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IPR000101 is a Gamma-glutamyltranspeptidase.
<p>Gamma-glutamyltranspeptidase ([ec:2.3.2.2]) (GGT) [[cite:PUB00003561]] catalyses the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification [[cite:PUB00006169]]. In prokaryotes and eukaryotes, it is an enzyme that consists of two polypeptide chains, a heavy and a light subunit, processed from a single chain precursor by an autocatalytic cleavage. The active site of GGT is known to be located in the light subunit. The sequences of mammalian and bacterial GGT show a number of regions of high similarity [[cite:PUB00002088]]. Pseudomonas cephalosporin acylases ([ec:3.5.1]) that convert 7-beta-(4-carboxybutanamido)-cephalosporanic acid (GL-7ACA) into 7-aminocephalosporanic acid (7ACA) and glutaric acid are evolutionary related to GGT and also show some GGT activity [[cite:PUB00000636]]. Like GGT, these GL-7ACA acylases, are also composed of two subunits. This entry also includes the highly similar Scoloptoxin SSD14 from Scolopendra dehaani. SSD14 (which is also cleaved into alpha and beta subunits) has been shown to induce human platelet aggregation [[cite:PUB00092777]].</p> <p>As an autocatalytic peptidase GGT belongs to MEROPS peptidase family T3 (gamma-glutamyltransferase family, clan PB(T)). The active site residue for members of this family and family T1 is C-terminal to the autolytic cleavage site. The type example is gamma-glutamyltransferase 1 from Escherichia coli.</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 |
|---|---|---|---|---|
| Biological process | Glutathione catabolic process | The chemical reactions and pathways resulting in the breakdown of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins. | ||
| Molecular function | Glutathione hydrolase activity | Catalysis of the reaction: glutathione + H2O = L-cysteinylglycine + L-glutamate. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | 7 | |||
| – | PREDICTED: gamma-glutamyltranspeptidase 1-like [Glycine max] gi|356520836|ref|XP_003529066.1| | 11 | ||
| – | Gamma-glutamyltranspeptidase; TAIR: AT4G29210.1 gamma-glutamyl transpeptidase 4; Swiss-Prot: sp|Q9M0G0|GAGT3_ARATH Gamma-glutamyltranspeptidase 3; TrEMBL-Plants: tr|I1KJR9|I1KJR9_SOYBN Uncharacterized protein; Found in the gene: LotjaGi2g1v0227900 | 16 | ||
| – | Gamma-glutamyltranspeptidase; TAIR: AT4G29210.1 gamma-glutamyl transpeptidase 4; Swiss-Prot: sp|Q9M0G0|GAGT3_ARATH Gamma-glutamyltranspeptidase 3; TrEMBL-Plants: tr|I1KJR9|I1KJR9_SOYBN Uncharacterized protein; Found in the gene: LotjaGi2g1v0227900 | 12 | ||
| – | Gamma-glutamyltranspeptidase; TAIR: AT4G39640.1 gamma-glutamyl transpeptidase 1; Swiss-Prot: sp|Q8VYW6|GAGT1_ARATH Gamma-glutamyltranspeptidase 1; TrEMBL-Plants: tr|I1LMY0|I1LMY0_SOYBN Uncharacterized protein; Found in the gene: LotjaGi6g1v0084100 | 20 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| TMhelix | TMHMM | 1 | 20.00 |