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radical SAM protein
Radical SAM proteins catalyse diverse reactions, including unusual methylations, isomerisation, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation. [1]. 11222759. Radical SAM, a novel protein superfamily linking unresolved. steps in familiar biosynthetic pathways with radical mechanisms:. functional characterization using new analysis and information. visualization methods.. Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE;. Nucleic Acids Res 2001;29:1097-1106.. [2]. 17335281. Anaerobic sulfatase-maturating enzymes: radical SAM enzymes able. to catalyze in vitro sulfatase post-translational modification.. Benjdia A, Leprince J, Guillot A, Vaudry H, Rabot S, Berteau O;. J Am Chem Soc. 2007;129:3462-3463.. [3]. 16766528. A new type of bacterial sulfatase reveals a novel maturation. pathway in prokaryotes.. Berteau O, Guillot A, Benjdia A, Rabot S;. J Biol Chem. 2006;281:22464-22470. (from Pfam)
cobalamin-dependent protein
This domain binds to B12 (adenosylcobamide)[1-3], it is found in several enzymes, such as glutamate mutase Swiss:Q05488, methionine synthase Swiss:Q99707 and methylmalonyl-CoA mutase Swiss:P22033. It contains a conserved DxHxxGx(41)SxVx(26)GG motif, which is important for B12 binding [2]. [1]. 9739092. How a protein prepares for B12 binding: structure and dynamics. of the B12-binding subunit of glutamate mutase from Clostridium. tetanomorphum.. Tollinger M, Konrat R, Hilbert BH, Marsh EN, Krautler B;. Structure 1998;6:1021-1033.. [2]. 11914353. Role for vitamin B(12) in light induction of gene expression in. the bacterium Myxococcus xanthus.. Cervantes M, Murillo FJ;. J Bacteriol. 2002;184:2215-2224.. [3]. 18315685. Vitamin B12 partners the CarH repressor to downregulate a. photoinducible promoter in Myxococcus xanthus.. Perez-Marin MC, Padmanabhan S, Polanco MC, Murillo FJ,. Elias-Arnanz M;. Mol Microbiol. 2008;67:804-819. (from Pfam)
B12-binding domain-containing radical SAM protein
B12-binding domain-containing radical SAM protein generates radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity; contains a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster; transfer of a single electron from the iron-sulfur cluster to SAM leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical
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