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Supplementary figure

Membrane-association determinants of the ω-amino acid monooxygenase PvdA, a pyoverdine biosynthetic enzyme from Pseudomonas aeruginosa, by F. Imperi, L. Putignani, F. Tiburzi, C. Ambrosi, R. Cipollone, P. Ascenzi and P. Visca

Microbiology vol. 154, part 9, pp. 2804-2813

Fig. S1. Multiple sequence alignment of PvdA with proximate homologues generated by the Jpred software (http://barton.ebi.ac.uk/servers/jpred.html). Amino acid positions are indicated on top. Only regions containing conserved residues are considered by Jpred algorithms. Identical and similar residues common to the 22 aligned proteins are shaded in dark and light yellow, respectively. Similar residues are I, L, V and M; F and Y; D and E; S and T; R and K. Light green rectangles indicate the FAD, NAD(P)H and F/LATGY domains with strictly consensus motifs highlighted by black boxes. Protein sequences, with the accession number in parentheses, are: Mycobacterium tuberculosis CDC1551 probable monooxygenase, Mon. M.tub (O53294); Nitrosomonas europaea ATCC 19718 FAD-dependent pyridine nucleotide-disulphide oxidoreductase, Mon. N.eur (Q82TE8); Caulobacter crescentus ATCC 19089 uncharacterized monooxygenase, Mon. C.cre (Q9A588); Fugu rubripes uncharacterized flavin monooxygenase, FMO F.rub (Q802T5); Gallus gallus uncharacterized flavin-containing monooxygenase, FMO3 G.gal (Q8QH01); Agrobacterium tumefaciens ATCC 33970 uncharacterized oxidoreductase, Oxi. A.tum (Q8UJQ2); Rhesus macaque dimethylaniline monooxygenase, FMO2 R.mac (Q28505); Arabidopsis thaliana monooxygenase, Mon. A.tha (O64489); Ustilago maydis l-Orn N^δ-oxygenase, Sid1 U.may (P56584); Saccharomyces pombe monooxygenase, Mon. S.pom (Q9P7T0); Aureobasidium pullulans hydroxylase, Hydro. A.pul (O94115); Bordetella pertussis alcaligin biosynthesis enzyme, AlcA B.per (P59855); Halobacterium salinarium monooxygenase, HxyA H.sal (Q9HHV0); Escherichia coli l-lysine N^ε-hydroxylase, IucD E.col (P11295); Sinorhizobium meliloti rhizobactin biosynthesis enzyme, RhbE R.mel (Q9Z3Q8); Yersinia pestis CO92 putative siderophore biosynthetic enzyme, AlcA Y.pes (Q8ZFZ3); Shewanella oneidensis siderophore biosynthesis monooxygenase, Mon. S.one (Q8ECU3); Aspergillus oryzae Orn N^δ-oxygenase, Mon. A.ory (Q8J2V1); Bacillus halodurans uncharacterized monooxygenase, Mon. B.hal (Q9K9M5); Streptomyces coelicolor putative monooxygenase, Mon. S.coe (Q9L071); Anabaena sp. uncharacterized monooxygenase, Mon. A. sp. (Q8YZR5); Pseudomonas aeruginosa PAO1 l-Orn N^δ-oxygenase, PvdA P.aer (Q51548). The predicted buried state (B) of PvdA amino acids with less than 5 % solvent accessibility is shown below the PvdA sequence. The inferred α-helices (H) and β-strands (E) of the PvdA consensus secondary structure are represented as red cylinders and green arrows, respectively. Negatively (D and E) and positively (R and K) charged PvdA amino acid residues are indicated by blue and red bold characters, respectively.

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