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cyclic pyranopterin monophosphate synthase MoaC
Members of this family are involved in molybdenum cofactor biosynthesis. However their molecular function is not known. [1]. 10411269. Characterization of a molybdenum cofactor biosynthetic gene. cluster in Rhodobacter capsulatus which is specific for the. biogenesis of dimethylsulfoxide reductase.. Solomon PS, Shaw AL, Lane I, Hanson GR, Palmer T, McEwan AG;. Microbiology 1999;145:1421-1429. (from Pfam)
cyclic pyranopterin monophosphate synthase MoaC catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP), as part of the molybdenum cofactor biosynthesis
MoaC catalyzes an early step in molybdenum cofactor biosynthesis in E. coli. The Arabidopsis homolog Cnx3 complements MoaC deficiency in E. coli (MUID:95197640). Eukarotic members of this family branch within the bacterial branch, with the archaeal members as an apparent outgroup. This protein is absent in a number of the pathogens with smaller genomes, including Mycoplasmas, Chlamydias, and spirochetes, but is found in most other complete genomes to date. The homolog form Synechocystis sp. is fused to a MobA-homologous region and is an outlier to all other bacterial forms by both neighbor-joining and UPGMA analyses. Members of this family are well-conserved. The seed for this model excludes both archaeal sequences and the most divergent bacterial sequences, but still finds all candidate MoaC sequences easily between trusted and noise cutoffs. We suggest that sequences branching outside the set that contains all seed members be regarded only as putative functional equivalents of MoaC unless and until a member of the archaeal outgroup is shown to have equivalent function.
Along with MoaA is involved in conversion of a guanosine derivative into molybdopterin precursor Z; involved in molybdenum cofactor biosynthesis
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