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F6A3C0 (F6A3C0_GARVH) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 15. 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
Ordered Locus Names:HMPREF9231_1017 EMBL AEF30862.1
OrganismGardnerella vaginalis (strain HMP9231) [Complete proteome] [HAMAP] EMBL AEF30862.1
Taxonomic identifier1009464 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeGardnerella

Protein attributes

Sequence length246 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 site1801 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 site18212-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
F6A3C0 [UniParc].

Last modified July 27, 2011. Version 1.
Checksum: EA0BB88C4943DED9

FASTA24627,713
        10         20         30         40         50         60 
MTYKLVLLRH GQSAWNKTNQ FTGWVDVPLT EQGVEEAKHG GELLKEKNVL PDIVFTSLLR 

        70         80         90        100        110        120 
RAINTANYAL DAADRLWIPV RRSWRLNERH YGALQGKNKS EIRQEYGDEK FMIWRRSYAT 

       130        140        150        160        170        180 
PPPEIDPNDE YSQTNDPRYA GDPVPETEAL ANVVTRVTPY WESDIIPELK SGKTVMIAAH 

       190        200        210        220        230        240 
GNSLRAIVKM LDNLSEEEIS KVNIPTAIPL LYELDENFKP IKPRGEYLDP EAAAAGAAAV 


AAQGQK 

« Hide

References

[1]"Complete sequence of Gardnerella vaginalis HMP9231."
Durkin A.S., Kim M.K., Hostetler J., Torralba M., Gillis M., Methe B., Sutton G., Nelson K.E.
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HMP9231.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002725 Genomic DNA. Translation: AEF30862.1.
RefSeqYP_005838339.1. NC_017456.1.

3D structure databases

ProteinModelPortalF6A3C0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEF30862; AEF30862; HMPREF9231_1017.
GeneID12445119.
KEGGgvh:HMPREF9231_1017.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01834.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

BioCycGVAG1009464:GLDL-1008-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 nameF6A3C0_GARVH
AccessionPrimary (citable) accession number: F6A3C0
Entry history
Integrated into UniProtKB/TrEMBL: July 27, 2011
Last sequence update: July 27, 2011
Last modified: June 11, 2014
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)