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E8WR25 (E8WR25_GEOS8) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 17. 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:GM18_0586 EMBL ADW12067.1
OrganismGeobacter sp. (strain M18) [Complete proteome] [HAMAP] EMBL ADW12067.1
Taxonomic identifier443143 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length234 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 RuleBase RU004512

Catalytic activity

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

Pathway

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

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 EMBL ADW12067.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

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

Region21 – 2222-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region87 – 9042-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region114 – 11522-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site91Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1821 By similarity HAMAP-Rule MF_01039
Binding site1512-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6012-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site9812-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18412-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
E8WR25 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: BC42514B9DA56FC9

FASTA23427,397
        10         20         30         40         50         60 
MRQLVLVRHG ESVWNRENLF TGWTDVDLSE RGEEESRNAG TLLREKGFVF DVAFTSVLRR 

        70         80         90        100        110        120 
AIRTLWLILE EMDLMWIPER KDWRLNERHY GALQGLNKAQ TAEEYGEEQV RLWRRSYHVR 

       130        140        150        160        170        180 
PPALAEEDQR YPGRDPRYSS LARHLIPMTE CLQDTVERVL PCWQQQIVPA LRECRRPLVV 

       190        200        210        220        230 
AHGNSLRGLI KYLDRVSDAD IIDLEIPTGT PLVYDLDDDL KPIRHYYATD TGIG 

« Hide

References

[1]"Complete sequence of Geobacter sp. M18."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Holmes D. expand/collapse author list , Aklujkar M., Lovley D., Woyke T.
Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M18 EMBL ADW12067.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002479 Genomic DNA. Translation: ADW12067.1.
RefSeqYP_004197343.1. NC_014973.1.

3D structure databases

ProteinModelPortalE8WR25.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADW12067; ADW12067; GM18_0586.
GeneID10196156.
KEGGgeb:GM18_0586.
PATRIC46945013. VBIGeoSp68312_0577.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.

Enzyme and pathway databases

BioCycGSP443143:GHZL-596-MONOMER.
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 nameE8WR25_GEOS8
AccessionPrimary (citable) accession number: E8WR25
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: February 19, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)