(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Proteobacteria: NE > Alphaproteobacteria: NE > Sphingomonadales: NE > Sphingomonadaceae: NE > Sphingomonas: NE > Sphingomonas paucimobilis: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Pseudomonas paucimobilis: N, E.
Sphingomonas paucimobilis NBRC 13935: N, E.
Sphingobium sp. MI1205: N, E.
Sphingobium indicum B90A: N, E.
Molecular evidence
Database
No mutation 8 structures(e.g. : 4H77, 4H7D, 4H7E... more)(less) 4H77: Crystal structure of haloalkane dehalogenase LinB from Sphingobium sp. MI1205, 4H7D: Crystal structure of haloalkane dehalogenase LinB T81A mutant from Sphingobium sp. MI1205, 4H7E: Crystal structure of haloalkane dehalogenase LinB V112A mutant from Sphingobium sp. MI1205, 4H7F: Crystal structure of haloalkane dehalogenase LinB V134I mutant from Sphingobium sp. MI1205, 4H7H: Crystal structure of haloalkane dehalogenase LinB T135A mutant from Sphingobium sp. MI1205, 4H7I: Crystal structure of haloalkane dehalogenase LinB L138I mutant from Sphingobium sp. MI1205, 4H7J: Crystal structure of haloalkane dehalogenase LinB H247A mutant from Sphingobium sp. MI1205, 4H7K: Crystal structure of haloalkane dehalogenase LinB I253M mutant from Sphingobium sp. MI1205 No kinetic
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MSLGAKPFGEKKFIEIKGRRMAYIDEGTGDPILFQHGNPTSSYLWRNIMP HCAGLGRLIACDLIGMGDSDKLDPSGPERYTYAEHRDYLDALWEALDLGD RVVLVVHDWGSVLGFDWARRHRERVQGIAYMEAVTMPLEWADFPEQDRDL FQAFRSQAGEELVLQDNVFVEQVLPGLILRPLSEAEMAAYREPFLAAGEA RRPTLSWPRQIPIAGTPADVVAIARDYAGWLSESPIPKLFINAEPGHLTT GRIRDFCRTWPNQTEITVAGAHFIQEDSPDEIGAAIAAFVRRLRPA
The enzymes LinBUT and LinBMI (LinB from Sphingobium japonicum UT26 and Sphingobium sp. MI1205, respectively) catalyze the hydrolytic dechlorination of beta-hexachlorocyclohexane (beta-HCH) and yield different products, 2,3,4,5,6-pentachlorocyclohexanol (PCHL) and 2,3,5,6-tetrachlorocyclohexane-1,4-diol (TCDL), respectively, despite their 98% identity in amino acid sequence. To reveal the structural basis of their different enzymatic properties, we performed site-directed mutagenesis and X-ray crystallographic studies of LinBMI and its seven point mutants. The mutation analysis revealed that the seven amino acid residues uniquely found in LinBMI were categorized into three groups based on the efficiency of the first-step (from beta-HCH to PCHL) and second-step (from PCHL to TCDL) conversions. Crystal structure analyses of wild-type LinBMI and its seven point mutants indicated how each mutated residue contributed to the first- and second-step conversions by LinBMI. The dynamics simulation analyses of wild-type LinBMI and LinBUT revealed that the entrance of the substrate access tunnel of LinBUT was more flexible than that of LinBMI, which could lead to the different efficiencies of dehalogenation activity between these dehalogenases.
Sphingomonas paucimobilis (Pseudomonas paucimobilis); Sphingobium sp., Sphingobium indicum; Haloalkane dehalogenase linB gene
