(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 > Gammaproteobacteria: NE > Thiotrichales: NE > Piscirickettsiaceae: NE > Cycloclasticus: NE > Cycloclasticus sp. P1: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid 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.) Cycloclasticus zancles 78-ME: N, E.
Cycloclasticus zancles 7-ME: N, E.
Cycloclasticus sp. PY97M: N, E.
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 MMAGLQRVGYPNGLFLIIEFFVHIIYLHGFCSSVDSFKAQLVKSYIERNN VHTLFLKDLPPSPAQAMSLVEAHIASLDDQYWGVVGSSLGGFYATYLSQK YAKKAVLINPAVDAHLILEKALGKNTNYHTGESFDFTLTHLQELQQLHLP KLQQAQNLLLLTKVGDEVLDFQKGVDYYQGSEQVVLEGGDHGFADYENYL EKTFDFLTS
Esterases receive special attention because their wide distribution in biological systems and environments and their importance for physiology and chemical synthesis. The prediction of esterases substrate promiscuity level from sequence data and the molecular reasons why certain such enzymes are more promiscuous than others, remain to be elucidated. This limits the surveillance of the sequence space for esterases potentially leading to new versatile biocatalysts and new insights into their role in cellular function. Here we performed an extensive analysis of the substrate spectra of 145 phylogenetically and environmentally diverse microbial esterases, when tested with 96 diverse esters. We determined the primary factors shaping their substrate range by analyzing substrate range patterns in combination with structural analysis and protein-ligand simulations. We found a structural parameter that helps ranking (classifying) promiscuity level of esterases from sequence data at 94% accuracy. This parameter, the active site effective volume, exemplifies the topology of the catalytic environment by measuring the active site cavity volume corrected by the relative solvent accessible surface area (SASA) of the catalytic triad. Sequences encoding esterases with active site effective volumes (cavity volume/SASA) above a threshold show greater substrate spectra, which can be further extended in combination with phylogenetic data. This measure provides also a valuable tool for interrogating substrates capable of being converted. This measure, found to be transferred to phosphatases of the haloalkanoic acid dehalogenase superfamily and possibly other enzymatic systems, represents a powerful tool for low-cost bioprospecting for esterases with broad substrate ranges, in large scale sequence datasets.
Title: Genome Sequence of the Polycyclic Aromatic Hydrocarbon-Degrading Bacterium Strain Marinobacter nanhaiticus D15-8WT Cui Z, Gao W, Li Q, Xu G, Zheng L Ref: Genome Announc, 1:, 2013 : PubMed
Marinobacter nanhaiticus strain D15-8W(T) was isolated from a phenanthrene-degrading consortium, enriched from sediment of the South China Sea. Here, we present the draft genome of strain D15-8W(T), which contains 5,358,309 bp with a G+C content of 58.53% and contains 4,829 protein-coding genes and 47 tRNA genes.
Title: Complete genome sequence of the pyrene-degrading bacterium Cycloclasticus sp. strain P1 Lai Q, Li W, Wang B, Yu Z, Shao Z Ref: Journal of Bacteriology, 194:6677, 2012 : PubMed
Cycloclasticus sp. strain P1 was isolated from deep-sea sediments of the Pacific Ocean and characterized as a unique bacterium in the degradation of pyrene, a four-ring polycyclic aromatic hydrocarbon (PAH). Here we report the complete genome of P1 and genes associated with PAH degradation.
Cycloclasticus sp. P1, EH60 Alpha/beta hydrolase fold-containing protein CCSP0084