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B1VS80 (GPMA_STRGG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 41. 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:SGR_4005
OrganismStreptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350) [Complete proteome] [HAMAP]
Taxonomic identifier455632 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length253 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_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

Molecule processing

Chain1 – 2532532,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_1000135980

Regions

Region25 – 2622-phospho-D-glycerate binding By similarity
Region91 – 9442-phospho-D-glycerate binding By similarity
Region118 – 11922-phospho-D-glycerate binding By similarity

Sites

Active site131Tele-phosphohistidine intermediate By similarity
Active site1861 By similarity
Binding site1912-phospho-D-glycerate By similarity
Binding site6412-phospho-D-glycerate By similarity
Binding site10212-phospho-D-glycerate By similarity
Binding site18812-phospho-D-glycerate By similarity

Sequences

Sequence LengthMass (Da)Tools
B1VS80 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 805B19AE803FD97C

FASTA25328,425
        10         20         30         40         50         60 
MADAPYKLIL LRHGESEWNA KNLFTGWVDV NLTEKGEKEA VRGGELLKDA GLLPDVLHTS 

        70         80         90        100        110        120 
LQRRAIRTAQ LALESADRLW IPVRRSWRLN ERHYGALQGK DKAQTLAEFG EEQFMLWRRS 

       130        140        150        160        170        180 
YDTPPPPLAR DDEFSQFDDP RYATLPPEVR PDTECLKDVV VRMLPYWFDS IVPDLLTGRT 

       190        200        210        220        230        240 
VLVAAHGNSL RGLVKHLDGI SDEDISGLNI PTGIPLSYEL DADFKPLKPG GTYLDPDAAK 

       250 
AAIEAVKNQG KKK 

« Hide

References

[1]"Genome sequence of the streptomycin-producing microorganism Streptomyces griseus IFO 13350."
Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H., Yamashita A., Hattori M., Horinouchi S.
J. Bacteriol. 190:4050-4060(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 4626 / NBRC 13350.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009493 Genomic DNA. Translation: BAG20834.1.
RefSeqYP_001825517.1. NC_010572.1.

3D structure databases

ProteinModelPortalB1VS80.
SMRB1VS80. Positions 8-242.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING455632.SGR_4005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG20834; BAG20834; SGR_4005.
GeneID6214098.
KEGGsgr:SGR_4005.
PATRIC23754614. VBIStrGri32265_4077.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMAWTILEGT.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

BioCycSGRI455632:GD3A-4049-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 nameGPMA_STRGG
AccessionPrimary (citable) accession number: B1VS80
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 41 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