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Q4L8T0 (GPMA_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 63. 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:SH0636
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [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_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

Molecule processing

Chain1 – 2282282,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_0000179918

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
Q4L8T0 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 0C65EFA7A78A02F4

FASTA22826,735
        10         20         30         40         50         60 
MPKLILCRHG QSEWNAKNLF TGWEDVQLSE QGRNEAITSG RKLKENGIEI DVAFTSLLTR 

        70         80         90        100        110        120 
ALETTQFLLA ESDQEWIPVH KSWRLNERHY GKLQGLNKDE ARKEFGEEQV HQWRRSYDVK 

       130        140        150        160        170        180 
PPAQTEEQRE SYLKDRRYRH LDHRMMPYSE SLKTTLERVV PIWTDKISQH LLDGETVLVA 

       190        200        210        220 
AHGNSIRALI KYLDNVSDED IIGYEIKTGA PLIYELDDNL NVIDHYYL 

« Hide

References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC1435.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006716 Genomic DNA. Translation: BAE03945.1.
RefSeqYP_252551.1. NC_007168.1.

3D structure databases

ProteinModelPortalQ4L8T0.
SMRQ4L8T0. Positions 3-228.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279808.SH0636.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE03945; BAE03945; SH0636.
GeneID3482202.
KEGGsha:SH0636.
PATRIC19617295. VBIStaHae67511_0624.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMAKDDERFP.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

BioCycSHAE279808:GJX7-638-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.
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]
SUPFAMSSF53254. SSF53254. 1 hit.
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGPMA_STAHJ
AccessionPrimary (citable) accession number: Q4L8T0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: August 2, 2005
Last modified: June 11, 2014
This is version 63 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