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A6L625 (A6L625_BACV8) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 53. 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
Ordered Locus Names:BVU_3515 EMBL ABR41139.1
OrganismBacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP] EMBL ABR41139.1
Taxonomic identifier435590 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length249 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

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 SAAS SAAS001345 HAMAP-Rule MF_01039
   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

Region21 – 2222-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region87 – 9042-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region114 – 11522-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site91Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1821 By similarity HAMAP-Rule MF_01039
Binding site1512-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6012-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site9812-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18412-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
A6L625 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 08CD5AB8561F85FC

FASTA24928,490
        10         20         30         40         50         60 
MKRIVLLRHG ESLWNKENRF TGWTDVDLSE KGVEEACKAG DALREAGFSF EAAYTSYLKR 

        70         80         90        100        110        120 
AVKTLNCVLD RLDEDWIPVE KTWRLNEKHY GMLQGLNKSE TAVQYGEEQV HIWRRSYDVA 

       130        140        150        160        170        180 
PAPVGKDDPR NPGMDIRYAG VPDRELPRTE SLKDTIGRVM PYWKCIIFPA LMYKDSLLVV 

       190        200        210        220        230        240 
AHGNSLRGII KHLKGISDTD ISNLNLPTAV PYVFEFDDRL VLVKDYYLGN PEEIRKRAEA 


VAKQGMAKK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000139 Genomic DNA. Translation: ABR41139.1.
RefSeqYP_001300761.1. NC_009614.1.

3D structure databases

ProteinModelPortalA6L625.
SMRA6L625. Positions 1-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING435590.BVU_3515.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR41139; ABR41139; BVU_3515.
GeneID5304475.
KEGGbvu:BVU_3515.
PATRIC21072086. VBIBacVul85104_3624.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMANDEIAPQ.
OrthoDBEOG6C8N1H.
ProtClustDBPRK14115.

Enzyme and pathway databases

BioCycBVUL435590:GH96-3506-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 nameA6L625_BACV8
AccessionPrimary (citable) accession number: A6L625
Entry history
Integrated into UniProtKB/TrEMBL: July 24, 2007
Last sequence update: July 24, 2007
Last modified: February 19, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)