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A0B773 (A0B773_METTP) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 55. 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:Mthe_0757 EMBL ABK14547.1
OrganismMethanosaeta thermophila (strain DSM 6194 / PT) (Methanothrix thermophila (strain DSM 6194 / PT)) [Complete proteome] [HAMAP] EMBL ABK14547.1
Taxonomic identifier349307 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosaetaceaeMethanosaeta

Protein attributes

Sequence length218 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

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
   Molecular functionIsomerase HAMAP-Rule MF_01039 EMBL ABK14547.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

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

Sites

Active site91Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1751 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 site17712-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
A0B773 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 2CB5B1C5FF531B3F

FASTA21825,317
        10         20         30         40         50         60 
MYKLVLLRHG QSSYNAERRF TGWSDPDLTA QGMIEAREAG RILRRSGYTL DIAFVSMLRR 

        70         80         90        100        110        120 
AIKTLCGVLD EMDLLWIPVR KSWMLNERHY GELEGQIIDD VPDELKMYRH SFDIRPPALS 

       130        140        150        160        170        180 
EDDPRHPRFD RRYSDLESPP AGESIRDVQE RLLILWTYEI APEILSGRGV IVTTHANVIR 

       190        200        210 
AFMNYLEGVP TEGLMVPRGR PIVYELGEDL KPIRRYCL 

« Hide

References

[1]"Complete sequence of Methanosaeta thermophila PT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Smith K.S., Ingram-Smith C., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6194 / PT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000477 Genomic DNA. Translation: ABK14547.1.
RefSeqYP_843187.1. NC_008553.1.

3D structure databases

ProteinModelPortalA0B773.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349307.Mthe_0757.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK14547; ABK14547; Mthe_0757.
GeneID4463275.
KEGGmtp:Mthe_0757.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMAHLWRRSY.

Enzyme and pathway databases

BioCycMMET349307:GHKI-775-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
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]
SUPFAMSSF53254. SSF53254. 1 hit.
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA0B773_METTP
AccessionPrimary (citable) accession number: A0B773
Entry history
Integrated into UniProtKB/TrEMBL: November 28, 2006
Last sequence update: November 28, 2006
Last modified: June 11, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)