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A8YYG4 (GPMA_STAAT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Short name=BPG-dependent PGAM
Short name=PGAM
Short name=Phosphoglyceromutase
Short name=dPGM
EC=5.4.2.11
Gene names
Name:gpmA
Ordered Locus Names:USA300HOU_2398
OrganismStaphylococcus aureus (strain USA300 / TCH1516) [Complete proteome] [HAMAP]
Taxonomic identifier451516 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length228 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

Catalytic activity

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

Pathway

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

Sequence similarities

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

Ontologies

Keywords
   Biological processGlycolysis
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

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

Molecule processing

Chain1 – 2282282,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_1000084333

Regions

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

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A8YYG4 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 1751F3AFB1EE068E

FASTA22826,680
        10         20         30         40         50         60 
MPKLILCRHG QSEWNAKNLF TGWEDVNLSE QGINEATRAG EKVRENNIAI DVAFTSLLTR 

        70         80         90        100        110        120 
ALDTTHYILT ESKQQWIPVY KSWRLNERHY GGLQGLNKDD ARKEFGEEQV HIWRRSYDVK 

       130        140        150        160        170        180 
PPAETEEQRE AYLADRRYNH LDKRMMPYSE SLKDTLVRVI PFWTDHISQY LLDGQTVLVS 

       190        200        210        220 
AHGNSIRALI KYLEDVSDED IINYEIKTGA PLVYELTDDL EVIDKYYL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000730 Genomic DNA. Translation: ABX30388.1.
RefSeqYP_001576267.1. NC_010079.1.

3D structure databases

ProteinModelPortalA8YYG4.
SMRA8YYG4. Positions 1-228.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING451516.USA300HOU_2398.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX30388; ABX30388; USA300HOU_2398.
GeneID5777487.
KEGGsax:USA300HOU_2398.
PATRIC19600082. VBIStaAur36919_2509.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.
OrthoDBEOG6C8N1H.
ProtClustDBPRK14119.

Enzyme and pathway databases

BioCycSAUR451516:GJQ4-2487-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. PTHR11931. 1 hit.
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGPMA_STAAT
AccessionPrimary (citable) accession number: A8YYG4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 42 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