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Q0A915 (GPMA_ALKEH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 58. 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:Mlg_1323
OrganismAlkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeAlkalilimnicola

Protein attributes

Sequence length232 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 – 2322322,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_1000064026

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
Q0A915 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 648BEFD0EC0AD8C3

FASTA23226,825
        10         20         30         40         50         60 
MKKLVLLRHG QSIWNQENRF TGWHDVDLTE KGREEAQAAG QLMKRHGLRF DYAYTSVLKR 

        70         80         90        100        110        120 
AIRTLWIGLD ELDQMWIPVT KAWQLNERHY GALTGLNKAE TAEEYGAEQV HIWRRSYDTP 

       130        140        150        160        170        180 
PPPLDETSPY HPRHDPRYAS LKPEQLPATE SLALTLERVL PYWNERIVPT LRDCDNVLIA 

       190        200        210        220        230 
AHGNSIRALI KHLDGLDDEA IMKVEIATGD PLVYELDDAL AVVDKHYLRE RD 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000453 Genomic DNA. Translation: ABI56672.1.
RefSeqYP_742162.1. NC_008340.1.

3D structure databases

ProteinModelPortalQ0A915.
SMRQ0A915. Positions 1-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING187272.Mlg_1323.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI56672; ABI56672; Mlg_1323.
GeneID4268662.
KEGGaeh:Mlg_1323.
PATRIC20861887. VBIAlkEhr114327_1322.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

BioCycAEHR187272:GHAX-1358-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_ALKEH
AccessionPrimary (citable) accession number: Q0A915
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 17, 2006
Last modified: June 11, 2014
This is version 58 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