{"metadata":{"accession":"PF14793","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR027820","hierarchy":null,"name":{"name":"Pyrimidine/purine nucleotide 5'-monophosphate nucleosidases","short":"DUF4478"},"description":[{"text":"<p>This is an N-terminal domain found in pyrimidine/purine nucleotide 5'-monophosphate nucleosidases (PpnN) in bacteria. PpnN catalyzes the hydrolysis of the N-glycosidic bond of diverse pyrimidine and purine nucleotide 5'-monophosphates, to form ribose 5-phosphate and the corresponding free base. It can use AMP, GMP, IMP, CMP, dTMP and UMP as substrates [[cite:PUB00084997]]. It is found in association with [pfam:PF03641] and [pfam:PF11892].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00084997":{"PMID":27941785,"ISBN":null,"volume":"14","issue":"2","year":2017,"title":"Nontargeted in vitro metabolomics for high-throughput identification of novel enzymes in Escherichia coli.","URL":null,"raw_pages":"187-194","medline_journal":"Nat Methods","ISO_journal":"Nat. Methods","authors":["Sevin DC","Fuhrer T","Zamboni N","Sauer U."],"DOI_URL":"https://doi.org/10.1038/nmeth.4103"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":5,"interactions":0,"matches":2624,"pathways":0,"proteins":2624,"proteomes":2618,"sets":0,"structural_models":{"alphafold":1594},"structures":9,"taxa":3448},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":30,"alignment:full":881},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}