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B4STV2 (PGK_STRM5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 33. 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:Smal_3216
OrganismStenotrophomonas maltophilia (strain R551-3) [Complete proteome] [HAMAP]
Taxonomic identifier391008 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group

Protein attributes

Sequence length391 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 – 391391Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000096380

Regions

Nucleotide binding345 – 3484ATP 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 site3191ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B4STV2 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: A4AA3E2B8CD4AFE5

FASTA39140,763
        10         20         30         40         50         60 
MSIVRMTDLD LSGKRVLIRQ DLNVPIENGR ITSEQRITAS LPTLKRALEQ GAAVMVTSHL 

        70         80         90        100        110        120 
GRPKEGVWSE ADSLAPVAQR LSELLGREVP LVRDWVDGVD VQPGQLVLLE NCRMNVGEGK 

       130        140        150        160        170        180 
DDEALSKKYA ALCDVFVMDA FGTAHRAQAS THGVIRFAPV AAGGPLLMAE LDALAQALDA 

       190        200        210        220        230        240 
PAKPLLAIVA GSKVSTKLEL LASLVGKVDQ LIVGGGIANT FIAAAGYNVG KSLYEPDLLD 

       250        260        270        280        290        300 
TAKKIVADAK ARGADIPLPV DVVTAKQFLP DAVAEVKAVD AVAEDDLILD IGPQTAAQYA 

       310        320        330        340        350        360 
QLIENAGTVV WNGPVGVFEF EAFSKGTEAL ARAIASSNAF SIAGGGDTLA AVDKFDIAAQ 

       370        380        390 
VSYISTGGGA FLEFLEGKTL PAVAALDARG A 

« Hide

References

[1]"Complete sequence of Stenotrophomonas maltophilia R551-3."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Taghavi S., Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R551-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001111 Genomic DNA. Translation: ACF52915.1.
RefSeqYP_002029598.1. NC_011071.1.

3D structure databases

ProteinModelPortalB4STV2.
SMRB4STV2. Positions 2-390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391008.Smal_3216.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF52915; ACF52915; Smal_3216.
GeneID6476270.
KEGGsmt:Smal_3216.
PATRIC23711416. VBISteMal40512_3240.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMADMIFDIG.
OrthoDBEOG64N9Z0.
ProtClustDBPRK00073.

Enzyme and pathway databases

BioCycSMAL391008:GH1H-3289-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_STRM5
AccessionPrimary (citable) accession number: B4STV2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 33 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