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Reviewed, UniProtKB/Swiss-Prot Q5LAT7 (GPMA_BACFN)

Last modified February 9, 2010. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
      Short name=Phosphoglyceromutase
      Short name=PGAM
      Short name=BPG-dependent PGAM
      Short name=dPGM
    EC=5.4.2.1
Gene names
Name: gpmA
Ordered Locus Names: BF3091
OrganismBacteroides fragilis (strain ATCC 25285 / NCTC 9343) [Complete proteome] [HAMAP]
Taxonomic identifier272559 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. HAMAP MF_01039

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01039

Pathway

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

   Molecular function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2482482,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP MF_01039
PRO_0000229105

Sites

Active site91Tele-phosphohistidine intermediate By similarity
Active site1821 By similarity
Site601Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LAT7-1 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: 9AABB6D011528F18

FASTA24828,803
        10         20         30         40         50         60 
MKKIVLLRHG ESAWNKENRF TGWTDVDLTE KGIAEACKAG ELLKENGFNF DKAYTSYLKR 

        70         80         90        100        110        120 
AVKTLNCVLD RMDQDWIPVE KSWRLNEKHY GDLQGLNKSE TAAKYGDEQV LIWRRSYDIA 

       130        140        150        160        170        180 
PNALSEDDPR NPRFENRYQE VPDAELPRTE SLKDTIERIM PYWKCIIFPN LKTADEILVV 

       190        200        210        220        230        240 
AHGNSLRGII KHLKHISDEE IVKLNLPTAV PYVFEFSDEL NLEKDYFLGD PEEIRKLMEA 


VANQGKKK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR626927 Genomic DNA. Translation: CAH08786.1.
RefSeqYP_212704.1.

3D structure databases

SMRQ5LAT7. Positions 1-246.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5LAT7.

Genome annotation databases

GeneID3289187.
GenomeReviewsGene locus BF3091 in contig CR626927_GR.
KEGGbfs:BF3091.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHBG658938.
OMAVPLTECL.

Enzyme and pathway databases

BioCycBFRA272559:BF3091-MONOMER.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
[Tree]
InterProIPR001345. PG/BPGM_mutase_AS.
IPR013078. PG_mutase.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. Phosphogly_mut1. 1 hit.
PfamPF00300. PGAM. 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_BACFN
AccessionPrimary (citable) accession number: Q5LAT7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: June 21, 2005
Last modified: February 9, 2010
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents