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A5CXU9 (PGK_VESOH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 49. 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:COSY_0072
OrganismVesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA) [Complete proteome] [HAMAP]
Taxonomic identifier412965 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbionts

Protein attributes

Sequence length392 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 – 392392Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000058089

Regions

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

Sites

Binding site361Substrate By similarity
Binding site1131Substrate By similarity
Binding site1461Substrate By similarity
Binding site1971ATP By similarity
Binding site3141ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5CXU9 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 884A9F8876B2C3CB

FASTA39241,878
        10         20         30         40         50         60 
MSVINLSDLD LNSKRVLIRQ DLNVPISNGV VTSDKRIKAS LPTIKMALNQ GAKVMLMSHR 

        70         80         90        100        110        120 
GRPIEGDPSD GFSLQPVADR LSELLNTTVR LEKDWLDGVE MNNGKVVLCE NVRFNVGEMV 

       130        140        150        160        170        180 
NDDELSKRMA AICDIFVMDA FGTAHRAQAS TYGVAKYAPI ACSGPLLSEE LDALGKALDN 

       190        200        210        220        230        240 
PKRPMVAIVG GSKVSTKLTV LESLSKIVDQ LVVGGGIANT FIAAQGFNVG KSLCEYDLIP 

       250        260        270        280        290        300 
IAKKLMEDCE IPVSKDVVCG KEFSDVAEAE TKASKDVADD DMIFDIGPKS AQQLADIMRN 

       310        320        330        340        350        360 
AGTIVWNGPV GVFEFDQFAG GTETLGKAIA ESNAFSIAGG GDTLAAVDKY GIEDKISYIS 

       370        380        390 
TGGGAFLEFL EGKKLPAVEV LEQRALEVIK LA 

« Hide

References

[1]"Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea clam, Calyptogena okutanii."
Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M., Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T., Kato C., Kitagawa M., Kato I., Maruyama T.
Curr. Biol. 17:881-886(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HA.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009247 Genomic DNA. Translation: BAF61208.1.
RefSeqYP_001218932.1. NC_009465.1.

3D structure databases

ProteinModelPortalA5CXU9.
SMRA5CXU9. Positions 2-385.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING412965.COSY_0072.

Proteomic databases

PRIDEA5CXU9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF61208; BAF61208; COSY_0072.
GeneID5172231.
KEGGvok:COSY_0072.
PATRIC32019953. VBICanVes128383_0070.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAAGHPVGK.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycCVES412965:GHZZ-73-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_VESOH
AccessionPrimary (citable) accession number: A5CXU9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 12, 2007
Last modified: June 11, 2014
This is version 49 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