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P59160 (GPMA_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:gpm
Ordered Locus Names:BRA1052, BS1330_II1044
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length206 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_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

Molecule processing

Chain1 – 2062062,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_0000179857

Regions

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

Sites

Active site101Tele-phosphohistidine intermediate By similarity
Active site1581 By similarity
Binding site1612-phospho-D-glycerate By similarity
Binding site6112-phospho-D-glycerate By similarity
Binding site9912-phospho-D-glycerate By similarity
Binding site16012-phospho-D-glycerate By similarity

Sequences

Sequence LengthMass (Da)Tools
P59160 [UniParc].

Last modified December 13, 2002. Version 1.
Checksum: 4287DDAA47754E9B

FASTA20622,886
        10         20         30         40         50         60 
MSRTLVLVRH GQSEWNLKNL FTGWRDPGLT EQGHAEAKAA GQRLKAAGLK FDIAYTSALS 

        70         80         90        100        110        120 
RAQVTCQHIL DELGQPGLET IRDQALNERD YGDLSGLNKD DARAKWGEEQ VHIWRRSYDV 

       130        140        150        160        170        180 
PPPGGESLKD TGARVWPYYL HTIQPHVLRE ETVLVAAHGN SLRALIMALD GLTPEQILKQ 

       190        200 
ELNTGVPIIY RLNADSTVAS KEILSA 

« Hide

References

[1]"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts."
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. expand/collapse author list , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.
[2]"Revised genome sequence of Brucella suis 1330."
Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.
J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014292 Genomic DNA. Translation: AAN34219.1.
CP002998 Genomic DNA. Translation: AEM20496.1.
RefSeqNP_700214.1. NC_004311.2.
YP_005614722.1. NC_017250.1.

3D structure databases

ProteinModelPortalP59160.
SMRP59160. Positions 5-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204722.BRA1052.

Proteomic databases

PRIDEP59160.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN34219; AAN34219; BRA1052.
AEM20496; AEM20496; BS1330_II1044.
GeneID1165497.
12139277.
KEGGbms:BRA1052.
bsi:BS1330_II1044.
PATRIC17794939. VBIBruSui107850_3277.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.
OrthoDBEOG6C8N1H.
ProtClustDBPRK01295.

Enzyme and pathway databases

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 nameGPMA_BRUSU
AccessionPrimary (citable) accession number: P59160
Secondary accession number(s): G0KE58
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2002
Last sequence update: December 13, 2002
Last modified: February 19, 2014
This is version 76 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

Brucella suis

Brucella suis (strain 1330): entries and gene names