Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q1MMY4 (GPMA_RHIL3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 51. 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=5.4.2.1
Gene names
Name:gpmA
Ordered Locus Names:RL0179
OrganismRhizobium leguminosarum bv. viciae (strain 3841) [Complete proteome] [HAMAP]
Taxonomic identifier216596 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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: HAMAP

   Molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2112112,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_1000064090

Sites

Active site101Tele-phosphohistidine intermediate By similarity
Active site1581 By similarity
Site611Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1MMY4 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: D47203157D3728A7

FASTA21123,235
        10         20         30         40         50         60 
MSGTLVLVRH GQSDWNLKNL FTGWKDPDLT ELGIQEANTG GAALAEYGIK FDVAYTSVLV 

        70         80         90        100        110        120 
RAQHTLKLIL DKVGQPDLLT IRDQALNERD YGDLSGLNKD DARAKWGEEQ VHIWRRSYDV 

       130        140        150        160        170        180 
PPPGGESLRD TGARVWPYYL TEILPRVLRG EKVLVAAHGN SLRSLVMVLD KLSREGVLAL 

       190        200        210 
NLATGVPMVY KLKADSTVAS KEVLGDMSGA H 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM236080 Genomic DNA. Translation: CAK05668.1.
RefSeqYP_765784.1. NC_008380.1.

3D structure databases

ProteinModelPortalQ1MMY4.
SMRQ1MMY4. Positions 5-204.
ModBaseSearch...

Protein-protein interaction databases

STRING216596.RL0179.

Proteomic databases

ProMEXQ1MMY4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK05668; CAK05668; RL0179.
GeneID4402944.
KEGGrle:RL0179.
PATRIC23136723. VBIRhiLeg32091_1315.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
OMAGQSDWNL.
ProtClustDBPRK01295.

Enzyme and pathway databases

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_RHIL3
AccessionPrimary (citable) accession number: Q1MMY4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 30, 2006
Last modified: May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families