.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000013 Genomic DNA. Translation: AAU06913.1.
RefSeqYP_072505.1. NC_006156.1.

3D structure databases

ProteinModelPortalQ662V8.
SMRQ662V8. Positions 1-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290434.BG0055.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU06913; AAU06913; BG0055.
GeneID2957894.
KEGGbga:BG0055.
PATRIC20565671. VBIBorGar102262_0165.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000227108.
KOK00927.
OMADMIFDIG.
OrthoDBEOG64N9Z0.
ProtClustDBPRK00073.

Enzyme and pathway databases

BioCycBGAR290434:BG0055-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_BORGA
AccessionPrimary (citable) accession number: Q662V8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 67 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