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A4T096 (GPMA_POLSQ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:Pnuc_1948
OrganismPolynucleobacter necessarius subsp. asymbioticus (strain DSM 18221 / CIP 109841 / QLW-P1DMWA-1) [Complete proteome] [HAMAP]
Taxonomic identifier312153 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaePolynucleobacter

Protein attributes

Sequence length229 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

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_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

Molecule processing

Chain1 – 2292292,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039
PRO_1000084327

Regions

Region21 – 2222-phospho-D-glycerate binding By similarity
Region87 – 9042-phospho-D-glycerate binding By similarity
Region114 – 11522-phospho-D-glycerate binding By similarity

Sites

Active site91Tele-phosphohistidine intermediate By similarity
Active site1821 By similarity
Binding site1512-phospho-D-glycerate By similarity
Binding site6012-phospho-D-glycerate By similarity
Binding site9812-phospho-D-glycerate By similarity
Binding site18412-phospho-D-glycerate By similarity

Sequences

Sequence LengthMass (Da)Tools
A4T096 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: E946BD6C41659698

FASTA22926,322
        10         20         30         40         50         60 
MKQLVLIRHG ESAWNLENRF TGWADVDLTP KGAEQALAAG EHLRKAGYEF DVAYTSVLRR 

        70         80         90        100        110        120 
AIRTLWHVQD AMDLMWLPVV HSWRLNERHY GALTGLNKAE TAAQYGDEQV HIWRRSYDIR 

       130        140        150        160        170        180 
PPLLEADDER NPKNDSRYAK LNESDIPLGE CLKDNVERVL PLWNESIAPA LKANKRVLLV 

       190        200        210        220 
AHGNSIRSLI KYLDQMSDEA IMEVNVPNGI PLVYELDDNL KPIQHFYLD 

« Hide

References

[1]"Complete genome sequence of Polynucleobacter necessarius subsp. asymbioticus type strain (QLW-P1DMWA-1(T))."
Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M., Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.
Stand. Genomic Sci. 6:74-83(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 18221 / CIP 109841 / QLW-P1DMWA-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000655 Genomic DNA. Translation: ABP35160.1.
RefSeqYP_001156724.1. NC_009379.1.

3D structure databases

ProteinModelPortalA4T096.
SMRA4T096. Positions 3-228.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING312153.Pnuc_1948.

Proteomic databases

PRIDEA4T096.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP35160; ABP35160; Pnuc_1948.
GeneID5053013.
KEGGpnu:Pnuc_1948.
PATRIC22968421. VBIPolNec12025_2014.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.
OrthoDBEOG6C8N1H.
ProtClustDBPRK14115.

Enzyme and pathway databases

BioCycPNEC312153:GH50-1991-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 nameGPMA_POLSQ
AccessionPrimary (citable) accession number: A4T096
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 15, 2007
Last modified: February 19, 2014
This is version 53 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