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Infection manifestations can range from simple, acute pharyngitis to more complex, necrotizing fasciitis. To date, most treatments for <jats:styled-content style=\"fixed-case\">GAS<\/jats:styled-content> infections involve the use of common antibiotics including tetracycline and clindamycin. Unfortunately, new strains have been identified that are resistant to these drugs, therefore, new targets must be identified to treat drug\u2010resistant strains. This work is focused on the structural and functional characterization of three proteins: spNadC, spNadD, and spNadE. These enzymes are involved in the biosynthesis of nicotinamide adenine dinucleotide (<jats:styled-content style=\"fixed-case\">NAD<\/jats:styled-content><jats:sup>+<\/jats:sup>). The structures of spNadC and spNadE were determined. SpNadC is suggested to play a role in <jats:styled-content style=\"fixed-case\">GAS<\/jats:styled-content> virulence, while spNadE, functions as an <jats:styled-content style=\"fixed-case\">NAD<\/jats:styled-content> synthetase and is considered to be a new drug target. Determination of the spNadE structure uncovered a putative, <jats:styled-content style=\"fixed-case\">NH<\/jats:styled-content><jats:sub>3<\/jats:sub> channel, which may provide insight into the mechanistic details of <jats:styled-content style=\"fixed-case\">NH<\/jats:styled-content><jats:sub>3<\/jats:sub>\u2010dependent <jats:styled-content style=\"fixed-case\">NAD<\/jats:styled-content><jats:sup>+<\/jats:sup> synthetases in prokaryotes.<\/jats:p><\/jats:sec><jats:sec><jats:title>Enzymes<\/jats:title><jats:p>Quinolinate phosphoribosyltransferase: <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.chem.qmul.ac.uk\/iubmb\/enzyme\/EC2\/4\/2\/19.html\">EC2.4.2.19<\/jats:ext-link> and <jats:styled-content style=\"fixed-case\">NAD<\/jats:styled-content> synthetase: <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.chem.qmul.ac.uk\/iubmb\/enzyme\/EC6\/3\/1\/5.html\">EC6.3.1.5<\/jats:ext-link>.<\/jats:p><\/jats:sec><jats:sec><jats:title>Database<\/jats:title><jats:p>Protein structures for spNadC, spNadC<jats:sub>\u039469A<\/jats:sub>, and spNadE are deposited into Protein Data Bank under the accession codes <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.rcsb.org\/pdb\/search\/structidSearch.do?structureId=5HUL\">5HUL<\/jats:ext-link>, <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.rcsb.org\/pdb\/search\/structidSearch.do?structureId=5HUO\">5HUO<\/jats:ext-link> &amp; <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.rcsb.org\/pdb\/search\/structidSearch.do?structureId=5HUP\">5HUP<\/jats:ext-link>, and <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.rcsb.org\/pdb\/search\/structidSearch.do?structureId=5HUH\">5HUH<\/jats:ext-link> &amp; <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.rcsb.org\/pdb\/search\/structidSearch.do?structureId=5HUJ\">5HUJ<\/jats:ext-link>, respectively.<\/jats:p><\/jats:sec>","DOI":"10.1111\/febs.14136","type":"journal-article","created":{"date-parts":[[2017,6,15]],"date-time":"2017-06-15T22:26:10Z","timestamp":1497565570000},"page":"2425-2441","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["<i>Streptococcus pyogenes<\/i> quinolinate\u2010salvage pathway\u2014structural and functional studies of quinolinate phosphoribosyl transferase and NH<sub>3<\/sub>\u2010dependent NAD<sup>+<\/sup> synthetase"],"prefix":"10.1111","volume":"284","author":[{"given":"William T.","family":"Booth","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry 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