{"metadata":{"accession":"PF03976","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR022488","hierarchy":null,"name":{"name":"Polyphosphate kinase 2 (PPK2)","short":"PPK2"},"description":[{"text":"<p>Inorganic polyphosphate (polyP) plays a role in metabolism and regulation and has been proposed to serve as a energy source in a pre-ATP world.  In prokaryotes, the synthesis and utilisation of polyP are catalysed by PPK1, PPK2 and polyphosphatases. Proteins with a single PPK2 domain catalyse polyP-dependent phosphorylation of ADP to ATP, whereas proteins containing 2 fused PPK2 domains phosphorylate AMP to ADP. The structure of PPK2 from Pseudomonas aeruginosa has revealed a a 3-layer alpha/beta/alpha sandwich fold with an alpha-helical lid similar to the structures of microbial thymidylate kinases [[cite:PUB00051190]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00020169":{"PMID":12486232,"ISBN":null,"volume":"99","issue":"26","year":2002,"title":"A polyphosphate kinase (PPK2) widely conserved in bacteria.","URL":null,"raw_pages":"16678-83","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc. Natl. Acad. Sci. U.S.A.","authors":["Zhang H","Ishige K","Kornberg A."],"DOI_URL":"http://dx.doi.org/10.1073/pnas.262655199"},"PUB00051190":{"PMID":19001261,"ISBN":null,"volume":"105","issue":"46","year":2008,"title":"Polyphosphate-dependent synthesis of ATP and ADP by the family-2 polyphosphate kinases in bacteria.","URL":null,"raw_pages":"17730-5","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc. Natl. Acad. Sci. U.S.A.","authors":["Nocek B","Kochinyan S","Proudfoot M","Brown G","Evdokimova E","Osipiuk J","Edwards AM","Savchenko A","Joachimiak A","Yakunin AF."],"DOI_URL":"http://dx.doi.org/10.1073/pnas.0807563105"},"PUB00020170":{"PMID":12482933,"ISBN":null,"volume":"99","issue":"26","year":2002,"title":"Polyphosphate kinase (PPK2), a potent, polyphosphate-driven generator of GTP.","URL":null,"raw_pages":"16684-8","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc. Natl. Acad. Sci. U.S.A.","authors":["Ishige K","Zhang H","Kornberg A."],"DOI_URL":"http://dx.doi.org/10.1073/pnas.262655299"}},"set_info":{"accession":"CL0023","name":"P-loop_NTPase"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":19,"interactions":0,"matches":20776,"pathways":0,"proteins":18956,"proteomes":12086,"sets":1,"structural_models":{"alphafold":12011},"structures":33,"taxa":16643},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":8,"alignment:full":10316},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"3czp","name":"Crystal structure of putative polyphosphate kinase 2 from Pseudomonas aeruginosa PA01"}}}