4.1.99.14	evolution	enzyme SPL belongs to the radical SAM (S-adenosylmethionine) enzyme superfamily. The superfamily is defined by the characteristic tri-cysteinyl motif: CX3CX2C that binds to a [4Fe-4S] cluster	-, 748849	
4.1.99.14	evolution	spore photoproduct lyase (SPL) is a member of the radical S-adenosyl-L-methionine (SAM) superfamily, the family members utilize S-adenosyl-Lmethionine (SAM) and a redox active [4Fe-4S] cluster to carry out diverse radical reactions including rearrangements, sulfur insertions and oxidations. Electron-nuclear double resonance and X-ray crystallography of several members of the superfamily have shown that the unique iron is coordinated by the amino and carboxylate moieties of S-adenosyl-L-methionine. An innersphere electron transfer from a reduced [4Fe-4S]+ cluster to the sulfonium of SAM leads to homolytic S-C(5') bond cleavage to generate a 5'-deoxyadenosyl radical (dAdo) intermediate, which abstracts a hydrogen atom from substrate to initiate a radical transformation	-, 748241	
4.1.99.14	evolution	the enzyme is a member of the radical SAM superfamily	-, 726998	
4.1.99.14	evolution	the enzyme is a member of the radical SAM superfamily, but SP lyase is the only known radical SAM enzyme to date catalyzing DNA repair. Clostridia SP lyases possess a conserved cysteine residue upstream the radical SAM motif (Cys74), which is substituted by a serine residue in Bacilli SP lyases	-, 748852	
4.1.99.14	evolution	the enzyme is a member of the radical SAM superfamily, but SP lyase is the only known radical SAM enzyme to date catalyzing DNA repair. Clostridia SP lyases possess a conserved cysteine residue upstream the radical SAM motif (Cys74), which is substituted by a serine residue in Bacilli SP lyases. Cys74 in Ca SP lyase occupies a critical location similar to Cys140 in Gt SP lyase	-, 748852	
4.1.99.14	evolution	the enzyme is a member of the radical SAM superfamily, but SP lyase is the only known radical SAM enzyme to date catalyzing DNA repair. Cys74 in Ca SP lyase occupies a critical location similar to Cys140 in Gt SP lyase	-, 748852	
4.1.99.14	evolution	the enzyme is a member of the radical SAM superfamily, which is defined by the characteristic CXXXCXXC motif	-, 748201	
4.1.99.14	evolution	the enzyme is a member of the so-called radical SAM superfamily, which is defined by the characteristic CXXXCXXC motif. The three cysteine residues serve as ligands respectively for three irons in the [4Fe-4S] cluster, with the fourth iron being coordinated by the S-adenosylmethionine in a bi-dentate manner, with its amino and carboxylate moieties serving as the fourth and fifth ligands to the cluster. SPL and the DNA photolyase, EC 4.1.99.3, show amino acid sequence homolgy and might have descended from a common ancestral protein	-, 727074	
4.1.99.14	evolution	the enzyme is the first member of the radical SAM superfamily (comprising more than 44000 members) to bear a catalytically operating hydrogen atom transfer chain that is essential for S-adenosyl-L-methionine regeneration after the catalytic cycle	-, 727020	
4.1.99.14	evolution	unlike DNA photolyases, EC 4.1.99.3, SP lyase belongs to the emerging superfamily of radical S-adenosyl-L-methionine (SAM) enzymes	-, 728401