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Q6AAU8 (GPMA_PROAC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 66. 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:PPA0364
OrganismPropionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]
Taxonomic identifier267747 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Protein attributes

Sequence length249 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 – 2492492,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_0000229136

Regions

Region22 – 2322-phospho-D-glycerate binding By similarity
Region88 – 9142-phospho-D-glycerate binding By similarity
Region115 – 11622-phospho-D-glycerate binding By similarity

Sites

Active site101Tele-phosphohistidine intermediate By similarity
Active site1831 By similarity
Binding site1612-phospho-D-glycerate By similarity
Binding site6112-phospho-D-glycerate By similarity
Binding site9912-phospho-D-glycerate By similarity
Binding site18512-phospho-D-glycerate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6AAU8 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: E36BB2762B1D283D

FASTA24927,990
        10         20         30         40         50         60 
MTAKLILLRH GESEWNSKNL FTGWVDVDLN EKGEGEARHA ADLLKQENLL PDIVHTSLLR 

        70         80         90        100        110        120 
RAIHTAYLAL DGCDRHWIPV HRSWRLNERH YGALQGLNKA ETKEKYGNDQ FMAWRRSYDV 

       130        140        150        160        170        180 
RPPDLDRDSE FSQFHDPRYA DIPASERPVA ECLKDVVARM VPYFTSDIAA DLKDGKTVLV 

       190        200        210        220        230        240 
AAHGNSLRAL VKHLDEISDE DIAGLNIPTG IPLFYELDDN LKPVTRGGRY LDPEAAAAGA 


KAVANQGNK 

« Hide

References

[1]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017283 Genomic DNA. Translation: AAT82118.1.
RefSeqYP_055076.1. NC_006085.1.

3D structure databases

ProteinModelPortalQ6AAU8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267747.PPA0364.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT82118; AAT82118; PPA0364.
GeneID2931500.
KEGGpac:PPA0364.
PATRIC23035377. VBIProAcn64440_0373.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMAKDDERFP.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

BioCycPACN267747:GHO9-362-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_PROAC
AccessionPrimary (citable) accession number: Q6AAU8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: September 13, 2004
Last modified: June 11, 2014
This is version 66 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