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EC Number Cofactor Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.44Fe-S center residues Cys81, Cys85 and Cys88 are predicted to comprise the iron-sulfur cluster. In the crystal structure, their side chains face each other to create the cluster site 723823
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.44S-adenosyl-L-methionine - 747086, 747631, 748046
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.44[4Fe-4S]-center - 722112, 748046
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.44[4Fe-4S]-center contains two [4Fe-4S] clusters 747631
Display the word mapDisplay the reaction diagram Show all sequences 4.1.3.44[4Fe-4S]-center the N-terminal half of the enzyme beside the radical-SAM cysteine triad, contains an additional highly conserved cysteine motif involved in the coordination of a second [4Fe-4S] cluster. This cluster displays a free coordination site that interacts with pyruvate, the second substrate of the reaction 725500
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