{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T13:21:27Z","timestamp":1786972887400,"version":"build-2736575974"},"reference-count":67,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2000,4,1]],"date-time":"2000-04-01T00:00:00Z","timestamp":954547200000},"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":["Appl Environ Microbiol"],"published-print":{"date-parts":[[2000,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Protocatechuate 3,4-dioxygenase (EC\n            <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"ec\" xlink:href=\"1.13.11.3\" xlink:type=\"simple\">1.13.11.3<\/jats:ext-link>\n            ) catalyzes the ring cleavage step in the catabolism of aromatic compounds through the protocatechuate branch of the \u03b2-ketoadipate pathway. A protocatechuate 3,4-dioxygenase was purified from\n            <jats:italic>Streptomyces<\/jats:italic>\n            sp. strain 2065 grown in\n            <jats:italic>p<\/jats:italic>\n            -hydroxybenzoate, and the N-terminal sequences of the \u03b2- and \u03b1-subunits were obtained. PCR amplification was used for the cloning of the corresponding genes, and DNA sequencing of the flanking regions showed that the\n            <jats:italic>pcaGH<\/jats:italic>\n            genes belonged to a 6.5-kb protocatechuate catabolic gene cluster; at least seven genes in the order\n            <jats:italic>pcaIJFHGBL<\/jats:italic>\n            appear to be transcribed unidirectionally. Analysis of the cluster revealed the presence of a\n            <jats:italic>pcaL<\/jats:italic>\n            homologue which encodes a fused \u03b3-carboxymuconolactone decarboxylase\/\u03b2-ketoadipate enol-lactone hydrolase previously identified in the\n            <jats:italic>pca<\/jats:italic>\n            gene cluster from\n            <jats:italic>Rhodococcus opacus<\/jats:italic>\n            1CP. The\n            <jats:italic>pcaIJ<\/jats:italic>\n            genes encoded proteins with a striking similarity to succinyl-coenzyme A (CoA):3-oxoacid CoA transferases of eukaryotes and contained an indel which is strikingly similar between high-G+C gram-positive bacteria and eukaryotes.\n          <\/jats:p>","DOI":"10.1128\/aem.66.4.1499-1508.2000","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T09:55:30Z","timestamp":1027763730000},"page":"1499-1508","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":91,"title":["Characterization of the Protocatechuic Acid Catabolic Gene Cluster from\n            <i>Streptomyces<\/i>\n            sp. 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