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Q01YD0 (GPMA_SOLUE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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=5.4.2.1
Gene names
Name:gpmA
Ordered Locus Names:Acid_4374
OrganismSolibacter usitatus (strain Ellin6076) [Complete proteome] [HAMAP]
Taxonomic identifier234267 [NCBI]
Taxonomic lineageBacteriaAcidobacteriaSolibacteresSolibacteralesSolibacteraceaeCandidatus Solibacter

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: UniProtKB-KW

   Molecular functionphosphoglycerate mutase activity

Inferred from electronic annotation. Source: EC

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_1000064098

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q01YD0 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 625CFCF90EF6A5F4

FASTA24828,238
        10         20         30         40         50         60 
MKKLVLIRHG ESTWNKENRF TGWTDVDLSD EGRQQATEAA EVLKREGYVF DVAYTSVLKR 

        70         80         90        100        110        120 
AIRTLWTVLD GMDLMWIPVH RSWRLNERHY GALQGLNKAE TAAKFGEDQV KIWRRSYDIP 

       130        140        150        160        170        180 
PPVLTADDPR FPGHDPRYQS LTKEELPLTE CLKDTVARFL PLWHDTIAPA IRSGQRVIIA 

       190        200        210        220        230        240 
AHGNSLRALV KYLDGVSEAD IVELNIPTGM PLVYELDDDL KPLNRYYLGD PEKVKAAMEA 


VAAQGKKK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000473 Genomic DNA. Translation: ABJ85335.1.
RefSeqYP_825620.1. NC_008536.1.

3D structure databases

ProteinModelPortalQ01YD0.
SMRQ01YD0. Positions 3-236.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ01YD0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4427368.
GenomeReviewsGene locus Acid_4374 in contig CP000473_GR.
KEGGsus:Acid_4374.
NMPDRfig|234267.9.peg.4160.
PATRIC32011240. VBICanSol30224_4585.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHBG658938.
OMAEWNALNL.
PhylomeDBQ01YD0.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
[Tree]
InterProIPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
KOK01834.
PANTHERPTHR11931. Phosphogly_mut1. 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_SOLUE
AccessionPrimary (citable) accession number: Q01YD0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 14, 2006
Last modified: January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families