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Q0SMJ5 (GPMA_BORAP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:BAPKO_0702, BafPKo_0682
OrganismBorrelia afzelii (strain PKo) [Complete proteome] [HAMAP]
Taxonomic identifier390236 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

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

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 – 2482482,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_1000064033

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

Sequences

Sequence LengthMass (Da)Tools
Q0SMJ5 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 342F369B47AB0E0E

FASTA24828,499
        10         20         30         40         50         60 
MYKLVLVRHG ESEWNKENLF TGWTDVKLSD KGVDEAIEAG LLLKQEGYFF DIAFSSLLSR 

        70         80         90        100        110        120 
ANDTLNIILK ELGQSYISVK KTWRLNERHY GALQGLNKSE TAAKYGEDKV LIWRRSYDVP 

       130        140        150        160        170        180 
PMSLDESDDR HPIKDPRYKY IPKRELPSTE CLKDTIARVI PYWIDEIAKE ILEGKKVIVA 

       190        200        210        220        230        240 
AHGNSLRALV KYLDNLSEED VLKLNIPTGI PLVYELDKDL NPIKHYYLGD ENKIKKAMES 


VASQGKLR 

« Hide

References

[1]"Comparative genome analysis: selection pressure on the Borrelia vls cassettes is essential for infectivity."
Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J., Wilske B., Platzer M.
BMC Genomics 7:211-211(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PKo.
[2]"Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii Lyme disease agent isolates."
Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J., Fraser-Liggett C.M., Schutzer S.E.
J. Bacteriol. 193:6995-6996(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PKo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000395 Genomic DNA. Translation: ABH01933.1.
CP002933 Genomic DNA. Translation: AEL69878.1.
RefSeqYP_005592868.1. NC_017238.1.
YP_710109.1. NC_008277.1.

3D structure databases

ProteinModelPortalQ0SMJ5.
SMRQ0SMJ5. Positions 2-239.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390236.BAPKO_0702.

Proteomic databases

PRIDEQ0SMJ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABH01933; ABH01933; BAPKO_0702.
AEL69878; AEL69878; BafPKo_0682.
GeneID12158770.
4227649.
KEGGbaf:BAPKO_0702.
bafz:BafPKo_0682.
PATRIC37189661. VBIBorAfz3878_0718.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

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_BORAP
AccessionPrimary (citable) accession number: Q0SMJ5
Secondary accession number(s): G0IQK8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 5, 2006
Last modified: February 19, 2014
This is version 58 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