Fig. 5.
Fig. 5. Multiple sequence alignment of the cytosolic C-terminal nucleotide binding domains of gp91-phox with members of the FNR family with known 3-dimensional structure. / The deduced amino acid sequence of gp91-phox is aligned with the amino acid sequences of ferredoxin NADP+ reductase from spinach (1fnb),43 Azotobacter vinelandii(1a8p),59 and Anabaena (1quf);60phthalate dioxygenase reductase from Pseudomonas cepacia(2pia);46 nitrate reductase from corn (1cnf);61 cytochrome b5 reductase from pig liver (1ndh);62 flavohemoglobin fromAlcaligenes eutrophus (1fhp);63 and flavodoxin reductase from Escherichia coli (1fdr).64 Secondary structure elements are underlined, conserved residues shown in bold, and mutated residues indicated by an asterisk.

Multiple sequence alignment of the cytosolic C-terminal nucleotide binding domains of gp91-phox with members of the FNR family with known 3-dimensional structure.

The deduced amino acid sequence of gp91-phox is aligned with the amino acid sequences of ferredoxin NADP+ reductase from spinach (1fnb),43,Azotobacter vinelandii(1a8p),59 and Anabaena (1quf);60phthalate dioxygenase reductase from Pseudomonas cepacia(2pia);46 nitrate reductase from corn (1cnf);61 cytochrome b5 reductase from pig liver (1ndh);62 flavohemoglobin fromAlcaligenes eutrophus (1fhp);63 and flavodoxin reductase from Escherichia coli (1fdr).64 Secondary structure elements are underlined, conserved residues shown in bold, and mutated residues indicated by an asterisk.

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