{"metadata":{"accession":"cd10317","entry_id":null,"type":"domain","go_terms":null,"source_database":"cdd","member_databases":null,"integrated":null,"hierarchy":null,"name":{"name":"C-terminal domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase","short":"RGL4_C"},"description":[{"text":"<p>The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold.  Both the middle and the C-terminal domain are putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11. [[cite:PUB00083824], [cite:PUB00027701], [cite:PUB00083820], [cite:PUB00083822], [cite:PUB00083823]]</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00083823":{"PMID":7654407,"ISBN":null,"volume":"16","issue":"4","year":1995,"title":"Polysaccharide lyases.","URL":null,"raw_pages":"323-47","medline_journal":"FEMS Microbiol Rev","ISO_journal":"FEMS Microbiol. Rev.","authors":["Sutherland IW."],"DOI_URL":"http://dx.doi.org/10.1111/j.1574-6976.1995.tb00179.x"},"PUB00083822":{"PMID":15224891,"ISBN":null,"volume":"23","issue":"4","year":2003,"title":"Polysaccharide lyases: recent developments as biotechnological tools.","URL":null,"raw_pages":"233-66","medline_journal":"Crit Rev Biotechnol","ISO_journal":"Crit. Rev. Biotechnol.","authors":["Michaud P","Da Costa A","Courtois B","Courtois J."],"DOI_URL":"http://dx.doi.org/10.1080/07388550390447043"},"PUB00083824":{"PMID":20925655,"ISBN":null,"volume":"432","issue":"3","year":2010,"title":"A hierarchical classification of polysaccharide lyases for glycogenomics.","URL":null,"raw_pages":"437-44","medline_journal":"Biochem J","ISO_journal":"Biochem. J.","authors":["Lombard V","Bernard T","Rancurel C","Brumer H","Coutinho PM","Henrissat B."],"DOI_URL":"http://dx.doi.org/10.1042/BJ20101185"},"PUB00083820":{"PMID":10907797,"ISBN":null,"volume":"35","issue":"3","year":2000,"title":"Structural and functional comparison of polysaccharide-degrading enzymes.","URL":null,"raw_pages":"221-51","medline_journal":"Crit Rev Biochem Mol Biol","ISO_journal":"Crit. Rev. Biochem. Mol. Biol.","authors":["Jedrzejas MJ."],"DOI_URL":"http://dx.doi.org/10.1080/10409230091169195"},"PUB00027701":{"PMID":15135077,"ISBN":null,"volume":"565","issue":"1-3","year":2004,"title":"Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4.","URL":null,"raw_pages":"188-94","medline_journal":"FEBS Lett","ISO_journal":"FEBS Lett.","authors":["McDonough MA","Kadirvelraj R","Harris P","Poulsen JC","Larsen S."],"DOI_URL":"http://dx.doi.org/10.1016/j.febslet.2004.03.094"}},"set_info":{"accession":"cl15687","name":"RGL4_C"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":0,"interactions":0,"matches":6164,"pathways":0,"proteins":6020,"proteomes":1443,"sets":1,"structural_models":{"alphafold":4979,"bfvd":0},"structures":4,"taxa":3260},"entry_annotations":{},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}