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Q2S3A7 (PGK_SALRD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:SRU_1199
OrganismSalinibacter ruber (strain DSM 13855 / M31) [Reference proteome] [HAMAP]
Taxonomic identifier309807 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeSalinibacter

Protein attributes

Sequence length398 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
Reference 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 – 398398Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000009646

Regions

Nucleotide binding354 – 3574ATP By similarity
Region21 – 233Substrate binding By similarity
Region64 – 674Substrate binding By similarity

Sites

Binding site411Substrate By similarity
Binding site1231Substrate By similarity
Binding site1561Substrate By similarity
Binding site2071ATP By similarity
Binding site2941ATP; via carbonyl oxygen By similarity
Binding site3251ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2S3A7 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 41C94D8C5B13D2B8

FASTA39841,487
        10         20         30         40         50         60 
MHKLTLDDVD VRGQRVLIRV DFNVPLDTSE DGSPCVGDDT RIRAALPTIR HVLDHGGKAI 

        70         80         90        100        110        120 
LVSHLGRPGG QPDPDLSLAC VADHLGTLIE ERVRFSSNTV GDTVEEVING MSEGSVILLE 

       130        140        150        160        170        180 
NTRFDAGEKA NDEAFATALA NLADVYVNDA FGAAHRAHAS TAGVAEFMDV AALGRLMEDE 

       190        200        210        220        230        240 
IEALTRVRDD PAHPMVAILG GSKVSDKLGT IRALSETADH LLIGGAMSYT FLKVLGHEVG 

       250        260        270        280        290        300 
ASRVEADRLD TAEDLYEQAE GTITLPTDHV VAEAPEADAT ASVVEGDIPA ELMGLDIGPA 

       310        320        330        340        350        360 
TIDAYRDRIL GAATVVWNGP MGVFEVDPFA DGTTAIAEAM ADATDDGAFS VVGGGDSVSA 

       370        380        390 
LTRSGCDDRI SHVSTGGGAL LTFLEGAPLP GVEALTDA 

« Hide

References

[1]"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea."
Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F.
Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13855 / M31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000159 Genomic DNA. Translation: ABC45859.1.
RefSeqYP_445324.1. NC_007677.1.

3D structure databases

ProteinModelPortalQ2S3A7.
SMRQ2S3A7. Positions 2-397.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING309807.SRU_1199.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC45859; ABC45859; SRU_1199.
GeneID3851848.
KEGGsru:SRU_1199.
PATRIC23424809. VBISalRub86502_1245.

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAGLDCGEK.
OrthoDBEOG64N9Z0.
PhylomeDBQ2S3A7.
ProtClustDBCLSK2775029.

Enzyme and pathway databases

BioCycSRUB309807:GJJD-1196-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_SALRD
AccessionPrimary (citable) accession number: Q2S3A7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: February 19, 2014
This is version 59 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