hydrolase activity, acting on ester bonds.

MTLARREFLHVLALAAAGMGLTSRAANAAIEYDLAPMGNLSLLHFTDSHAQLLPVHYREP SYNIGLGEAFGRPPHIVGQHLLDYFGLSPATAQAHALTSLDFETAASKYGKLGGFAHLAT LIKRLRAERPHSLLLDGGDTWQGSATALWTQGRDMIEACRLLGVDMMTGHWEFTYGMDRV REIINNELAPIEFLAQNVYLTEDAAFNDRPAFDEETGLVFKPYSLRMVNGVAVAVIGQAF PYTTLANPRYLIDEWSFGIREERVQASVEAARAEGAEVVVLLSHNGMDVDLKLASRVSGI DVILGGHTHDGVPVPSIVHNNGGQTLVVNSGSNGKFLSVLDLDVRAGRVQNYQFRLLPVF ANLLTPDPEMASLIEAVRSPYEDRLNEVLATTDTLLYRRGNFSGTFDQIIVDALREVQGA DIALSPGFRWGTTLLPGDSITMEQLMDQTAITYAKSTLAEMTGSDIHALLEDIADNLFNP DPYYQMGGDMVRVGGLSYTIDPSVPMGQRISELQFKNKPLDPNRRYRVAGWASVRPQPDE SPDIWQVVGDYLRDRKRIDQVAVNMPHVKGVTNNPGWIRQ589

	PMID	Title & Author	Abstract	Year
0	16995898	Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum. Hensen D, Sperling D, Trüper HG, Brune DC, Dahl C.	Two different pathways for thiosulphate oxidation are present in the purple sulphur bacterium Allochromatium vinosum: oxidation to tetrathionate and complete oxidation to sulphate with obligatory formation of sulphur globules as intermediates. The tetrathionate:sulphate ratio is strongly pH-dependent with tetrathionate formation being preferred under acidic conditions. Thiosulphate dehydrogenase, a constitutively expressed monomeric 30 kDa c-type cytochrome with a pH optimum at pH 4.2 catalyses tetrathionate formation. A periplasmic thiosulphate-oxidizing multienzyme complex (Sox) has been described to be responsible for formation of sulphate from thiosulphate in chemotrophic and phototrophic sulphur oxidizers that do not form sulphur deposits. In the sulphur-storing A. vinosum we identified five sox genes in two independent loci (soxBXA and soxYZ). For SoxA a thiosulphate-dependent induction of expression, above a low constitutive level, was observed. Three sox-encoded proteins were purified: the heterodimeric c-type cytochrome SoxXA, the monomeric SoxB and the heterodimeric SoxYZ. Gene inactivation and complementation experiments proved these proteins to be indispensable for thiosulphate oxidation to sulphate. The intermediary formation of sulphur globules in A. vinosum appears to be related to the lack of soxCD genes, the products of which are proposed to oxidize SoxY-bound sulphane sulphur. In their absence the latter is instead transferred to growing sulphur globules.	2006
1	19535341	Mechanism for the hydrolysis of a sulfur-sulfur bond based on the crystal structure of the thiosulfohydrolase SoxB. Sauvé V, Roversi P, Leath KJ, Garman EF, Antrobus R, Lea SM, Berks BC.	SoxB is an essential component of the bacterial Sox sulfur oxidation pathway. SoxB contains a di-manganese(II) site and is proposed to catalyze the release of sulfate from a protein-bound cysteine S-thiosulfonate. A direct assay for SoxB activity is described. The structure of recombinant Thermus thermophilus SoxB was determined by x-ray crystallography to a resolution of 1.5 A. Structures were also determined for SoxB in complex with the substrate analogue thiosulfate and in complex with the product sulfate. A mechanistic model for SoxB is proposed based on these structures.	2009
2	32457501	A novel bacterial thiosulfate oxidation pathway provides a new clue about the formation of zero-valent sulfur in deep sea. Zhang J, Liu R, Xi S, Cai R, Zhang X, Sun C.	Zero-valent sulfur (ZVS) has been shown to be a major sulfur intermediate in the deep-sea cold seep of the South China Sea based on our previous work, however, the microbial contribution to the formation of ZVS in cold seep has remained unclear. Here, we describe a novel thiosulfate oxidation pathway discovered in the deep-sea cold seep bacterium Erythrobacter flavus 21-3, which provides a new clue about the formation of ZVS. Electronic microscopy, energy-dispersive, and Raman spectra were used to confirm that E. flavus 21-3 effectively converts thiosulfate to ZVS. We next used a combined proteomic and genetic method to identify thiosulfate dehydrogenase (TsdA) and thiosulfohydrolase (SoxB) playing key roles in the conversion of thiosulfate to ZVS. Stoichiometric results of different sulfur intermediates further clarify the function of TsdA in converting thiosulfate to tetrathionate (-O3S-S-S-SO3-), SoxB in liberating sulfone from tetrathionate to form ZVS and sulfur dioxygenases (SdoA/SdoB) in oxidizing ZVS to sulfite under some conditions. Notably, homologs of TsdA, SoxB, and SdoA/SdoB widely exist across the bacteria including in Erythrobacter species derived from different environments. This strongly indicates that this novel thiosulfate oxidation pathway might be frequently used by microbes and plays an important role in the biogeochemical sulfur cycle in nature.	2020

Hensen D , Sperling D , Hans G. Trüper, et al. Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum[J]. Molecular Microbiology, 2006, 62. Falkenby L G , Szymanska M , Holkenbrink C , et al. Quantitative proteomics of Chlorobaculum tepidum: insights into the sulfur metabolism of a phototrophic green sulfur bacterium[J]. Fems Microbiology Letters, 2011, 323(2):142-150.