{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T15:56:04Z","timestamp":1790870164324,"version":"4.1.0"},"reference-count":76,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,8,25]],"date-time":"2026-08-25T00:00:00Z","timestamp":1787616000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R 35GM133506"],"award-info":[{"award-number":["R 35GM133506"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["BB\/X00306X\/1"],"award-info":[{"award-number":["BB\/X00306X\/1"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Structure"],"published-print":{"date-parts":[[2026,10]]},"DOI":"10.1016\/j.str.2026.07.015","type":"journal-article","created":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T14:44:55Z","timestamp":1787582695000},"page":"1347-1362.e6","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Structural plasticity drives convergent evolution and functional diversification of GNAT polyamine acetyltransferases"],"prefix":"10.1016","volume":"34","author":[{"given":"Joel","family":"Roca-Martinez","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hazel N.","family":"Leiva Martel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jialin","family":"Yin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huy Duc","family":"Do","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Van Thi Bich","family":"Le","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicola","family":"Bordin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Clemens","family":"Rauer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christine","family":"Orengo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7951-9141","authenticated-orcid":false,"given":"Misty L.","family":"Kuhn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.str.2026.07.015_bib1","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1186\/s13059-019-1835-8","article-title":"The CAFA challenge reports improved protein function prediction and new functional annotations for hundreds of genes through experimental screens","volume":"20","author":"Zhou","year":"2019","journal-title":"Genome Biol."},{"key":"10.1016\/j.str.2026.07.015_bib2","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1186\/s13059-016-1037-6","article-title":"An expanded evaluation of protein function prediction methods shows an improvement in accuracy","volume":"17","author":"Jiang","year":"2016","journal-title":"Genome Biol."},{"key":"10.1016\/j.str.2026.07.015_bib3","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.sbi.2021.05.012","article-title":"Computational approaches to predict protein functional families and functional sites","volume":"70","author":"Rauer","year":"2021","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.str.2026.07.015_bib4","doi-asserted-by":"crossref","first-page":"D490","DOI":"10.1093\/nar\/gks1211","article-title":"New functional families (FunFams) in CATH to improve the mapping of conserved functional sites to 3D structures","volume":"41","author":"Sillitoe","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.str.2026.07.015_bib5","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1186\/s12859-019-2988-x","article-title":"FunFam protein families improve residue level molecular function prediction","volume":"20","author":"Scheibenreif","year":"2019","journal-title":"BMC Bioinf."},{"key":"10.1016\/j.str.2026.07.015_bib6","doi-asserted-by":"crossref","first-page":"e00090-19","DOI":"10.1128\/MMBR.00090-19","article-title":"Small-Molecule Acetylation by GCN5-Related N-Acetyltransferases in Bacteria","volume":"84","author":"Burckhardt","year":"2020","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.str.2026.07.015_bib7","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1128\/MMBR.00020-15","article-title":"Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress","volume":"79","author":"Hentchel","year":"2015","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.str.2026.07.015_bib8","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/j.abb.2004.09.003","article-title":"Structure and functions of the GNAT superfamily of acetyltransferases","volume":"433","author":"Vetting","year":"2005","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.str.2026.07.015_bib9","doi-asserted-by":"crossref","DOI":"10.1128\/mbio.03221-23","article-title":"An acetyltransferase effector conserved across Legionella species targets the eukaryotic eIF3 complex to modulate protein translation","volume":"15","author":"Syriste","year":"2024","journal-title":"mBio"},{"key":"10.1016\/j.str.2026.07.015_bib10","doi-asserted-by":"crossref","first-page":"16328","DOI":"10.1074\/jbc.M009988200","article-title":"The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase","volume":"276","author":"Peneff","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2026.07.015_bib11","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1110\/ps.0233503","article-title":"X-ray structure of the AAC(6\u2019)-Ii antibiotic resistance enzyme at 1.8 A resolution; examination of oligomeric arrangements in GNAT superfamily members","volume":"12","author":"Burk","year":"2003","journal-title":"Protein Sci."},{"key":"10.1016\/j.str.2026.07.015_bib12","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2419096122","article-title":"Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ","volume":"122","author":"Park","year":"2025","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.str.2026.07.015_bib13","doi-asserted-by":"crossref","first-page":"1316","DOI":"10.1016\/j.jmb.2015.01.009","article-title":"A novel polyamine allosteric site of SpeG from Vibrio cholerae is revealed by its dodecameric structure","volume":"427","author":"Filippova","year":"2015","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.str.2026.07.015_bib14","doi-asserted-by":"crossref","first-page":"7187","DOI":"10.1021\/bi700256z","article-title":"Mechanistic And Structural Analysis of Human Spermidine\/spermine N1-Acetyltransferase [hSSAT]","volume":"46","author":"Hegde","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.str.2026.07.015_bib15","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1021\/acsinfecdis.6b00058","article-title":"Structural and Biochemical Characterization of Acinetobacter spp. Aminoglycoside Acetyltransferases Highlights Functional and Evolutionary Variation among Antibiotic Resistance Enzymes","volume":"3","author":"Stogios","year":"2017","journal-title":"ACS Infect. Dis."},{"key":"10.1016\/j.str.2026.07.015_bib16","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1016\/S0969-2126(97)00260-8","article-title":"CATH--a hierarchic classification of protein domain structures","volume":"5","author":"Orengo","year":"1997","journal-title":"Structure"},{"key":"10.1016\/j.str.2026.07.015_bib17","doi-asserted-by":"crossref","DOI":"10.1002\/pro.5140","article-title":"Clustering protein functional families at large scale with hierarchical approaches","volume":"33","author":"Bordin","year":"2024","journal-title":"Protein Sci."},{"key":"10.1016\/j.str.2026.07.015_bib18","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1093\/nar\/gkp1049","article-title":"GeMMA: functional subfamily classification within superfamilies of predicted protein structural domains","volume":"38","author":"Lee","year":"2010","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.str.2026.07.015_bib19","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1007988","article-title":"Classification and phylogeny for the annotation of novel eukaryotic GNAT acetyltransferases","volume":"16","author":"Krtenic","year":"2020","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.str.2026.07.015_bib20","doi-asserted-by":"crossref","first-page":"18693","DOI":"10.1074\/jbc.TM118.005670","article-title":"Polyamine function in archaea and bacteria","volume":"293","author":"Michael","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2026.07.015_bib21","doi-asserted-by":"crossref","first-page":"14896","DOI":"10.1074\/jbc.R116.734780","article-title":"Polyamines in Eukaryotes, Bacteria, and Archaea","volume":"291","author":"Michael","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2026.07.015_bib22","doi-asserted-by":"crossref","first-page":"8736","DOI":"10.1074\/jbc.RA120.013833","article-title":"Polyamines regulate gene expression by stimulating translation of histone acetyltransferase mRNAs","volume":"295","author":"Sakamoto","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2026.07.015_bib23","doi-asserted-by":"crossref","first-page":"5622","DOI":"10.1093\/emboj\/18.20.5622","article-title":"Functional interaction between GCN5 and polyamines: a new role for core histone acetylation","volume":"18","author":"Pollard","year":"1999","journal-title":"EMBO J."},{"key":"10.1016\/j.str.2026.07.015_bib24","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1111\/j.1574-6968.2009.01744.x","article-title":"Spermidine regulates Vibrio cholerae biofilm formation via transport and signaling pathways","volume":"299","author":"McGinnis","year":"2009","journal-title":"FEMS Microbiol. Lett."},{"key":"10.1016\/j.str.2026.07.015_bib25","doi-asserted-by":"crossref","first-page":"1715","DOI":"10.1007\/s10529-013-1286-3","article-title":"A wider role for polyamines in biofilm formation","volume":"35","author":"Karatan","year":"2013","journal-title":"Biotechnol. Lett."},{"key":"10.1016\/j.str.2026.07.015_bib26","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1111\/j.1582-4934.2007.00077.x","article-title":"Physiological polyamines: simple primordial stress molecules","volume":"11","author":"Rhee","year":"2007","journal-title":"J. Cell Mol. Med."},{"key":"10.1016\/j.str.2026.07.015_bib27","article-title":"Functional polyamine metabolic enzymes and pathways encoded by the virosphere","volume":"120","author":"Li","year":"2023","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.str.2026.07.015_bib28","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.semcdb.2022.12.004","article-title":"Good cop, bad cop: Polyamines play both sides in host immunity and viral replication","volume":"146","author":"Cruz-Pulido","year":"2023","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.str.2026.07.015_bib29","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.str.2026.07.015_bib30","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","article-title":"Accurate structure prediction of biomolecular interactions with AlphaFold 3","volume":"630","author":"Abramson","year":"2024","journal-title":"Nature"},{"key":"10.1016\/j.str.2026.07.015_bib31","doi-asserted-by":"crossref","first-page":"W29","DOI":"10.1093\/nar\/gkr367","article-title":"HMMER web server: interactive sequence similarity searching","volume":"39","author":"Finn","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.str.2026.07.015_bib32","doi-asserted-by":"crossref","first-page":"2302","DOI":"10.1093\/nar\/gki524","article-title":"TM-align: a protein structure alignment algorithm based on the TM-score","volume":"33","author":"Zhang","year":"2005","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.str.2026.07.015_bib33","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1038\/s41587-023-01773-0","article-title":"Fast and accurate protein structure search with Foldseek","volume":"42","author":"van Kempen","year":"2024","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.str.2026.07.015_bib34","doi-asserted-by":"crossref","DOI":"10.1016\/j.jsb.2020.107506","article-title":"SpeG polyamine acetyltransferase enzyme from Bacillus thuringiensis forms a dodecameric structure and exhibits high catalytic efficiency","volume":"210","author":"Tsimbalyuk","year":"2020","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.str.2026.07.015_bib35","doi-asserted-by":"crossref","first-page":"49887","DOI":"10.1021\/acsomega.4c08743","article-title":"A Structurally Diverse Compound Screening Library to Identify Substrates for Diamine, Polyamine, and Related Acetyltransferases","volume":"9","author":"Leiva","year":"2024","journal-title":"ACS Omega"},{"key":"10.1016\/j.str.2026.07.015_bib36","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbrc.2025.151302","article-title":"N-terminal domain swapping: A new paradigm for spermidine\/spermine N-acetyltransferase (SSAT) protein structures?","volume":"748","author":"Mayer-Harnisch","year":"2025","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.str.2026.07.015_bib37","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.str.2020.12.004","article-title":"Structural and functional characterization of the N-terminal acetyltransferase Naa50","volume":"29","author":"Weidenhausen","year":"2021","journal-title":"Structure"},{"key":"10.1016\/j.str.2026.07.015_bib38","first-page":"W380","article-title":"mTM-align: a server for fast protein structure database search and multiple protein structure alignment","volume":"46","author":"Dong","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.str.2026.07.015_bib39","doi-asserted-by":"crossref","first-page":"1530","DOI":"10.1093\/molbev\/msaa015","article-title":"IQ-TREE 2: New Models and Efficient Methods for Phylogenetic Inference in the Genomic Era","volume":"37","author":"Minh","year":"2020","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.str.2026.07.015_bib40","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1186\/s13321-015-0069-3","article-title":"Why is Tanimoto index an appropriate choice for fingerprint-based similarity calculations?","volume":"7","author":"Bajusz","year":"2015","journal-title":"J. Cheminf."},{"key":"10.1016\/j.str.2026.07.015_bib41","doi-asserted-by":"crossref","first-page":"30223","DOI":"10.1074\/jbc.M113.501353","article-title":"Structural, Functional, and Inhibition Studies of a Gcn5-related N-Acetyltransferase (GNAT) Superfamily Protein PA4794","volume":"288","author":"Majorek","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2026.07.015_bib42","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1146\/annurev.biophys.29.1.81","article-title":"GCN5-related N-acetyltransferases: a structural overview","volume":"29","author":"Dyda","year":"2000","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"10.1016\/j.str.2026.07.015_bib43","doi-asserted-by":"crossref","first-page":"36249","DOI":"10.1074\/jbc.M114.613901","article-title":"Insights into the Specificity of Lysine Acetyltransferases","volume":"289","author":"Tucker","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2026.07.015_bib44","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.bbapap.2016.10.011","article-title":"Insight into the 3D structure and substrate specificity of previously uncharacterized GNAT superfamily acetyltransferases from pathogenic bacteria","volume":"1865","author":"Majorek","year":"2017","journal-title":"Biochim. Biophys. Acta Proteins Proteom."},{"key":"10.1016\/j.str.2026.07.015_bib45","doi-asserted-by":"crossref","DOI":"10.1002\/pro.4725","article-title":"Mapping roles of active site residues in the acceptor site of the PA3944 Gcn5-related N-acetyltransferase enzyme","volume":"32","author":"Variot","year":"2023","journal-title":"Protein Sci."},{"key":"10.1016\/j.str.2026.07.015_bib46","doi-asserted-by":"crossref","first-page":"2063","DOI":"10.1073\/pnas.0511008103","article-title":"Structures of wild-type and mutant human spermidine\/spermine N1-acetyltransferase, a potential therapeutic drug target","volume":"103","author":"Bewley","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.str.2026.07.015_bib47","doi-asserted-by":"crossref","first-page":"9145","DOI":"10.1021\/bi8009357","article-title":"The crystal structure of spermidine\/spermine N1-acetyltransferase in complex with spermine provides insights into substrate binding and catalysis","volume":"47","author":"Montemayor","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.str.2026.07.015_bib48","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1042\/BCJ20260162","article-title":"Roles of acidic residues in SpeG acetyltransferases-insights into importance for kinetic activity and polyamine binding in allosteric and acceptor sites","volume":"483","author":"Leiva Martel","year":"2026","journal-title":"Biochem. J."},{"key":"10.1016\/j.str.2026.07.015_bib49","doi-asserted-by":"crossref","first-page":"2528","DOI":"10.1038\/s41467-023-38218-w","article-title":"N-Formimidoylation\/-iminoacetylation modification in aminoglycosides requires FAD-dependent and ligand-protein NOS bridge dual chemistry","volume":"14","author":"Wang","year":"2023","journal-title":"Nat. Commun."},{"key":"10.1016\/j.str.2026.07.015_bib50","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1111\/tpj.16148","article-title":"Biochemical and structural basis of polyamine, lysine and ornithine acetylation catalyzed by spermine\/spermidine N-acetyl transferase in moss and maize","volume":"114","author":"B\u011bl\u00ed\u010dek","year":"2023","journal-title":"Plant J."},{"key":"10.1016\/j.str.2026.07.015_bib51","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1038\/352172a0","article-title":"Convergent evolution of similar function in two structurally divergent enzymes","volume":"352","author":"Kuriyan","year":"1991","journal-title":"Nature"},{"key":"10.1016\/j.str.2026.07.015_bib52","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1006\/jmbi.1999.3059","article-title":"The Zn-peptidase superfamily: functional convergence after evolutionary divergence","volume":"292","author":"Makarova","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.str.2026.07.015_bib53","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.tig.2021.06.016","article-title":"Retention of duplicated genes in evolution","volume":"38","author":"Kuzmin","year":"2022","journal-title":"Trends Genet."},{"key":"10.1016\/j.str.2026.07.015_bib54","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1111\/evo.14434","article-title":"Glutamine synthetase evolutionary history revisited: Tracing back beyond the Last Universal Common Ancestor","volume":"76","author":"de Carvalho Fernandes","year":"2022","journal-title":"Evolution"},{"key":"10.1016\/j.str.2026.07.015_bib55","doi-asserted-by":"crossref","first-page":"2119","DOI":"10.1093\/molbev\/msn161","article-title":"Evolutionary diversification in polyamine biosynthesis","volume":"25","author":"Minguet","year":"2008","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.str.2026.07.015_bib56","doi-asserted-by":"crossref","first-page":"1815","DOI":"10.1099\/00221287-146-8-1815","article-title":"Phylogeny of related functions: the case of polyamine biosynthetic enzymes","volume":"146","author":"Sekowska","year":"2000","journal-title":"Microbiology (Read.)"},{"key":"10.1016\/j.str.2026.07.015_bib57","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.101219","article-title":"Discovery of ancestral L-ornithine and L-lysine decarboxylases reveals parallel, pseudoconvergent evolution of polyamine biosynthesis","volume":"297","author":"Li","year":"2021","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2026.07.015_bib58","doi-asserted-by":"crossref","first-page":"39224","DOI":"10.1074\/jbc.M110.163154","article-title":"Evolution and multiplicity of arginine decarboxylases in polyamine biosynthesis and essential role in Bacillus subtilis biofilm formation","volume":"285","author":"Burrell","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2026.07.015_bib59","doi-asserted-by":"crossref","first-page":"25708","DOI":"10.1074\/jbc.M110.121137","article-title":"Evolution of substrate specificity within a diverse family of beta\/alpha-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidine","volume":"285","author":"Deng","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2026.07.015_bib60","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2023.105005","article-title":"Neofunctionalization of S-adenosylmethionine decarboxylase into pyruvoyl-dependent L-ornithine and L-arginine decarboxylases is widespread in bacteria and archaea","volume":"299","author":"Li","year":"2023","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.str.2026.07.015_bib61","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1016\/S0959-440X(99)80051-7","article-title":"From protein structure to function","volume":"9","author":"Orengo","year":"1999","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.str.2026.07.015_bib62","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1006\/jmbi.1998.2043","article-title":"Supersites within superfolds. Binding site similarity in the absence of homology1","volume":"282","author":"Russell","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.str.2026.07.015_bib63","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1111\/febs.17332","article-title":"Paradigms of convergent evolution in enzymes","volume":"292","author":"Riziotis","year":"2025","journal-title":"FEBS J."},{"key":"10.1016\/j.str.2026.07.015_bib64","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1016\/j.jmb.2007.06.017","article-title":"Convergent Evolution of Enzyme Active Sites Is not a Rare Phenomenon","volume":"372","author":"Gherardini","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.str.2026.07.015_bib65","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1007569","article-title":"Functional analysis of Rossmann-like domains reveals convergent evolution of topology and reaction pathways","volume":"15","author":"Medvedev","year":"2019","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.str.2026.07.015_bib66","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/S1367-5931(02)00018-2","article-title":"Emergence of diverse biochemical activities in evolutionarily conserved structural scaffolds of proteins","volume":"7","author":"Anantharaman","year":"2003","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.str.2026.07.015_bib67","doi-asserted-by":"crossref","first-page":"D266","DOI":"10.1093\/nar\/gkaa1079","article-title":"CATH: increased structural coverage of functional space","volume":"49","author":"Sillitoe","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.str.2026.07.015_bib68","doi-asserted-by":"crossref","first-page":"W200","DOI":"10.1093\/nar\/gky448","article-title":"HMMER web server: 2018 update","volume":"46","author":"Potter","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.str.2026.07.015_bib69","doi-asserted-by":"crossref","first-page":"1719","DOI":"10.1093\/bioinformatics\/btx828","article-title":"mTM-align: an algorithm for fast and accurate multiple protein structure alignment","volume":"34","author":"Dong","year":"2018","journal-title":"Bioinformatics"},{"key":"10.1016\/j.str.2026.07.015_bib70","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1093\/molbev\/msu300","article-title":"IQ-TREE: A Fast and Effective Stochastic Algorithm for Estimating Maximum-Likelihood Phylogenies","volume":"32","author":"Nguyen","year":"2015","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.str.2026.07.015_bib71","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1038\/nmeth.4285","article-title":"ModelFinder: fast model selection for accurate phylogenetic estimates","volume":"14","author":"Kalyaanamoorthy","year":"2017","journal-title":"Nat. Methods"},{"key":"10.1016\/j.str.2026.07.015_bib72","doi-asserted-by":"crossref","first-page":"W78","DOI":"10.1093\/nar\/gkae268","article-title":"Interactive Tree of Life (iTOL) v6: recent updates to the phylogenetic tree display and annotation tool","volume":"52","author":"Letunic","year":"2024","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.str.2026.07.015_bib73","doi-asserted-by":"crossref","first-page":"1422","DOI":"10.1093\/bioinformatics\/btp163","article-title":"Biopython: freely available Python tools for computational molecular biology and bioinformatics","volume":"25","author":"Cock","year":"2009","journal-title":"Bioinformatics"},{"key":"10.1016\/j.str.2026.07.015_bib74","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1186\/s13059-019-1832-y","article-title":"OrthoFinder: phylogenetic orthology inference for comparative genomics","volume":"20","author":"Emms","year":"2019","journal-title":"Genome Biol."},{"key":"10.1016\/j.str.2026.07.015_bib75","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2021.645768","article-title":"The Vibrio cholerae SpeG Spermidine\/Spermine N-Acetyltransferase Allosteric Loop and \u03b26-\u03b27 Structural Elements Are Critical for Kinetic Activity","volume":"8","author":"Le","year":"2021","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.str.2026.07.015_bib76","doi-asserted-by":"crossref","DOI":"10.1093\/gbe\/evaf139","article-title":"Protein Structural Phylogenetics","volume":"17","author":"Puente-Lelievre","year":"2025","journal-title":"Genome Biol. Evol."}],"container-title":["Structure"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212626002467?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212626002467?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T15:10:56Z","timestamp":1790867456000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0969212626002467"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10]]},"references-count":76,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2026,10]]}},"alternative-id":["S0969212626002467"],"URL":"https:\/\/doi.org\/10.1016\/j.str.2026.07.015","relation":{},"ISSN":["0969-2126"],"issn-type":[{"value":"0969-2126","type":"print"}],"subject":[],"published":{"date-parts":[[2026,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural plasticity drives convergent evolution and functional diversification of GNAT polyamine acetyltransferases","name":"articletitle","label":"Article Title"},{"value":"Structure","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.str.2026.07.015","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Crown Copyright \u00a9 2026 Published by Elsevier Inc.","name":"copyright","label":"Copyright"}]}}