This entry represents a domain centrally found in Phosphomevalonate dehydratase small subunit from Aeropyrum pernix (PMDh-S) and similar prokaryotic proteins previously annotated as aconitase X subunit 2, the swiveling domain subunit [[cite:PUB00080857]]. PMDh-S is a component of a hydro-lyase that catalyses the dehydration of mevalonate 5-phosphate (MVA5P) to form trans- anhydromevalonate 5-phosphate (tAHMP) [[cite:PUB00098043],[cite:PUB00154971]]. It is involved in the archaea; mevalonate (MVA) pathway, which provides fundamental precursos for isoprenoid biosynthesis such as isopentenyl diphosphate (IPP) and dimenthylallyl diphosphate (DMAPP) [[cite:PUB00098043],[cite:PUB00154970]]. This domain is also found at the N-terminal end of Cis-3-hydroxy-L-proline dehydratase from Agrobacterium fabrum (LhpI), which catalyses the dehydration of cis-3-hydroxy-L-proline (c3LHyp) to Delta1-pyrroline-2- carboxylate (Pyr2C) [[cite:PUB00088769]].
","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00154971":{"PMID":36992929,"ISBN":null,"volume":"14","issue":null,"year":2023,"title":"A [4Fe-4S] cluster resides at the active center of phosphomevalonate dehydratase, a key enzyme in the archaeal modified mevalonate pathway.","URL":null,"raw_pages":"1150353","medline_journal":"Front Microbiol","ISO_journal":"Front Microbiol","authors":["Komeyama M","Kanno K","Mino H","Yasuno Y","Shinada T","Ito T","Hemmi H."],"DOI_URL":"https://doi.org/10.3389/fmicb.2023.1150353"},"PUB00088769":{"PMID":27929065,"ISBN":null,"volume":"6","issue":null,"year":2016,"title":"Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase.","URL":null,"raw_pages":"38720","medline_journal":"Sci Rep","ISO_journal":"Sci Rep","authors":["Watanabe S","Tajima K","Fujii S","Fukumori F","Hara R","Fukuda R","Miyazaki M","Kino K","Watanabe Y."],"DOI_URL":"https://doi.org/10.1038/srep38720"},"PUB00080857":{"PMID":14568143,"ISBN":null,"volume":"227","issue":"1","year":2003,"title":"Filling a gap in the central metabolism of archaea: prediction of a novel aconitase by comparative-genomic analysis.","URL":null,"raw_pages":"17-23","medline_journal":"FEMS Microbiol Lett","ISO_journal":"FEMS Microbiol. Lett.","authors":["Makarova KS","Koonin EV."],"DOI_URL":"http://dx.doi.org/10.1016/S0378-1097(03)00596-2"},"PUB00154970":{"PMID":31924615,"ISBN":null,"volume":"86","issue":"6","year":2020,"title":"Reconstruction of the \"Archaeal\" Mevalonate Pathway from the Methanogenic Archaeon Methanosarcina mazei in Escherichia coli Cells.","URL":null,"raw_pages":"e02889-19","medline_journal":"Appl Environ Microbiol","ISO_journal":"Appl Environ Microbiol","authors":["Yoshida R","Yoshimura T","Hemmi H."],"DOI_URL":"https://doi.org/10.1128/AEM.02889-19"},"PUB00098043":{"PMID":30224495,"ISBN":null,"volume":"115","issue":"40","year":2018,"title":"Modified mevalonate pathway of the archaeon Aeropyrum pernix proceeds via trans-anhydromevalonate 5-phosphate.","URL":null,"raw_pages":"10034-10039","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc Natl Acad Sci U S A","authors":["Hayakawa H","Motoyama K","Sobue F","Ito T","Kawaide H","Yoshimura T","Hemmi H."],"DOI_URL":null}},"set_info":{"accession":"CL0364","name":"Leu-IlvD"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":22,"interactions":0,"matches":2019,"pathways":0,"proteins":2019,"proteomes":1838,"sets":1,"structural_models":{"alphafold":1449},"structures":6,"taxa":3213},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":63,"alignment:full":1114},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"7cns","name":"Crystal structure of Thermococcus kodakaraensis aconitase X (holo-form)"}}}