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{
"metadata": {
"accession": "PS51443",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
"member_databases": null,
"integrated": "IPR007719",
"hierarchy": null,
"name": {
"name": "Phytochelatin synthase (PCS) domain profile",
"short": "PCS"
},
"description": [
{
"text": "<p>Phytochelatins (PCs) are well known as the heavy metal-detoxifying peptides in\nhigher plants, eukaryotic algae, fungi, nematode and cyanobacteria. These\npeptides, of the general structure (gamma-Glu-Cys)n-Gly (with n=2-11), are\nenzymatically synthesized from the substrate glutathione (GSH). PCs are\nsynthesized posttranslationally by the PC synthase (PCS) (EC 2.3.2.15), a\ngamma-glutamylcysteine (gamma-EC) transpeptidase. PC synthesis is proposed to\nhave two distinct steps: (Step1) formation of gamma-EC concomitant with the\ncleavage of Gly from GSH; and (Step 2) transfer of the gamma-EC unit to an\nacceptor GSH molecule or an oligomeric PC peptide (PCn). Eukaryotic PCS\ntypically has a conserved N-terminal domain and a variable C-terminal domain,\nboth of which are cysteine-rich. The N-terminal core domain is sufficient to\nconfer a PCS activity and therefore can be referred to the catalytic domain.\nCyanobacterial PCS contains the conserved N-terminal catalytic domain but not\nthe variable C-terminal domain found in eukaryotic PCSs. It can act as a GSH\nhydrolase and weakly as a peptide ligase [[cite:PUB00047123]][[cite:PUB00039759]].\n\nThe catalytic PCS domain belongs to the petidase family C83 of the papain\nsuperfamily of cysteine proteases [E1], with the structurally conserved\n\"catalytic triad\" and oxyanion hole in the active site. It has an overall\n\"crescent\" shape with alpha/beta fold containing eight alpha-helices and six\nbeta-strands [[cite:PUB00039759]].\n\nThe profile we developed covers the entire PCS domain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00039759": {
"PMID": 16339904,
"ISBN": null,
"volume": "102",
"issue": "52",
"year": 2005,
"title": "A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis.",
"URL": null,
"raw_pages": "18848-53",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Vivares D",
"Arnoux P",
"Pignol D."
],
"DOI_URL": "http://dx.doi.org/10.1073/pnas.0505833102"
},
"PUB00047123": {
"PMID": 14975765,
"ISBN": null,
"volume": "315",
"issue": "3",
"year": 2004,
"title": "Characterization of phytochelatin synthase-like protein encoded by alr0975 from a prokaryote, Nostoc sp. PCC 7120.",
"URL": null,
"raw_pages": "751-5",
"medline_journal": "Biochem Biophys Res Commun",
"ISO_journal": "Biochem. Biophys. Res. Commun.",
"authors": [
"Tsuji N",
"Nishikori S",
"Iwabe O",
"Shiraki K",
"Miyasaka H",
"Takagi M",
"Hirata K",
"Miyamoto K."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.bbrc.2004.01.122"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 3290,
"pathways": 0,
"proteins": 3261,
"proteomes": 1353,
"sets": 0,
"structural_models": {
"alphafold": 2768,
"bfvd": 0
},
"structures": 5,
"taxa": 3985
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "6tho",
"name": "Acylintermediate of glutathione and the mature primitive phytochelatin synthase Alr0975 from Nostoc PCC 7120 at atomic resolution."
}
}
}
