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P62708 (GPMA_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 68. 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
Synonyms:gpm, pgm, pgmA
Ordered Locus Names:c0831
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01039

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Sequence caution

The sequence AAN79304.1 differs from that shown. Reason: Erroneous initiation.

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

Initiator methionine11Removed By similarity
Chain2 – 2502492,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_0000179875

Regions

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

Sites

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

Sequences

Sequence LengthMass (Da)Tools
P62708 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A6E0A49406F8482A

FASTA25028,556
        10         20         30         40         50         60 
MAVTKLVLVR HGESQWNKEN RFTGWYDVDL SEKGVSEAKA AGKLLKEEGY SFDFAYTSVL 

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

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

       190        200        210        220        230        240 
IAAHGNSLRA LVKYLDNMSE EEILELNIPT GVPLVYEFDE NFKPLKRYYL GNADEIAAKA 

       250 
AAVANQGKAK 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN79304.1. Different initiation.
RefSeqNP_752761.1. NC_004431.1.

3D structure databases

ProteinModelPortalP62708.
SMRP62708. Positions 2-248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c0831.

Proteomic databases

PRIDEP62708.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN79304; AAN79304; c0831.
GeneID1037999.
KEGGecc:c0831.
PATRIC18279721. VBIEscCol75197_0790.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000221682.
KOK01834.
OMARYATIPP.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

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_ECOL6
AccessionPrimary (citable) accession number: P62708
Secondary accession number(s): P31217
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 68 of the entry and version 2 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