{"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."}}}