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Information on EC 3.1.6.20 - S-sulfosulfanyl-L-cysteine sulfohydrolase
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3.1.6.20 S-sulfosulfanyl-L-cysteine sulfohydrolaseIUBMB Comments
Contains Mn2+. The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate. It catalyses two reactions in the pathway. In both cases the enzyme hydrolyses a sulfonate moiety that is bound (either directly or via a sulfane) to a cysteine residue of a SoxY protein, releasing sulfate. The enzyme from Paracoccus pantotrophus contains a pyroglutamate (cycloglutamate) at its N-terminus.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
[SoxY protein]-S-sulfosulfanyl-L-cysteine
+
=
[SoxY protein]-S-sulfanyl-L-cysteine
+
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine
+
=
[SoxY protein]-S-disulfanyl-L-cysteine
+
Synonyms
thiosulfohydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SoxB
sulfate thiol esterase
SoxB
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O = [SoxY protein]-S-disulfanyl-L-cysteine + sulfate
(2)
-
-
-
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O = [SoxY protein]-S-sulfanyl-L-cysteine + sulfate
(1)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
[SoxY protein]-S-sulfosulfanyl-L-cysteine sulfohydrolase
Contains Mn2+. The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate. It catalyses two reactions in the pathway. In both cases the enzyme hydrolyses a sulfonate moiety that is bound (either directly or via a sulfane) to a cysteine residue of a SoxY protein, releasing sulfate. The enzyme from Paracoccus pantotrophus contains a pyroglutamate (cycloglutamate) at its N-terminus.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
[SoxYZ protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxYZ protein]-S-disulfanyl-L-cysteine + sulfate
[SoxYZ protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxYZ protein]-S-sulfanyl-L-cysteine + sulfate
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
Allochromatium vinosum DSM180T
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
Allochromatium vinosum DSM180T
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxYZ protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxYZ protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxYZ protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxYZ protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxYZ protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxYZ protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxYZ protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxYZ protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxYZ protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxYZ protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxYZ protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxYZ protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
[SoxYZ protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxYZ protein]-S-disulfanyl-L-cysteine + sulfate
[SoxYZ protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxYZ protein]-S-sulfanyl-L-cysteine + sulfate
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
Allochromatium vinosum DSM180T
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
Allochromatium vinosum DSM180T
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
?
[SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxYZ protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxYZ protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxYZ protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxYZ protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxYZ protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
[SoxYZ protein]-S-disulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxYZ protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxYZ protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxYZ protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxYZ protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
[SoxYZ protein]-S-sulfosulfanyl-L-cysteine + H2O
[SoxYZ protein]-S-sulfanyl-L-cysteine + sulfate
-
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). P72177_PARDE
564
0
61909
TrEMBL
other Location (Reliability: 2)
Q72IT0_THET2
Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
573
0
63890
TrEMBL
-
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with thiosulfate and sulfate, sitting drop vapor diffusion method, using 25% (w/v) PEG 400 as precipitant
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and Hitrap pheny lcolumn chromatography
-
phenyl Sepharose column chromatography, MonoQ column chromatography, and Superdex 200 gel filtration
Q Sepharose column chromatography, phenyl Sepharose column chromatography, and Sephacryl S-200 gel filtration
-
Strep-Tactin Superflow column chromatography and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the enzyme gene is used as a marker for detection of sulfur-oxidizing bacteria in coastal sediments
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Friedrich, C.; Rother, D.; Bardischewsky, F.; Ouentmeier, A.; Fischer, J.
Oxidation of reduced inorganic sulfur compounds by bacteria emergence of a common mechanism?
Appl. Environ. Microbiol.
67
2873-2882
2001
Paracoccus pantotrophus
brenda
Alam, M.; Pyne, P.; Mazumdar, A.; Peketi, A.; Ghosh, W.
Kinetic enrichment of 34S during proteobacterial thiosulfate oxidation and the conserved role of SoxB in S-S bond breaking
Appl. Environ. Microbiol.
79
4455-4464
2013
Advenella kashmirensis, Hydrogenovibrio crunogenus, Paracoccus pantotrophus
brenda
Krishnani, K.; Gopikrishna, G.; Pillai, S.; Gupta, B.
Abundance of sulphur-oxidizing bacteria in coastal aquaculture using soxB gene analyses
Aquac. Res.
41
1290-1301
2010
uncultured bacterium
-
brenda
Quentmeier, A.; Hellwig, P.; Bardischewsky, F.; Grelle, G.; Kraft, R.; Friedrich, C.
Sulfur oxidation in Paracoccus pantotrophus Interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB protein
Biochem. Biophys. Res. Commun.
312
1011-1018
2003
Paracoccus pantotrophus
brenda
Bagchi, A.; Ghosh, T.
A structural study towards the understanding of the interactions of SoxY, SoxZ, and SoxB, leading to the oxidation of sulfur anions via the novel global sulfur oxidizing (sox) operon
Biochem. Biophys. Res. Commun.
335
609-615
2005
Paracoccus pantotrophus
brenda
Quentmeier, A.; Friedrich, C.
The cysteine residue of the SoxY protein as the active site of protein-bound sulfur oxidation of Paracoccus pantotrophus GB17
FEBS Lett.
503
168-172
2001
Paracoccus pantotrophus, Paracoccus pantotrophus GB17
brenda
Tourova, T.; Slobodova, N.; Bumazhkin, B.; Kolganova, T.; Muyzer, G.; Sorokin, D.
Analysis of community composition of sulfur-oxidizing bacteria in hypersaline and soda lakes using soxB as a functional molecular marker
FEMS Microbiol. Ecol.
84
280-289
2013
Thioalkalivibrio nitratireducens, Thiohalophilus thiocyanatoxydans, Halothiobacillus sp., Thioalkalivibrio paradoxus, Roseinatronobacter thiooxidans, Thiohalorhabdus denitrificans, Thiohalomonas denitrificans, Thiohalobacter thiocyanaticus, Thioalkalivibrio nitratis, Thioalkalivibrio thiocyanoxidans, Thioalkalivibrio versutus, Thioalkalivibrio denitrificans, Thioalkalivibrio halophilus, Thioalkalivibrio jannaschii, Thioalkalibacter halophilus, Ectothiorhodosinus mongolicus
brenda
Petri, R.; Podgorsek, L.; Imhoff, J.
Phylogeny and distribution of the soxB gene among thiosulfate-oxidizing bacteria
FEMS Microbiol. Lett.
197
171-178
2001
Aquifex aeolicus, Chlorobaculum thiosulfatiphilum, Chlorobaculum tepidum, Prosthecochloris vibrioformis f. thiosulfatophilum, Paracoccus pantotrophus, Rhodopseudomonas palustris, Starkeya novella, Halothiobacillus neapolitanus, Thiobacillus thioparus, Paracoccus versutus, Marinobacter sp., Pelodictyon phaeoclathratiforme, Guyparkeria hydrothermalis, Hydrogenovibrio crunogenus, alpha proteobacterium HY-103, Chlorobaculum tepidum ATCC 49652, Rhodopseudomonas palustris CGA 009, Chlorobaculum thiosulfatiphilum DSM 249T, Paracoccus pantotrophus GB 17, Prosthecochloris vibrioformis f. thiosulfatophilum DSM 265, Halothiobacillus neapolitanus DSM 581T, Marinobacter sp. DS 40M8, Guyparkeria hydrothermalis DSM 7121, Hydrogenovibrio crunogenus HY-62, Paracoccus versutus DSM 582T, Pelodictyon phaeoclathratiforme DSM 5477, Starkeya novella DSM 506T, Marinobacter sp. HY-106, Thiobacillus thioparus DSM 505T
brenda
Wodara, C.; Kostka, S.; Egert, M.; Kelly, D.; Friedrich, C.
Identification and sequence analysis of the soxB gene essential for sulfur oxidation of Paracoccus denitrificans GB17
J. Bacteriol.
176
6188-6191
1994
Paracoccus denitrificans (P72177), Paracoccus denitrificans GB17 (P72177)
brenda
Friedrich, C.G.; Quentmeier, A.; Bardischewsky, F.; Rother, D.; Kraft, R.; Kostka, S.; Prinz, H.
Novel genes coding for lithotrophic sulfur oxidation of Paracoccus pantotrophus GB17
J. Bacteriol.
182
4677-4687
2000
Paracoccus pantotrophus, Paracoccus pantotrophus GB17
brenda
Sauve, V.; Roversi, P.; Leath, K.; Garman, E.; Antrobus, R.; Lea, S.; Berks, B.
Mechanism for the hydrolysis of a sulfur-sulfur bond based on the crystal structure of the thiosulfohydrolase SoxB
J. Biol. Chem.
284
21707-21718
2009
Thermus thermophilus (Q72IT0), Thermus thermophilus
brenda
Epel, B.; Schfer, K.; Quentmeier, A.; Friedrich, C.; Lubitz, W.
Multifrequency EPR analysis of the dimanganese cluster of the putative sulfate thiohydrolase SoxB of Paracoccus pantotrophus
J. Biol. Inorg. Chem.
10
636-642
2005
Paracoccus pantotrophus
brenda
Hensen, D.; Sperling, D.; Trueper, H.G.; Brune, D.C.; Dahl, C.
Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum
Mol. Microbiol.
62
794-810
2006
Allochromatium vinosum (Q1W3E6), Allochromatium vinosum DSM180T (Q1W3E6)
brenda
Grabarczyk, D.; Berks, B.
Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ
PLoS ONE
12
e0173395
2017
Thermus thermophilus
brenda
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