glutathionylspermidine synthase preATP-grasp family protein similar to Escherichia coli bifunctional glutathionylspermidine synthetase/amidase that catalyzes the formation of glutathionylspermidine from glutathione and spermidine; also catalyzes the reverse reaction
Glutathionylspermidine synthase preATP-grasp; This region contains the Glutathionylspermidine ...
269-614
7.35e-76
Glutathionylspermidine synthase preATP-grasp; This region contains the Glutathionylspermidine synthase enzymatic activity EC:6.3.1.8. This is the C-terminal region in bi-enzymes. Glutathionylspermidine (GSP) synthetases of Trypanosomatidae and Escherichia coli couple hydrolysis of ATP (to ADP and Pi) with formation of an amide bond between spermidine and the glycine carboxylate of glutathione (gamma-Glu-Cys-Gly). In the pathogenic trypanosomatids, this reaction is the penultimate step in the biosynthesis of the antioxidant metabolite, trypanothione (N1,N8-bis-(glutathionyl)spermidine), and is a target for drug design. This region, the pre-ATP grasp region, probably carries the substrate-binding site.
Pssm-ID: 427476 Cd Length: 371 Bit Score: 247.10 E-value: 7.35e-76
Glutathionylspermidine synthase preATP-grasp; This region contains the Glutathionylspermidine ...
269-614
7.35e-76
Glutathionylspermidine synthase preATP-grasp; This region contains the Glutathionylspermidine synthase enzymatic activity EC:6.3.1.8. This is the C-terminal region in bi-enzymes. Glutathionylspermidine (GSP) synthetases of Trypanosomatidae and Escherichia coli couple hydrolysis of ATP (to ADP and Pi) with formation of an amide bond between spermidine and the glycine carboxylate of glutathione (gamma-Glu-Cys-Gly). In the pathogenic trypanosomatids, this reaction is the penultimate step in the biosynthesis of the antioxidant metabolite, trypanothione (N1,N8-bis-(glutathionyl)spermidine), and is a target for drug design. This region, the pre-ATP grasp region, probably carries the substrate-binding site.
Pssm-ID: 427476 Cd Length: 371 Bit Score: 247.10 E-value: 7.35e-76
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
46-140
4.01e-04
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.
Pssm-ID: 461605 [Multi-domain] Cd Length: 83 Bit Score: 39.71 E-value: 4.01e-04
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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