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G8VGF4 (G8VGF4_PROAA) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039

Short name=BPG-dependent PGAM HAMAP-Rule MF_01039
Short name=PGAM HAMAP-Rule MF_01039
Short name=Phosphoglyceromutase HAMAP-Rule MF_01039
Short name=dPGM HAMAP-Rule MF_01039
EC=5.4.2.11 HAMAP-Rule MF_01039
Gene names
Name:gpmA HAMAP-Rule MF_01039
ORF Names:TIA2EST22_01830 EMBL AEW80698.1
OrganismPropionibacterium acnes TypeIA2 P.acn17 [Complete proteome] EMBL AEW80698.1
Taxonomic identifier1114967 [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. RuleBase RU004512 HAMAP-Rule MF_01039

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. RuleBase RU004512 HAMAP-Rule MF_01039 SAAS SAAS001345

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. RuleBase RU004512 HAMAP-Rule MF_01039

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily. HAMAP-Rule MF_01039

Ontologies

Keywords
   Biological processGlycolysis HAMAP-Rule MF_01039 SAAS SAAS001345
   Molecular functionIsomerase HAMAP-Rule MF_01039 SAAS SAAS001345
   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

Regions

Region22 – 2322-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region88 – 9142-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region115 – 11622-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site101Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1831 By similarity HAMAP-Rule MF_01039
Binding site1612-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6112-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site9912-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18512-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
G8VGF4 [UniParc].

Last modified February 22, 2012. 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]"Complete Genome Sequences of Three Propionibacterium acnes Isolates from the Type IA2 Cluster."
Voros A., Horvath B., Hunyadkurti J., McDowell A., Barnard E., Patrick S., Nagy I.
J. Bacteriol. 194:1621-1622(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: P.acn17 EMBL AEW80698.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003196 Genomic DNA. Translation: AEW80698.1.
RefSeqYP_004945888.1. NC_016512.1.

3D structure databases

ProteinModelPortalG8VGF4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEW80698; AEW80698; TIA2EST22_01830.
GeneID11482743.
KEGGpav:TIA2EST22_01830.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01834.

Enzyme and pathway databases

BioCycPACN1114967:GJTL-352-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 nameG8VGF4_PROAA
AccessionPrimary (citable) accession number: G8VGF4
Entry history
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: June 11, 2014
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)