2.1.1.269 evolution analysis of diversity of genes encoding DMSP demethylase (dmdA) and DMSP lyases (dddD, dddL, and dddP) in bacteria in the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay using DMSP degradation gene clone library analysis, overview. Both bacterial dmdA and dddP genes found in the two coves are completely confined to the Roseobacter clade, which indicated that this clade plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay. Diversity and distribution of dmdA genes within the Roseobacter clade, including the genera Litoreibacter, Loktanella, Octadecabacter, Roseobacter, Ruegeria, and Sulfitobacter, phylogenetic tree, overview 756542 2.1.1.269 evolution analysis of diversity of genes encoding DMSP demethylase (dmdA) and DMSP lyases (dddD, dddL, and dddP) in bacteria in the surface seawater of Ardley Cove and Great Wall Cove in Antarctic Maxwell Bay using DMSP degradation gene clone library analysis, overview. Both bacterial dmdA and dddP genes found in the two coves are completely confined to the Roseobacter clade, which indicated that this clade plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay. Diversity and distribution of dmdA genes within theRoseobacter clade, including the genera Litoreibacter, Loktanella, Octadecabacter, Roseobacter, Ruegeria, and Sulfitobacter, phylogenetic tree, overview 756542 2.1.1.269 evolution detection of taxon-specific gene expression in Roseobacter sp. HTCC2255 and in situ regulation of the first gene in each DMSP pathway, gene dddP and gene dmdA, that corresponds with shifts in the taxonomy of the phytoplankton community -, 736286 2.1.1.269 evolution DmdA belongs to a diverse family of enzymes, the overall fold of the DmdA is not similar to other enzymes that typically utilize the reduced form of tetrahydrofolate and in fact is a triple domain structure similar to what has been observed for the glycine cleavage T protein or sarcosine oxidase. All other THF binding fold enzymes produce 5,10-methylene-tetrahydrofolate. The relative positioning of Y206 in DmdA is different in comparison to the other THF dependent enzymes 720998 2.1.1.269 evolution phylogenetic analysis, multidimensional analysis based on the abundances of dimethylsulfoniopropionate degradation genes and environmental factors reveal that the distribution pattern of these genes is influenced by chlorophyll a concentrations and temperatures. dddP genes, dmdA subclade C/2 genes, and dmdA subclade D genes exhibit significant correlations with the marine Roseobacter clade, SAR11 subgroup Ib, and SAR11 subgroup Ia, respectively. SAR11 subgroups Ia and Ib, which possess dmdA genes, are suggested to be the main potential dimethylsulfoniopropionate consumers -, 735504 2.1.1.269 evolution though DmdA is homologous to the glycine cleavage T-protein and shares structural similarity, the mechanism of carbon transfer is more similar to S-adenosyl-methionine (SAM)-dependent methyl-transfer enzymes. DmdA catalyzes the transfer of a methyl group to form 5-methyl-THF, which is analogous to SAM-dependent reactions. The gene dmdA is abundant in marine waters -, 757585 2.1.1.269 metabolism both bipolar and endemic bacterial DMSP degradation genes exist in polar marine environments 756542 2.1.1.269 metabolism the bacterial switch is a proposed regulatory point in the global sulfur cycle that routes dimethylsulfoniopropionate to two fundamentally different fates in seawater through genes encoding either the cleavage or demethylation pathway, and affects the flux of volatile sulfur from ocean surface waters to the atmosphere -, 736286 2.1.1.269 metabolism the enzyme catalyzes the first step of the dimethylsulfoniopropionate, DMSP, cleavage pathway. DMSP is a ubiquitous phytoplankton metabolite that is degraded by marine microorganisms by at least two major pathways -, 718639 2.1.1.269 additional information positive correlation of katG expression with gene dmdA but not gene dddP during the period when regulation expression is uncoupled 736286 2.1.1.269 physiological function dimethylsulfoniopropionate (DMSP) demethylase is a tetrahydrofolate-dependent enzyme that initiates the DMSP demethylation pathway in marine bacteria. This enzyme is important for understanding of organic sulfur flux from the oceans because it directs the sulfur from DMSP away from dimethylsulfide -, 757585 2.1.1.269 physiological function DMSP demethylase is responsible for the dimethylsulfoniopropionate assimilation -, 735504 2.1.1.269 physiological function Roseobacter plays a significant role in DMSP catabolism in the coastal seawaters of Maxwell Bay 756542