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. 2003 Aug;69(8):4989–4993. doi: 10.1128/AEM.69.8.4989-4993.2003

FIG. 2.

FIG. 2.

Conserved regions in the amino acid sequences of the putative AiiA homologues. The sequences of putative AiiA homologues from Deinococcus radiodurans R1 (De.ra.gi15805209 and De.ra.gi15806823), Xylella fastidiosa 9a5c (Xy.fa.gi15837962), Mesorhizobium loti MAFF303099 (Me.lo.gi13475678), Staphylococcus aureus Mu50 (St.au.gi15924737), Listeria innocua Clip11262 (Li.in.gi16800723), Bacillus halodurans C-125 (Ba.ha.gi15615822), Sinorhizobium meliloti 1021 (Si.me.gi15964512), and Plesiomonas sp. strain M6 (Ps.sp.gi13173397) and the sequences of glyoxalase GloB (Ec.co.gi2494853) of E. coli and AiiA from Bacillus sp. strain 240B1, AiiAsoil, AttM, AiiB, and AiiC from A. tumefaciens (Ag.tu.) are shown. Each one of the five segments that are conserved among the Zn metallohydrolases (2) was present in the AiiA homologues. When more than 10 sequences (of 14) contain an identical (or a physiochemically similar residue) at a given site, the consensus residue (or the abbreviation of their physiochemical family) is reported below the alignment as follows: h for the hydrophobic residues L, I, M, and V; s for the small hydrophobic residues S, P, T, A and G; and n for the negatively charged residues and their relatives, D, E, N, and Q. The residues that are conserved among the AiiA homologues and the GloB Zn metallohydrolase are shown in bold type in the GloB sequence, and the residues interacting with the metal cations are noted by an asterisk. Numbers in parentheses indicate the number of residues omitted in the sequences.