|Domain Trusted Cutoff||439.00|
|Domain Noise Cutoff||400.30|
|Entry Date||Apr 20 2010 11:48AM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis . 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  identifies members of this archaeal GlmM family as the highest-scoring result.|
RT Acetamido sugar biosynthesis in the Euryarchaea.
RA Namboori SC, Graham DE
RL J Bacteriol. 2008 Apr;190(8):2987-96. Epub 2008 Feb 8.
RT Exopolysaccharide-associated protein sorting in environmental organisms: the PEP-CTERM/EpsH system. Application of a novel phylogenetic profiling heuristic.
RA Haft DH, Paulsen IT, Ward N, Selengut JD
RL BMC Biol. 2006 Aug 24;4:29.|
|Genome Property||GenProp0750: UDP-N-acetylglucosamine biosynthesis from fructose-6-phosphate (HMM)|
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