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These enzymes acetylate the antibiotic chloramphenicol, which renders it incapable of inhibiting bacterial protein synthesis. CATs can be classified into different types: Type A CATs are known to be important for antibiotic resistance to chloramphenicol and fusidic acid. Type B CATs are often called xenobiotic acetyltransferases and adopt a similar structural fold to streptogramin acetyltransferases, which are known to be critical for streptogramin antibiotic resistance. Type C CATs have recently been identified and can also acetylate chloramphenicol, but their roles in antibiotic resistance are largely unknown. Here, we structurally and kinetically characterized three\n                    <jats:italic>Vibrio<\/jats:italic>\n                    CAT proteins from a nonpathogenic species (\n                    <jats:italic>Aliivibrio fisheri<\/jats:italic>\n                    ) and two important human pathogens (\n                    <jats:italic>Vibrio cholerae<\/jats:italic>\n                    and\n                    <jats:italic>Vibrio vulnificus<\/jats:italic>\n                    ). We found all three proteins, including one in a superintegron (\n                    <jats:italic>V. cholerae<\/jats:italic>\n                    ), acetylated chloramphenicol, but did not acetylate aminoglycosides or dalfopristin. We also determined the 3D crystal structures of these CATs alone and in complex with crystal violet and taurocholate. These compounds are known inhibitors of Type A CATs, but have not been explored in Type B and Type C CATs. Based on sequence, structure, and kinetic analysis, we concluded that the\n                    <jats:italic>V. cholerae<\/jats:italic>\n                    and\n                    <jats:italic>V. vulnificus<\/jats:italic>\n                    CATs belong to the Type B class and the\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>A. fisheri<\/jats:italic>\n                    <\/jats:styled-content>\n                    CAT belongs to the Type C class. Ultimately, our results provide a framework for studying the evolution of antibiotic resistance gene acquisition and chloramphenicol acetylation in\n                    <jats:italic>Vibrio<\/jats:italic>\n                    and other species.\n                  <\/jats:p>","DOI":"10.1002\/pro.3793","type":"journal-article","created":{"date-parts":[[2019,11,25]],"date-time":"2019-11-25T01:58:48Z","timestamp":1574647128000},"page":"695-710","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Structural and functional characterization of three Type B and C chloramphenicol acetyltransferases from\n                    <i>Vibrio<\/i>\n                    species"],"prefix":"10.1002","volume":"29","author":[{"given":"Ashley","family":"Alcala","sequence":"first","affiliation":[{"name":"San Francisco State University Department of Chemistry and Biochemistry  San Francisco California"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guadalupe","family":"Ramirez","sequence":"additional","affiliation":[{"name":"San Francisco State University Department of Chemistry and Biochemistry  San Francisco California"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Allan","family":"Solis","sequence":"additional","affiliation":[{"name":"San Francisco State University Department of Chemistry and Biochemistry  San Francisco California"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Youngchang","family":"Kim","sequence":"additional","affiliation":[{"name":"Center for Structural Genomics of Infectious Diseases, Consortium for Advanced Science and Engineering University of Chicago  Chicago Illinois"},{"name":"Structural Biology Center X\u2010ray Science Division Argonne National Laboratory  Argonne 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