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3.1.3.22
evolution
the C-terminus of MtlD from Acinetobacter baylyi is similar to dehydrogenase domains found in other dehydrogenases with a glycine-rich conserved domain (Rossmann-fold) starting at position 247 for cosubstrate binding (GIHGFGAIGGG). The N-terminal domain of MtlD is similar to members of the HAD (haloacid dehalogenase) superfamily
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,
729646
3.1.3.22
physiological function
after deletion of the mtlD gene, cells no longer accumulate mannitol and growth is completely impaired at high salt concentrations
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,
751514
3.1.3.22
physiological function
the nutritionally versatile soil bacterium Acinetobacter baylyi ADP1 copes with salt stress by the accumulation of compatible solutes. The bacterium synthesizes the sugar alcohol mannitol de novo in response to osmotic stress. THe enzyme is essential for mannitol 1-phosphate biosynthesis, and it also possesses a unique sequence among known mannitol-1-phosphate dehydrogenases with a haloacid dehalogenase (HAD)-like phosphatase domain at the N-terminus. This domain has phosphatase activity
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729646
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