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Figure 9 | BMC Genomics

Figure 9

From: Bioinformatic evaluation of L-arginine catabolic pathways in 24 cyanobacteria and transcriptional analysis of genes encoding enzymes of L-arginine catabolism in the cyanobacterium Synechocystis sp. PCC 6803

Figure 9

ClustalW alignment of the putative L-arginine oxidase/dehydrogenase Slr0782 from Synechocystis sp. PCC 6803 with the characterized L-amino acid oxidase AoxA from Synechococcus elongatus PCC 6301 (P72346) [23]. Both proteins share an overall similarity of 57% (21% identical, 23% similar, and 13% weakly amino acid residues). The dinucleotide binding motif GxGxxG is boxed. * Identical amino acid residues, : similar amino acid residues (A/V/F/P/M/I/L/W, D/E, R/H/K, S/T/Y/H/C/N/G/Q, and • weakly similar amino acid residues. Gaps were introduced into the sequences to maintain an optimal alignment. Two putative transmembrane helices (aa 628–648; aa 670–690) were detected for Slr0782 using the DAS TM prediction algorithm [52]. Slr0782 also has 66% similarity (31% identical; 22% strongly similar, and 13% weakly similar amino acid residues) to AoxB of Synechococcus elongatus PCC 6301, an enzyme not yet characterized.

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