Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q63XU7 (GPMA_BURPS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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
Ordered Locus Names:BPSL0443
OrganismBurkholderia pseudomallei (strain K96243) [Reference proteome] [HAMAP]
Taxonomic identifier272560 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete proteome
Reference 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 – 2492492,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_0000229112

Regions

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

Sites

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

Secondary structure

....................................... 249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q63XU7 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: E51933D372E4896E

FASTA24927,893
        10         20         30         40         50         60 
MYKLVLIRHG ESTWNKENRF TGWVDVDLTE QGNREARQAG QLLKEAGYTF DIAYTSVLKR 

        70         80         90        100        110        120 
AIRTLWHVQD QMDLMYVPVV HSWRLNERHY GALSGLNKAE TAAKYGDEQV LVWRRSYDTP 

       130        140        150        160        170        180 
PPALEPGDER APYADPRYAK VPREQLPLTE CLKDTVARVL PLWNESIAPA VKAGKQVLIA 

       190        200        210        220        230        240 
AHGNSLRALI KYLDGISDAD IVGLNIPNGV PLVYELDESL TPIRHYYLGD QEAIAKAQAA 


VAQQGKSAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571965 Genomic DNA. Translation: CAH34431.1.
RefSeqYP_107068.1. NC_006350.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GW8X-ray1.93A/B1-249[»]
ProteinModelPortalQ63XU7.
SMRQ63XU7. Positions 2-236.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272560.BPSL0443.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH34431; CAH34431; BPSL0443.
GeneID3093540.
KEGGbps:BPSL0443.
PATRIC19260531. VBIBurPse99623_0497.

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.
OrthoDBEOG6C8N1H.
ProtClustDBPRK14115.

Enzyme and pathway databases

BioCycBPSE272560:GJNI-450-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...

Other

EvolutionaryTraceQ63XU7.

Entry information

Entry nameGPMA_BURPS
AccessionPrimary (citable) accession number: Q63XU7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 25, 2004
Last modified: February 19, 2014
This is version 63 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways