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B9MEZ2 (GPMA_ACIET) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 40. 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:Dtpsy_2828
OrganismAcidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)) [Complete proteome] [HAMAP]
Taxonomic identifier535289 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length247 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 – 2472472,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_1000149510

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
B9MEZ2 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 32A61BED9F3EC44D

FASTA24727,648
        10         20         30         40         50         60 
MHKLVLIRHG ESTWNLENRF TGWTDVDLTP TGIEQAKNAG RLLKAEGYEF DLAYTSVLKR 

        70         80         90        100        110        120 
ATRTLWHCLD EMDRTWLPVE HSWRLNERHY GALQGLNKAD MAKQYGDAQV LVWRRSYDTP 

       130        140        150        160        170        180 
PPALETTDPR SERGDLRYAG LQAGEVPLTE CLKDTVARVL PYWNESIAPA IRSGKRVLIA 

       190        200        210        220        230        240 
AHGNSIRALV KYLDNISDQD IVGLNIPNGI PLVYELDADL KPLRHYYLGD AEAAAKAAAA 


VASQGKA 

« Hide

References

[1]"Complete sequence of Diaphorobacter sp. TPSY."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TPSY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001392 Genomic DNA. Translation: ACM34262.1.
RefSeqYP_002554262.1. NC_011992.1.

3D structure databases

ProteinModelPortalB9MEZ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING535289.Dtpsy_2828.

Proteomic databases

PRIDEB9MEZ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM34262; ACM34262; Dtpsy_2828.
GeneID7384939.
KEGGdia:Dtpsy_2828.
PATRIC21782797. VBIDiaSp55748_2870.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMAHLWRRSY.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

BioCycAEBR535289:GHOO-2873-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_ACIET
AccessionPrimary (citable) accession number: B9MEZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: June 11, 2014
This is version 40 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