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B2VBS6 (GPMA_ERWT9) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 46. 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:ETA_22810
OrganismErwinia tasmaniensis (strain DSM 17950 / Et1/99) [Complete proteome] [HAMAP]
Taxonomic identifier338565 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeErwinia

Protein attributes

Sequence length250 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

Subunit structure

Homodimer By similarity. 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 – 2502502,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_1000135952

Regions

Region23 – 2422-phospho-D-glycerate binding By similarity
Region89 – 9242-phospho-D-glycerate binding By similarity
Region116 – 11722-phospho-D-glycerate binding By similarity

Sites

Active site111Tele-phosphohistidine intermediate By similarity
Active site1841 By similarity
Binding site1712-phospho-D-glycerate By similarity
Binding site6212-phospho-D-glycerate By similarity
Binding site10012-phospho-D-glycerate By similarity
Binding site18612-phospho-D-glycerate By similarity

Sequences

Sequence LengthMass (Da)Tools
B2VBS6 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 425C14EACBD44823

FASTA25028,463
        10         20         30         40         50         60 
MAVTKLVLVR HGESQWNNEN RFTGWYDVDL SDKGRTEAKA AGQLLKKEGF TFDFAYTSVL 

        70         80         90        100        110        120 
KRAIHTLWNI LDEVDQVWLP VEKSWRLNER HYGALQGLDK AETANKYGDE QVKQWRRGFA 

       130        140        150        160        170        180 
VTPPELDRAD ERFPGHDPRY ASLTAEQLPT TESLALTIDR VLPYWNESIL PRMKSGEKVI 

       190        200        210        220        230        240 
IAAHGNSLRA LVKYLDNMSE EEILELNIPT GVPLVYEFDE NFKPIKHYYL GDADEIAAKA 

       250 
AAVANQGKAK 

« Hide

References

[1]"The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic bacterium in the genus Erwinia."
Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R., Geider K.
Environ. Microbiol. 10:2211-2222(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17950 / Et1/99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU468135 Genomic DNA. Translation: CAO97327.1.
RefSeqYP_001908205.1. NC_010694.1.

3D structure databases

ProteinModelPortalB2VBS6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING465817.ETA_22810.

Proteomic databases

PRIDEB2VBS6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAO97327; CAO97327; ETA_22810.
GeneID6298972.
KEGGeta:ETA_22810.
PATRIC20430401. VBIErwTas9546_2364.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMAKDDERFP.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

BioCycETAS465817:GI36-2349-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_ERWT9
AccessionPrimary (citable) accession number: B2VBS6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: June 11, 2014
This is version 46 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