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IPR004456 is a 2,3-bisphosphoglycerate-independent phosphoglycerate mutase.
<p>This family represents 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM), it is a metalloenzyme found particularly in archaea and some eubacteria. It is responsible for the interconversion of 2-phosphoglycerate and 3-phosphoglycerate [[cite:PUB00055097]]. It is distantly related to the iPGAM ([interpro:IPR005995]) characteristic of plants and many eubacteria. The common active site and metal-binding residues of the phosphatase domain are easily identified, but the putative phosphotransferase domain is highly diverged. These proteins are unrelated to the cofactor-dependent PGAM. Activity has been demonstrated for proteins from Methanocaldococcus jannaschii (Methanococcus jannaschii) [[cite:PUB00014447], [cite:PUB00014397]], Pyrococcus furiosus [[cite:PUB00014397]], and Sulfolobus solfataricus [[cite:PUB00014464]]. These proteins were initially misidentified as phosphonopyruvate decarboxylase.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Catalytic activity | Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. | ||
| Molecular function | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity | Catalysis of the reaction: 2-phospho-D-glycerate = 3-phospho-D glycerate; this reaction does not require the cofactor 2,3-bisphosphoglycerate. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1-like [Glycine max] gi|356568873|ref|XP_003552632.1| | 10 | ||
| – | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase; TAIR: AT3G30841.1 Cofactor-independent phosphoglycerate mutase; Swiss-Prot: sp|O27628|APGM1_METTH 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1; TrEMBL-Plants: tr|I3SP89|I3SP89_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0524100 | 12 | ||
| – | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase; TAIR: AT3G30841.1 Cofactor-independent phosphoglycerate mutase; Swiss-Prot: sp|O27628|APGM1_METTH 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1; TrEMBL-Plants: tr|I3SP89|I3SP89_LOTJA Uncharacterized protein; Found in the gene: LotjaGi1g1v0524100 | 12 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd16011 | CDD | 1 | 33.33 |