{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,12]],"date-time":"2026-11-12T18:23:47Z","timestamp":1794507827347,"version":"4.9.1"},"reference-count":64,"publisher":"American Society for Microbiology","issue":"19","license":[{"start":{"date-parts":[[2001,10,1]],"date-time":"2001-10-01T00:00:00Z","timestamp":1001894400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2001,10]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    The complete 108,845-nucleotide sequence of catabolic plasmid pADP-1 from\n                    <jats:italic>Pseudomonas<\/jats:italic>\n                    sp. strain ADP was determined. Plasmid pADP-1 was previously shown to encode AtzA, AtzB, and AtzC, which catalyze the sequential hydrolytic removal of\n                    <jats:italic>s<\/jats:italic>\n                    -triazine ring substituents from the herbicide atrazine to yield cyanuric acid. Computational analyses indicated that pADP-1 encodes 104 putative open reading frames (ORFs), which are predicted to function in catabolism, transposition, and plasmid maintenance, transfer, and replication. Regions encoding transfer and replication functions of pADP-1 had 80 to 100% amino acid sequence identity to pR751, an IncP\u03b2 plasmid previously isolated from\n                    <jats:italic>Enterobacter aerogenes<\/jats:italic>\n                    . pADP-1 was shown to contain a functional mercury resistance operon with 99% identity to Tn\n                    <jats:italic>5053<\/jats:italic>\n                    . Complete copies of transposases with 99% amino acid sequence identity to TnpA from IS\n                    <jats:italic>1071<\/jats:italic>\n                    and TnpA from\n                    <jats:italic>Pseudomonas pseudoalcaligenes<\/jats:italic>\n                    were identified and flank each of the\n                    <jats:italic>atzA, atzB,<\/jats:italic>\n                    and\n                    <jats:italic>atzC<\/jats:italic>\n                    genes, forming structures resembling nested catabolic transposons. Functional analyses identified three new catabolic genes,\n                    <jats:italic>atzD<\/jats:italic>\n                    ,\n                    <jats:italic>atzE<\/jats:italic>\n                    , and\n                    <jats:italic>atzF,<\/jats:italic>\n                    which participate in atrazine catabolism. Crude extracts from\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    expressing AtzD hydrolyzed cyanuric acid to biuret. AtzD showed 58% amino acid sequence identity to TrzD, a cyanuric acid amidohydrolase, from\n                    <jats:italic>Pseudomonas<\/jats:italic>\n                    sp. strain NRRLB-12227. Two other genes encoding the further catabolism of cyanuric acid,\n                    <jats:italic>atzE<\/jats:italic>\n                    and\n                    <jats:italic>atzF<\/jats:italic>\n                    , reside in a contiguous cluster adjacent to a potential LysR-type transcriptional regulator.\n                    <jats:italic>E. coli<\/jats:italic>\n                    strains bearing\n                    <jats:italic>atzE<\/jats:italic>\n                    and\n                    <jats:italic>atzF<\/jats:italic>\n                    were shown to encode a biuret hydrolase and allophanate hydrolase, respectively.\n                    <jats:italic>atzDEF<\/jats:italic>\n                    are cotranscribed. AtzE and AtzF are members of a common amidase protein family. These data reveal the complete structure of a catabolic plasmid and show that the atrazine catabolic genes are dispersed on three disparate regions of the plasmid. These results begin to provide insight into how plasmids are structured, and thus evolve, to encode the catabolism of compounds recently added to the biosphere.\n                  <\/jats:p>","DOI":"10.1128\/jb.183.19.5684-5697.2001","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T05:58:18Z","timestamp":1027749498000},"page":"5684-5697","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":307,"title":["Complete Nucleotide Sequence and Organization of the Atrazine Catabolic Plasmid pADP-1 from\n                    <i>Pseudomonas<\/i>\n                    sp\n                    <i>.<\/i>\n                    Strain ADP"],"prefix":"10.1128","volume":"183","author":[{"given":"Betsy","family":"Martinez","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Department of Biochemistry, Molecular Biology and Biophysics,1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeffrey","family":"Tomkins","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Clemson University Genomics Institute, Clemson, South Carolina 296342"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lawrence P.","family":"Wackett","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Department of Biochemistry, Molecular Biology and Biophysics,1"},{"name":"<!--label omitted: 3-->Biological Process Technology Institute,3"},{"name":"<!--label omitted: 4-->Center for Microbial and Plant Genomics,4 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rod","family":"Wing","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Clemson University Genomics Institute, Clemson, South Carolina 296342"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael J.","family":"Sadowsky","sequence":"additional","affiliation":[{"name":"<!--label omitted: 3-->Biological Process Technology Institute,3"},{"name":"<!--label omitted: 4-->Center for Microbial and Plant Genomics,4 and"},{"name":"<!--label omitted: 5-->Department of Soil, Water &amp; Climate,5University of Minnesota, St. Paul, Minnesota 55108, and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.177.8.2008-2013.1995"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"1259","DOI":"10.1093\/protein\/8.12.1259","article-title":"Residues important for the function of a multihelical DNA binding domain in the new transcription factor family of Cam and Tet repressors","volume":"8","author":"Aramaki H.","year":"1995","unstructured":"Aramaki H. 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