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P0A5R6 (GPMA_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:gpm, gpm1, pgm
Ordered Locus Names:Rv0489, MT0508
ORF Names:MTCY20G9.15
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

Inferred from direct assay. Source: MTBBASE

   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 – 2492492,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP MF_01039
PRO_0000179893

Regions

Compositional bias235 – 2428Poly-Ala HAMAP MF_01039

Sites

Active site121Tele-phosphohistidine intermediate By similarity
Active site1831 By similarity
Site631Interaction with carboxyl group of phosphoglycerates By similarity

Secondary structure

1 ........................................ 249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A5R6 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 7063E6B91CDFF339

FASTA24927,216
        10         20         30         40         50         60 
MANTGSLVLL RHGESDWNAL NLFTGWVDVG LTDKGQAEAV RSGELIAEHD LLPDVLYTSL 

        70         80         90        100        110        120 
LRRAITTAHL ALDSADRLWI PVRRSWRLNE RHYGALQGLD KAETKARYGE EQFMAWRRSY 

       130        140        150        160        170        180 
DTPPPPIERG SQFSQDADPR YADIGGGPLT ECLADVVARF LPYFTDVIVG DLRVGKTVLI 

       190        200        210        220        230        240 
VAHGNSLRAL VKHLDQMSDD EIVGLNIPTG IPLRYDLDSA MRPLVRGGTY LDPEAAAAGA 


AAVAGQGRG

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842573 Genomic DNA. Translation: CAE55288.1.
AE000516 Genomic DNA. Translation: AAK44731.1.
PIRD70744.
RefSeqNP_334917.1. NC_002755.2.
YP_177731.1. NC_000962.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RIIX-ray1.70A/B/C/D1-249[»]
ProteinModelPortalP0A5R6.
SMRP0A5R6. Positions 3-239.
DisProtDP00295.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000000598; EBMYCP00000000598; EBMYCG00000000598.
EBMYCT00000071648; EBMYCP00000069707; EBMYCG00000071643.
GeneID887183.
923869.
GenomeReviewsGene locus MT0508 in contig AE000516_GR.
Gene locus Rv0489 in contig AL123456_GR.
KEGGmtc:MT0508.
mtu:Rv0489.
PATRIC18122824. VBIMycTub22151_0546.
TIGRMT0508.

Organism-specific databases

TubercuListRv0489.

Phylogenomic databases

GeneTreeEBGT00050000015087.
HOGENOMHBG658938.
OMAEWNALNL.
PhylomeDBP0A5R6.
ProtClustDBPRK14120.

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_MYCTU
AccessionPrimary (citable) accession number: P0A5R6
Secondary accession number(s): Q11140
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: January 25, 2012
This is version 48 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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