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F7XS04 (F7XS04_TREPU) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 18. 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:TPCCA_0168 EMBL AEH40123.1
OrganismTreponema paraluiscuniculi (strain Cuniculi A) [Complete proteome] [HAMAP] EMBL AEH40123.1
Taxonomic identifier545776 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema

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. RuleBase RU004512 HAMAP-Rule MF_01039

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. RuleBase RU004512 HAMAP-Rule MF_01039 SAAS SAAS001345

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. RuleBase RU004512 HAMAP-Rule MF_01039

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

Region20 – 2122-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region86 – 8942-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region113 – 11422-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site81Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1851 By similarity HAMAP-Rule MF_01039
Binding site1412-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site5912-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site9712-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18712-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
F7XS04 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 8589EE625A80D60B

FASTA25128,358
        10         20         30         40         50         60 
MKLVLIRHGE SEWNRLNLFT GWTDVPLTPR GESEAQEGGR VLQEAGFDFD LCYTSFLKRA 

        70         80         90        100        110        120 
IRTLNFVLQA LDREWLPVHK SWKLNERHYG DLQGLNKTET AQKYGEQQVR VWRRSFDVAP 

       130        140        150        160        170        180 
PPLTVGDARC PHTQASYRGV CASGRTPVLP FTESLKDTVA RVVPYFEEEI KPQMISGQRV 

       190        200        210        220        230        240 
LIVAHGNSLR ALMKHIESLD ETQIMEVNLP TGVPLVYEFE ADFTLCGKRF LGNEADVAAR 

       250 
AQAVADQGKS N 

« Hide

References

[1]"Complete genome sequence of Treponema paraluiscuniculi, strain Cuniculi A: the loss of infectivity to humans is associated with genome decay."
Smajs D., Zobanikova M., Strouhal M., Cejkova D., Dugan-Rocha S., Pospisilova P., Norris S.J., Albert T., Qin X., Hallsworth-Pepin K., Buhay C., Muzny D.M., Chen L., Gibbs R.A., Weinstock G.M.
PLoS ONE 6:E20415-E20415(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Cuniculi A EMBL AEH40123.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002103 Genomic DNA. Translation: AEH40123.1.
RefSeqYP_004672914.1. NC_015714.1.

3D structure databases

ProteinModelPortalF7XS04.
SMRF7XS04. Positions 1-249.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEH40123; AEH40123; TPCCA_0168.
GeneID10883848.
KEGGtpl:TPCCA_0168.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01834.

Enzyme and pathway databases

BioCycTPAR545776:GJC6-179-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 nameF7XS04_TREPU
AccessionPrimary (citable) accession number: F7XS04
Entry history
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: June 11, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)