{"metadata":{"accession":"IPR056301","entry_id":null,"type":"domain","go_terms":null,"source_database":"interpro","member_databases":{"pfam":{"PF23166":"Alpha-glucan water dikinase 1 Ig-like N-terminal domain"}},"integrated":null,"hierarchy":{"accession":"IPR056301","name":"Alpha-glucan water dikinase-like, N-terminal Ig-like domain","type":"Domain","children":[]},"name":{"name":"Alpha-glucan water dikinase-like, N-terminal Ig-like domain","short":"GWD-like_N_Ig"},"description":[{"text":"

This domain is found twice in the N-terminal region of alpha-glucan water dikinases (GWD) from plants including alpha-glucan water dikinase 1 (GWD1) from Arabidopsis thaliana and related plant proteins such as alpha-amylase 3 (AMY3).

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GWD1 is involved in the incorporation of phosphate into starch-like alpha-glucan, with preferred C-6 position of glucose units. It acts as an overall regulator of starch mobilization and it is required for starch degradation [[cite:PUB00153995]]. AMY3 is involved in the determination of the final structure of glucans by shortening long linear phospho-oligosaccharides in the chloroplast stroma. This enzyme can function on both soluble and insoluble glucan substrates to release small linear and branched malto-oligosaccharides [[cite:PUB00155673]].

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The domain represented by this entry is predicted to adopt a globular structure with an Ig-like topology. This domain is distantly related to CBM98 carbohydrate-binding family and is found associated with [interpro:IPR055495] in many members of this group.

","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00153995":{"PMID":11487701,"ISBN":null,"volume":"13","issue":"8","year":2001,"title":"The Arabidopsis sex1 mutant is defective in the R1 protein, a general regulator of starch degradation in plants, and not in the chloroplast hexose transporter.","URL":null,"raw_pages":"1907-18","medline_journal":"Plant Cell","ISO_journal":"Plant Cell","authors":["Yu TS","Kofler H","Hausler RE","Hille D","Flugge UI","Zeeman SC","Smith AM","Kossmann J","Lloyd J","Ritte G","Steup M","Lue WL","Chen J","Weber A."],"DOI_URL":"https://doi.org/10.1105/tpc.010091"},"PUB00155673":{"PMID":24089528,"ISBN":null,"volume":"288","issue":"47","year":2013,"title":"Arabidopsis thaliana AMY3 is a unique redox-regulated chloroplastic α-amylase.","URL":null,"raw_pages":"33620-33633","medline_journal":"J Biol Chem","ISO_journal":"J Biol Chem","authors":["Seung D","Thalmann M","Sparla F","Abou Hachem M","Lee SK","Issakidis-Bourguet E","Svensson B","Zeeman SC","Santelia D."],"DOI_URL":"https://doi.org/10.1074/jbc.M113.514794"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":114,"interactions":0,"matches":4161,"pathways":1,"proteins":2318,"proteomes":442,"sets":0,"structural_models":{"alphafold":1163,"bfvd":0},"structures":0,"taxa":1398},"entry_annotations":{"alignment:seed":157,"alignment:full":2292},"cross_references":{"ec":{"displayName":"ENZYME","description":"ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.","rank":19,"accessions":[{"accession":"2.7.9.4","url":"https://enzyme.expasy.org/EC/2.7.9.4"}]}},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}