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

C1AZ61 (GPMA_RHOOB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:ROP_17420
OrganismRhodococcus opacus (strain B4) [Complete proteome] [HAMAP]
Taxonomic identifier632772 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length251 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 – 2512512,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_1000149528

Regions

Region26 – 2722-phospho-D-glycerate binding By similarity
Region92 – 9542-phospho-D-glycerate binding By similarity
Region119 – 12022-phospho-D-glycerate binding By similarity

Sites

Active site141Tele-phosphohistidine intermediate By similarity
Active site1851 By similarity
Binding site2012-phospho-D-glycerate By similarity
Binding site6512-phospho-D-glycerate By similarity
Binding site10312-phospho-D-glycerate By similarity
Binding site18712-phospho-D-glycerate By similarity

Sequences

Sequence LengthMass (Da)Tools
C1AZ61 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 28A4537E8ADDB4CA

FASTA25127,745
        10         20         30         40         50         60 
MNGMSTGTLV LLRHGESEWN ALNLFTGWVD VHLTDKGIAE GKRAGELLLE HNLLPDVLYT 

        70         80         90        100        110        120 
SLLRRAISTA NIALDTADRH WIPVIRDWRL NERHYGALQG RNKAQVKDKY GDEQFMLWRR 

       130        140        150        160        170        180 
SYDTPPPTIE PGSEYSQDTD PRYANLDEVP LTECLKDVVV RLIPYWEDTI SADLLAGKTV 

       190        200        210        220        230        240 
LITAHGNSLR ALVKHLDGIS DEDIAGLNIP TGIPLRYDLD ENLKPLNPGG TYLDPEAAAA 

       250 
GAAAVANQGG K 

« Hide

References

[1]"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP011115 Genomic DNA. Translation: BAH49989.1.
RefSeqYP_002778934.1. NC_012522.1.

3D structure databases

ProteinModelPortalC1AZ61.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING632772.ROP_17420.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH49989; BAH49989; ROP_17420.
GeneID7743807.
KEGGrop:ROP_17420.
PATRIC23220713. VBIRhoOpa21106_1751.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.
OrthoDBEOG6C8N1H.
ProtClustDBPRK14120.

Enzyme and pathway databases

BioCycROPA632772:GH0Q-1766-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 nameGPMA_RHOOB
AccessionPrimary (citable) accession number: C1AZ61
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 34 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