Skip to main content
. Author manuscript; available in PMC: 2017 Jan 1.
Published in final edited form as: Plant Physiol Biochem. 2015 Nov 27;98:171–185. doi: 10.1016/j.plaphy.2015.11.017

Figure 2. Multiple sequence alignment of all characterized aldonolactone oxidoreductases including Arabidopsis GulLO (AtGulLO5 or At2g46740).

Figure 2

Conserved residues interacting with the parts of FAD in the alignment are shown as in Fraaije et al (1998). (G, glycine; H, histidine; s, small: G, A, S, T; h, hydrophobic: I, L, V; -, any residue). Numbers in parenthesis indicate the residues present in gaps and termini. The residue indicating oxygen reactivity is marked by asterisk (*; Leferink et al. 2009b). Arrow indicates the cysteine residue known to be involved with thiol modifying agents in AtGLDH (Leferink et al. 2009d). The Glu-Arg pair identified in the catalytic site of AtGLDH (Leferink et al. 2009c) is also highlighted. The sequences used are: BoGLDH (cauliflower; Swiss-Prot: O47881), IbGLDH (sweet potato; GenBank: BAA34995), NtGLDH (tobacco; GenBank: BAB13368), AtGLDH (Arabidopsis; Swiss-Prot: Q9SU56), AtGulLO5 (Arabidopsis; GenBank: AEC10747), RnGulLO (rat; Swiss-Prot: P10867), MmGulLO (mouse; GenBank: AAR15891), SsGulLO (pig; GenBank: AAN63634), ScALO (S. cerevisiae; Swiss-Prot: P54783), CaALO (C. albicans; GenBank: AAC98913), PgGUO (P. griseoroseum; Swiss-Prot: Q671X8), TbGalLO (T. brucei; Swiss-Prot: Q57ZU1), TcGalLO (T. cruzi; Swiss-Prot: Q4DPZ5), LdALO (L. donovani; GenBank: ACV04074), MtGulLDH (M. tuberculosis; Swiss-Prot: O06804).