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Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II
Phosphoglucomutase/phosphomannomutase, C-terminal domain
phosphoglucosamine mutase
The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis [1]. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: PF02878, PF02879 and PF02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP [2] identifies members of this archaeal GlmM family as the highest-scoring result.
phosphohexomutase domain-containing protein; phosphopentomutase/phosphoglucosamine mutase
phosphohexomutase domain-containing protein catalyzes catalyzes the reversible conversion of 1-phospho to 6-phosphohexose, with various sugars including glucose, mannose, glucosamine, and N-acetylglucosamine| phosphopentomutase (PPM)/phosphoglucosamine mutase (GLMM) catalyzes the conversion of deoxyribose 1-phosphate to deoxyribose 5-phosphate, or the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate, respectively
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