Figure 2.

Multiple sequence alignment of UlaGL protein sequences among bacteria. Multiple sequence alignment of E. coli UlaG (E. coli; top sequence) against six divergent UlaGL sequences from Gram-negative and Gram-positive bacteria. In descending order, sequences included are putative L-ascorbate 6-phosphate lactonases from Salmonella enterica subsp. enterica serovar Typhi str. CT18 (NP_458816); Klebsiella pneumoniae subsp. pneumoniae MGH 78578 (YP_001338203); Clostridium botulinum B str. Eklund 17B (YP_001887453); Yersinia intermedia ATCC 29909 (ZP_046368); Vibrio cholerae V51 (ZP_04919573); Streptococcus pyogenes MGAS315 (NP_663946); and Atopobium vaginae DSM 15829 (ZP_039469). Pairwise sequence identities are larger than 50% for all sequences in the multiple sequence alignment. Characteristic motifs of the metallo-β-lactamase protein fold are shown underlined on top of the alignment, and absolutely conserved catalytic aspartate and histidine residues within these motifs are marked underneath the alignment as red or blue squares, respectively. Residues involved in intersubunit contacts are boxed.

Fernandez et al. BMC Evolutionary Biology 2011 11:273   doi:10.1186/1471-2148-11-273
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