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Q87LL1 (PGK_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoglycerate kinase
EC=2.7.2.3
Gene names
Name:pgk
Ordered Locus Names:VP2600
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio ›

Protein attributes

Sequence length386 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.

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: 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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 386386Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_0000146036

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
Q87LL1 [UniParc].

Last modified May 23, 2003. Version 1.
Checksum: BD8F351F88DF8B4D

FASTA38640,733
        10         20         30         40         50         60 
MSVIKMTDLD LAGKRVFIRA DLNVPVKDGK VTSDARIIAS LPTIKHCLEA GAKVMVTSHL 

        70         80         90        100        110        120 
GRPTEGEYAE EFSLQPVVNY LNDALDCEVK LAKDYLDGLE LNAGELVVLE NVRFNKGEKK 

       130        140        150        160        170        180 
NEEELSKKYA ALCDVFVMDA FGTAHRAQAS THGVGMHAPV ACAGPLLANE LEALGKAMDK 

       190        200        210        220        230        240 
PARPMVAIVG GSKVSTKLTV LESLSKIADQ LVVGGGIANT FIAAAGHNVG KSLYEADLVD 

       250        260        270        280        290        300 
TAKKLMDECA IPVATDVACA KAFDENAEAE IKHVSEVQDD DMIFDLGPES TAALAEILKN 

       310        320        330        340        350        360 
AKTILWNGPV GVFEFKNFEA GTKGISEAIA ASEGFSVAGG GDTLAAIDKF GIKADVSYIS 

       370        380 
TGGGAFLEFV EGKVLPAVEM LEARAK

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000031 Genomic DNA. Translation: BAC60863.1.
RefSeqNP_798979.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87LL1.
SMRQ87LL1. Positions 2-386.
ModBaseSearch...

Protein-protein interaction databases

STRING223926.VP2600.

Proteomic databases

PRIDEQ87LL1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC60863; BAC60863; BAC60863.
GeneID1190124.
KEGGvpa:VP2600.
PATRIC20143356. VBIVibPar50997_2496.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAEKKNDEA.
ProtClustDBPRK00073.

Enzyme and pathway databases

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. PGK. 1 hit.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGK_VIBPA
AccessionPrimary (citable) accession number: Q87LL1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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