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Figure 1 | BMC Microbiology

Figure 1

From: Functional characterization of two members of histidine phosphatase superfamily in Mycobacterium tuberculosis

Figure 1

Multiple alignment of amino acid sequences of some members of histidine phosphatase superfamily with Rv2135c. The alignment was done with ClustalX2 using the default parameters. The asterisks indicate fully conserved amino acid residues of the superfamily. Colons indicate strongly similar residues, dots indicate weakly similar residues [37]. Bacillusap: Acid phosphatase of Bacillus licheniformis. Cryparpgm: Phosphoglycerate domain of Cryptosporidium parvum. E.colidpgM: Cofactor dependent phosphoglycerate mutase of E. coli. PhoE: Acid phosphatase of Bacillus stearothermophillus. Rv0489: Cofactor dependent phosphoglycerate mutase of M. tuberculosis. Rv2419c: Glucosyl-3-phosphoglycerate phosphatase of M. tuberculosis. Rv3214: Acid phosphatase of M. tuberculosis. Rv3837c: Probable cofactor dependent phosphoglycerate mutase of M. tuberculosis. YDR051pgm: Cofactor dependent phosphoglycerate mutase of Saccharomyces arboricola. Functions of Bacillusap, Cryparpgm and Rv3837c were predicted with bioinformatics while E.colidpgM, Rv0489, PhoE, Rv2419c, Rv3214 and YDR051pgm have been experimentally characterized.

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BMC Microbiology

ISSN: 1471-2180

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