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G7S3T3 (G7S3T3_STRSU) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039

Short name=BPG-dependent PGAM HAMAP-Rule MF_01039
Short name=PGAM HAMAP-Rule MF_01039
Short name=Phosphoglyceromutase HAMAP-Rule MF_01039
Short name=dPGM HAMAP-Rule MF_01039
EC=5.4.2.11 HAMAP-Rule MF_01039
Gene names
Name:gpmA HAMAP-Rule MF_01039 EMBL AER15766.1
ORF Names:SSU12_1587 EMBL AER15766.1
OrganismStreptococcus suis SS12 [Complete proteome] EMBL AER15766.1
Taxonomic identifier1005041 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. HAMAP-Rule MF_01039 SAAS SAAS013078

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01039 SAAS SAAS013078

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01039 SAAS SAAS013078

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily. HAMAP-Rule MF_01039

Ontologies

Keywords
   Biological processGlycolysis HAMAP-Rule MF_01039 SAAS SAAS013078
   Molecular functionIsomerase HAMAP-Rule MF_01039 SAAS SAAS013078
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region21 – 2222-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region87 – 9042-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region114 – 11522-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site91Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1821 By similarity HAMAP-Rule MF_01039
Binding site1512-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6012-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site9812-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18412-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
G7S3T3 [UniParc].

Last modified January 25, 2012. Version 1.
Checksum: CC115C67E58C0EE2

FASTA23026,042
        10         20         30         40         50         60 
MVKLVFARHG ESEWNKANLF TGWADVDLSE KGTQQAIDAG KLIKEAGIEF DLAFTSVLKR 

        70         80         90        100        110        120 
AIKTTNLALE AADQLWVPVE KSWRLNERHY GGLTGLNKAE AAAEFGDEQV HIWRRSYDTL 

       130        140        150        160        170        180 
PPEMAKDHEH SAHTDRRYAH LDDSVIPDAE NLKVTLERAL PFWEDKIAPA LKDGKNVFVG 

       190        200        210        220        230 
AHGNSIRALV KHIKQLSDDE IMDVEIPNFP PLVFELDENL NIVKEYYLEA 

« Hide

References

[1]"Comparative genomic analysis of Streptococcus suis reveals significant genomic diversity among different serotypes."
Zhang A., Yang M., Hu P., Wu J., Chen B., Hua Y., Yu J., Chen H., Xiao J., Jin M.
BMC Genomics 12:523-523(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SS12 EMBL AER15766.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002640 Genomic DNA. Translation: AER15766.1.
RefSeqYP_006079014.1. NC_017619.1.

3D structure databases

ProteinModelPortalG7S3T3.
SMRG7S3T3. Positions 2-228.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEG7S3T3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAER15766; AER15766; SSU12_1587.
GeneID12720653.
KEGGsuo:SSU12_1587.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01834.

Enzyme and pathway databases

BioCycSSUI1005041:GLLO-1636-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. PTHR11931. 1 hit.
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMSSF53254. SSF53254. 1 hit.
TIGRFAMsTIGR01258. pgm_1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameG7S3T3_STRSU
AccessionPrimary (citable) accession number: G7S3T3
Entry history
Integrated into UniProtKB/TrEMBL: January 25, 2012
Last sequence update: January 25, 2012
Last modified: July 9, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)