EC	1.14.14.181
Accepted name:	sulfoquinovose monooxygenase
Reaction:	6-sulfo-D-quinovose + FMNH2 + O2 = 6-dehydro-D-glucose + FMN + sulfite + H2O
Glossary:	D-quinovose = 6-deoxy-D-glucopyranose 6-dehydro-D-glucose = 6-oxo-D-quinovose
Other name(s):	6-deoxy-6-sulfo-D-glucose monooxygenase; smoC (gene name); squD (gene name)
Systematic name:	6-sulfo-D-quinovose,FMNH2:oxygen oxidoreductase
Comments:	The enzyme, characterized from the bacteria Agrobacterium fabrum and Rhizobium oryzae, is involved in a D-sulfoquinovose degradation pathway. FMNH2 is provided by an associated FMN reductase [SmoA, EC 1.5.1.42, FMN reductase (NADH)].
References:	1.  Liu, J., Wei, Y., Ma, K., An, J., Liu, X., Liu, Y., Ang, E.L., Zhao, H. and Zhang, Y. Mechanistically diverse pathways for sulfoquinovose degradation in bacteria. ACS Catal. 11 (2021) 14740–14750. 2.  Sharma, M., Lingford, J.P., Petricevic, M., Snow, A.J.D., Zhang, Y., Jarva, M.A., Mui, J.W., Scott, N.E., Saunders, E.C., Mao, R., Epa, R., da Silva, B.M., Pires, D.E.V., Ascher, D.B., McConville, M.J., Davies, G.J., Williams, S.J. and Goddard-Borger, E.D. Oxidative desulfurization pathway for complete catabolism of sulfoquinovose by bacteria. Proc. Natl. Acad. Sci. USA 119 (2022) e2116022119. [PMID: 35074914]
[EC 1.14.14.181 created 20022]
EC	2.2.1.14
Accepted name:	6-deoxy-6-sulfo-D-fructose transaldolase
Reaction:	6-deoxy-6-sulfo-D-fructose + D-glyceraldehyde 3-phosphate = (2S)-3-sulfolactaldehyde + β-D-fructofuranose 6-phosphate
Glossary:	(2S)-3-sulfolactaldehyde = (2S)-2-hydroxy-3-oxopropane-1-sulfonate
Other name(s):	sftT (gene name)
Systematic name:	6-deoxy-6-sulfo-D-fructose:D-glyceraldehyde-3-phosphate glyceronetransferase
Comments:	The enzyme, characterized from the bacterium Bacillus aryabhattai SOS1, is involved in a degradation pathway for 6-sulfo-D-quinovose. The enzyme can also use D-erythrose 4-phosphate as the acceptor, forming D-sedoheptulose 7-phosphate.
References:	1.  Frommeyer, B., Fiedler, A.W., Oehler, S.R., Hanson, B.T., Loy, A., Franchini, P., Spiteller, D. and Schleheck, D. Environmental and intestinal phylum Firmicutes bacteria metabolize the plant sugar sulfoquinovose via a 6-deoxy-6-sulfofructose transaldolase pathway. iScience 23:101510 (2020). [PMID: 32919372]
[EC 2.2.1.14 created 2021]
EC	3.2.1.199
Accepted name:	sulfoquinovosidase
Reaction:	a 6-sulfo-α-D-quinovosyl diacylglycerol + H2O = 6-sulfo-α-D-quinovose + a 1,2-diacylglycerol
Glossary:	quinovose = 6-deoxy-D-glucopyranose
Other name(s):	yihQ (gene name); 6-sulfo-α-D-quinovosyl diacylglycerol 6-sulfo-D-quinovohydrolase
Systematic name:	6-sulfo-α-D-quinovosyl diacylglycerol 6-sulfo-D-quinovohydrolase (configuration-retaining)
Comments:	The enzyme, characterized from the bacteria Escherichia coli and Pseudomonas putida, hydrolyses terminal non-reducing α-sulfoquinovoside residues in α-sulfoquinovosyl diacylglycerides and α-sulfoquinovosyl glycerol using a retaining mechanism. The enzyme belongs to the glycosyl hydrolase GH31 family.
References:	1.  Shibuya, I. and Benson, A. A. Hydrolysis of α-sulphoquinovosides by β-galactosidase. Nature 192 (1961) 1186–1187. 2.  Speciale, G., Jin, Y., Davies, G.J., Williams, S.J. and Goddard-Borger, E.D. YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids. Nat. Chem. Biol. 12 (2016) 215–217. [PMID: 26878550]
[EC 3.2.1.199 created 2016]
EC	4.3.1.30
Accepted name:	dTDP-4-amino-4,6-dideoxy-D-glucose ammonia-lyase
Reaction:	dTDP-4-amino-4,6-dideoxy-α-D-glucopyranose + S-adenosyl-L-methionine + reduced acceptor = dTDP-3-dehydro-4,6-dideoxy-α-D-glucopyranose + NH3 + L-methionine + 5′-deoxyadenosine + acceptor
Other name(s):	desII (gene name); eryCV (gene name); MegCV
Systematic name:	dTDP-4-amino-4,6-dideoxy-α-D-glucopyranose ammonia lyase (dTDP-3-dehydro-4,6-dideoxy-α-D-glucopyranose-forming)
Comments:	The enzyme, which is a member of the ’AdoMet radical’ (radical SAM) family, is involved in biosynthesis of TDP-α-D-desosamine. The reaction starts by the transfer of an electron from the reduced form of the enzyme’s [4Fe-4S] cluster to S-adenosyl-L-methionine, spliting it into methionine and the radical 5-deoxyadenosin-5′-yl, which attacks the sugar substrate.
References:	1.  Szu, P.H., Ruszczycky, M.W., Choi, S.H., Yan, F. and Liu, H.W. Characterization and mechanistic studies of DesII: a radical S-adenosyl-L-methionine enzyme involved in the biosynthesis of TDP-D-desosamine. J. Am. Chem. Soc. 131 (2009) 14030–14042. [PMID: 19746907] 2.  Ruszczycky, M.W., Choi, S.H. and Liu, H.W. Stoichiometry of the redox neutral deamination and oxidative dehydrogenation reactions catalyzed by the radical SAM enzyme DesII. J. Am. Chem. Soc. 132 (2010) 2359–2369. [PMID: 20121093] 3.  Ruszczycky, M.W., Choi, S.H., Mansoorabadi, S.O. and Liu, H.W. Mechanistic studies of the radical S-adenosyl-L-methionine enzyme DesII: EPR characterization of a radical intermediate generated during its catalyzed dehydrogenation of TDP-D-quinovose. J. Am. Chem. Soc. 133 (2011) 7292–7295. [PMID: 21513273]
[EC 4.3.1.30 created 2011]
EC	5.1.3.43
Accepted name:	sulfoquinovose mutarotase
Reaction:	6-sulfo-α-D-quinovose = 6-sulfo-β-D-quinovose
Systematic name:	6-sulfo-D-quinovose 1-epimerase
Comments:	The enzyme is found in bacteria that possess sulfoglycolytic pathways. The enzyme can also act on other aldohexoses such as D-galactose, D-glucose, D-glucose-6-phosphate, and D-glucuronate, but with lower efficiency. Does not act on D-mannose.
References:	1.  Abayakoon, P., Lingford, J.P., Jin, Y., Bengt, C., Davies, G.J., Yao, S., Goddard-Borger, E.D. and Williams, S.J. Discovery and characterization of a sulfoquinovose mutarotase using kinetic analysis at equilibrium by exchange spectroscopy. Biochem. J. 475 (2018) 1371–1383. [PMID: 29535276]
[EC 5.1.3.43 created 2019]