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D2TPF5 (D2TPF5_CITRI) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 27. 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 EMBL CBG87524.1
Ordered Locus Names:ROD_07471 EMBL CBG87524.1
OrganismCitrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280) [Complete proteome] [HAMAP] EMBL CBG87524.1
Taxonomic identifier637910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter

Protein attributes

Sequence length250 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 RuleBase RU004512

Catalytic activity

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

Pathway

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

Subunit structure

Homodimer By similarity. 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_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

Regions

Region23 – 2422-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region89 – 9242-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region116 – 11722-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site111Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1841 By similarity HAMAP-Rule MF_01039
Binding site1712-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6212-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site10012-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18612-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
D2TPF5 [UniParc].

Last modified March 2, 2010. Version 1.
Checksum: 1814C950DA5843FB

FASTA25028,493
        10         20         30         40         50         60 
MAVTKLVLVR HGESQWNNEN RFTGWYDVDL SEKGVGEAKA AGKLLKEEGY SFDFAYTSVL 

        70         80         90        100        110        120 
KRAIHTLWNV LDELDQAWLP VEKSWKLNER HYGALQGLNK AETAEKYGDE QVKQWRRGFA 

       130        140        150        160        170        180 
VTPPELTKDD ERYPGHDPRY AKLTEKELPL TESLALTIDR VIPYWNETIL PRMKSGERVI 

       190        200        210        220        230        240 
IAAHGNSLRA LVKYLDNMSE DEILELNIPT GVPLVYEFDE NFKPIKHYYL GNADEIAAKA 

       250 
AAVANQGKAK 

« Hide

References

[1]"The Citrobacter rodentium genome sequence reveals convergent evolution with human pathogenic Escherichia coli."
Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N., Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L., Parkhill J., Dougan G., Frankel G., Thomson N.R.
J. Bacteriol. 192:525-538(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ICC168 EMBL CBG87524.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FN543502 Genomic DNA. Translation: CBG87524.1.
RefSeqYP_003364371.1. NC_013716.1.

3D structure databases

ProteinModelPortalD2TPF5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBG87524; CBG87524; ROD_07471.
GeneID8710392.
KEGGcro:ROD_07471.
PATRIC32025397. VBICitRod33214_0733.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.

Enzyme and pathway databases

BioCycCROD637910:GJIG-771-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 nameD2TPF5_CITRI
AccessionPrimary (citable) accession number: D2TPF5
Entry history
Integrated into UniProtKB/TrEMBL: March 2, 2010
Last sequence update: March 2, 2010
Last modified: February 19, 2014
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)