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

E3ER63 (E3ER63_BIFBS) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 25. 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:gpm5 EMBL ADO53638.1
Synonyms:gpmA HAMAP-Rule MF_01039
Ordered Locus Names:BBIF_1433 EMBL ADO53638.1
OrganismBifidobacterium bifidum (strain S17) [Complete proteome] [HAMAP] EMBL ADO53638.1
Taxonomic identifier883062 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length246 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

Region22 – 2322-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region88 – 9142-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region115 – 11622-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site101Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1801 By similarity HAMAP-Rule MF_01039
Binding site1612-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6112-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site9912-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18212-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
E3ER63 [UniParc].

Last modified January 11, 2011. Version 1.
Checksum: 55D75151C543DBA1

FASTA24627,627
        10         20         30         40         50         60 
MTYKLVLLRH GQSAWNKTNQ FTGWVDVPLT EQGEAEAKRG GELLKEKNVL PDIVFTSLLR 

        70         80         90        100        110        120 
RAINTANIAL DAADRLWIPV QRDWRLNERH YGALQGKNKT EIRQEYGDEK FMLWRRSYAT 

       130        140        150        160        170        180 
PPPEIDPNDQ YAQNHDPRYA GDPVPEAECL ANVVERVKPY FESAIEPELR AGKTVLIAAH 

       190        200        210        220        230        240 
GNSLRAIVKM LDNLSEDEIA KVNIPTAIPL LYELDENFKP VKPRGEYLDP EAAAAGAAAV 


AAQGQK 

« Hide

References

[1]"Complete genome sequence of Bifidobacterium bifidum S17."
Zhurina D., Zomer A., Gleinser M., Brancaccio V.F., Auchter M., Waidmann M.S., Westermann C., van Sinderen D., Riedel C.U.
J. Bacteriol. 193:301-302(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S17 EMBL ADO53638.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002220 Genomic DNA. Translation: ADO53638.1.
RefSeqYP_003939212.1. NC_014616.1.

3D structure databases

ProteinModelPortalE3ER63.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADO53638; ADO53638; BBIF_1433.
GeneID9847666.
KEGGbbi:BBIF_1433.
PATRIC42480424. VBIBifBif172477_1488.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000221682.
KOK01834.
OMAKDDERFP.

Enzyme and pathway databases

BioCycBBIF883062:GH1R-1477-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 nameE3ER63_BIFBS
AccessionPrimary (citable) accession number: E3ER63
Entry history
Integrated into UniProtKB/TrEMBL: January 11, 2011
Last sequence update: January 11, 2011
Last modified: June 11, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)