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All of the predicted amino acid sequences except Ec-MoeB, Mlo-MoeZdR, and Pa-MoeB also have C-terminal similarity (BLAST E value < 1 -12) to a rhodanese-like domain (Pfam00581) (Figure 2c, Table 2) [ 26 ] . Rhodanese, a thiosulfate:cyanide sulfurtransferase (EC 2.8.
MoeB, as represented by the functionally characterized Ec-MoeB, consists of an N-terminal ThiF domain followed by a 2X CXXC domain with both CXXC pairs intact and no rhodanese-like domain.
In Ec-MoeB, β sheet 5 (residues 149-155 of Ec-MoeB, Figure 3) forms part of the pocket which accepts the C-terminal portion of MoaD, of which the terminal glycine is subsequently adenylated [ 7 ] . Ec-MoeB I155, located at the C-terminal end of this beta loop, is substituted in MoeBR proteins by Y and in MoeZ proteins by F or Y. These bulky substitutions may restrict access of the C-terminus of MoeD-like proteins and may indicate that a different type of substrate is adenylated by MoeBR and MoeZ.
Ec-MoeB, Mt-MoeBR, Pa-MoeB, Pa-MoeBR, and Sc-MoeBR all contain two pairs of cysteine residues, each arranged in a CXXC motif and spaced 68-70 residues apart, like those in ThiF proteins (arrows in Figures 2cand 3).
MoeBR has the ThiF and 2X CXXC domains configured like MoeB but includes an N-terminal rhodanese-like domain, the polyproline motif, and has a Y substitution at position 155 (Ec-MoeB numbering).