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Example sentences for: ec-
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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.
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.
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).
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