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D6Y4U9 (D6Y4U9_THEBD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | 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 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=5.4.2.1 HAMAP-Rule MF_01039
Gene names
Name:gpmA HAMAP-Rule MF_01039
Ordered Locus Names:Tbis_0496 EMBL ADG87224.1
OrganismThermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / NBRC 14880 / R51) [Complete proteome] [HAMAP] EMBL ADG87224.1
Taxonomic identifier469371 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Thermobispora ›

Protein attributes

Sequence length247 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. RuleBase RU004512 HAMAP-Rule MF_01039

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. RuleBase RU004512 HAMAP-Rule MF_01039 SAAS SAAS013078

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. RuleBase RU004512 HAMAP-Rule MF_01039

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily. HAMAP-Rule MF_01039

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site91Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1821 By similarity HAMAP-Rule MF_01039
Site601Interaction with carboxyl group of phosphoglycerates By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
D6Y4U9 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: E0CCDBEE1D6850D7

FASTA24727,596
        10         20         30         40         50         60 
MATLVLLRHG ESEWNLKGLF TGWVDVTLSP AGEEEARRGG RLLVEKGIYP DVVHTSVLTR 

        70         80         90        100        110        120 
AIKTANLALE AAGLLWLPVK RSWRLNERHY GALQGKDKAQ TRAQFGDEQF MLWRRSYDVP 

       130        140        150        160        170        180 
PPPIADDDEF SQRGDRRYAN LPPELIPRTE CLKDVVARLL PYWYDEIVPD LAAGKTVLVV 

       190        200        210        220        230        240 
AHGNSLRALV KHLEGISDQD IVGLNIPTGI PLRYELDENF RPKGPGEYLD PEAAKAAIEA 


VANQGKK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001874 Genomic DNA. Translation: ADG87224.1.
RefSeqYP_003651117.1. NC_014165.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADG87224; ADG87224; Tbis_0496.
GeneID9166978.
KEGGtbi:Tbis_0496.
PATRIC38283884. VBITheBis80272_0493.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000221682.
KOK01834.

Enzyme and pathway databases

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 nameD6Y4U9_THEBD
AccessionPrimary (citable) accession number: D6Y4U9
Entry history
Integrated into UniProtKB/TrEMBL: August 10, 2010
Last sequence update: August 10, 2010
Last modified: May 1, 2013
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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