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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, exemplified by Ec-MoeB, and MoeBR, exemplified by cnxF of Aspergillis nidulans [ 16 ] , participate in the synthesis of MPT-Mo as MSAEs.
All 12 sequences in this region have high similarity to the derived consensus sequence GXGXXG(7X)A(SX)GXGXXG(4X)D(9X)R, which defines a nucleotide binding motif [ 16 25 ] . In addition, all sequences have five residues, or conservative substitutions in the case of Pa-MoeB, shown to participate in the adenylation reaction catalyzed by Ec-MoeB (Figure 3) [ 7 ] . The fact that such high similarities are retained in the ThiF coding region across three bacterial divisions suggests that this domain functions more or less autonomously.
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.
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).