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Novel ATA can be identified in protein databases due to the extensive knowledge of sequence-function relationships. However, predicting thermo- and operational stability from the amino acid sequence is a persisting challenge and a vital step towards identifying efficient ATA biocatalysts for industrial applications. In this study, we performed a database mining and characterized selected putative enzymes of the \u03b2-alanine:pyruvate transaminase cluster (3N5M) \u2014 a subfamily with so far only a few described members, whose tetrameric structure was suggested to positively affect operational stability. Four putative transaminases (TA-1: <jats:italic>Bilophilia wadsworthia,<\/jats:italic> TA-5: <jats:italic>Halomonas elongata<\/jats:italic>, TA-9: <jats:italic>Burkholderia cepacia<\/jats:italic>, and TA-10: <jats:italic>Burkholderia multivorans<\/jats:italic>) were obtained in a soluble form as tetramers in <jats:italic>E. coli<\/jats:italic>. During comparison of these tetrameric with known dimeric transaminases we found that indeed novel ATA with high operational stabilities can be identified in this protein subfamily, but we also found exceptions to the hypothesized correlation that a tetrameric assembly leads to increased stability. The discovered ATA from <jats:italic>Burkholderia multivorans<\/jats:italic> features a broad substrate specificity, including isopropylamine acceptance, is highly active (6 U\/mg) in the conversion of 1-phenylethylamine with pyruvate and shows a thermostability of up to 70\u00a0\u00b0C under both, storage and operating conditions. In addition, 50% (v\/v) of isopropanol or DMSO can be employed as co-solvents without a destabilizing effect on the enzyme during an incubation time of 16\u00a0h at 30\u00a0\u00b0C.<\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Key points<\/jats:title>\n                <jats:p>\u2022 <jats:italic>Database mining identified a thermostable amine transaminase in the \u03b2-alanine:pyruvate transaminase\u00a0subfamily<\/jats:italic>.<\/jats:p>\n                <jats:p>\u2022 <jats:italic>The tetrameric transaminase tolerates 50% DMSO and isopropanol under operating conditions at 30\u00a0\u00b0C<\/jats:italic>.<\/jats:p>\n                <jats:p>\u2022 <jats:italic>A tetrameric structure is not necessarily associated with a higher operational stability<\/jats:italic><\/jats:p>\n              <\/jats:sec><jats:sec>\n                <jats:title>Graphical abstract<\/jats:title>\n                \n              <\/jats:sec>","DOI":"10.1007\/s00253-022-12071-1","type":"journal-article","created":{"date-parts":[[2022,8,6]],"date-time":"2022-08-06T10:02:32Z","timestamp":1659780152000},"page":"5563-5574","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Characterization of proteins from the 3N5M family reveals an operationally stable amine transaminase"],"prefix":"10.1007","volume":"106","author":[{"given":"Manideep","family":"Kollipara","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philipp","family":"Matzel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miriam","family":"Sowa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefan","family":"Brott","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0685-2696","authenticated-orcid":false,"given":"Uwe","family":"Bornscheuer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2542-725X","authenticated-orcid":false,"given":"Matthias","family":"H\u00f6hne","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2022,8,6]]},"reference":[{"key":"12071_CR1","doi-asserted-by":"publisher","first-page":"1134","DOI":"10.1039\/C6GC02769E","volume":"19","author":"D Baud","year":"2017","unstructured":"Baud D, Jeffries JWE, Moody TS, Ward JM, Hailes HC (2017) A metagenomics approach for new biocatalyst discovery: application to transaminases and the synthesis of allylic amines. 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