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A4TNS2 (GPMA_YERPP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 50. 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:YPDSF_2564
OrganismYersinia pestis (strain Pestoides F) [Complete proteome] [HAMAP]
Taxonomic identifier386656 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

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

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.

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

Chain1 – 2502502,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_1000064118

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
A4TNS2 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 3AF66E98C0AA8FEC

FASTA25028,358
        10         20         30         40         50         60 
MAVTKLVLVR HGESQWNNEN RFTGWYDVDL SEKGRSEAKA AGKLLKDEGF TFDFAYTSVL 

        70         80         90        100        110        120 
KRAIHTLWNI LDELDQAWLP TEKTWKLNER HYGALQGLNK SETAEKYGDE QVKQWRRGFA 

       130        140        150        160        170        180 
ITPPALEKSD ERFPGHDPRY AKLTDAELPT TESLALTIER VIPYWNDVIK PRIASGERVI 

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

       250 
AAVANQGKAK 

« Hide

References

[1]"Complete sequence of chromosome of Yersinia pestis Pestoides F."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pestoides F.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000668 Genomic DNA. Translation: ABP40934.1.
RefSeqYP_001163907.1. NC_009381.1.

3D structure databases

ProteinModelPortalA4TNS2.
SMRA4TNS2. Positions 3-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING386656.YPDSF_2564.

Proteomic databases

PRIDEA4TNS2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP40934; ABP40934; YPDSF_2564.
GeneID5063496.
KEGGypp:YPDSF_2564.
PATRIC18614758. VBIYerPes122972_3274.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMARYATIPP.
OrthoDBEOG6C8N1H.

Enzyme and pathway databases

BioCycYPES386656:GKD7-2611-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 nameGPMA_YERPP
AccessionPrimary (citable) accession number: A4TNS2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 15, 2007
Last modified: June 11, 2014
This is version 50 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