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

C5ADQ2 (C5ADQ2_BURGB) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 39. 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:bglu_1g31790 EMBL ACR30242.1
OrganismBurkholderia glumae (strain BGR1) [Complete proteome] [HAMAP] EMBL ACR30242.1
Taxonomic identifier626418 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length248 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 SAAS SAAS001345 RuleBase RU004512

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
   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

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
C5ADQ2 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: C114ABACD72823C5

FASTA24827,764
        10         20         30         40         50         60 
MHKLVLIRHG ESTWNKENRF TGWVDVDLTE QGNAEARQAG VLLKEAGYAF DVAYTSVLKR 

        70         80         90        100        110        120 
AIRTLWHVQD QMDQMYLPVI HSWRLNERHY GALSGLNKAE TAAKFGDEQV LVWRRSYDTP 

       130        140        150        160        170        180 
PPALAADDER APYGDPRYAK VPREQLPLTE CLKDTVARVL PLWNESIAPA IKSGRQVLIA 

       190        200        210        220        230        240 
AHGNSLRALI KYLDGISDAD IVGLNIPNGV PLVYELDENL KPIRHYYLGD QDAIAKAQAA 


VAQQGKAK 

« Hide

References

[1]"Complete genome sequence of Burkholderia glumae BGR1."
Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.
J. Bacteriol. 191:3758-3759(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BGR1 EMBL ACR30242.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001503 Genomic DNA. Translation: ACR30242.1.
RefSeqYP_002912946.1. NC_012724.2.

3D structure databases

ProteinModelPortalC5ADQ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING626418.bglu_1g31790.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR30242; ACR30242; bglu_1g31790.
GeneID7908190.
KEGGbgl:bglu_1g31790.
PATRIC19114133. VBIBurGlu130723_6117.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMAKDDERFP.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

BioCycBGLU626418:GJI5-3230-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 nameC5ADQ2_BURGB
AccessionPrimary (citable) accession number: C5ADQ2
Entry history
Integrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: June 11, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)