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Literature summary extracted from

  • Friedrich, C.; Rother, D.; Bardischewsky, F.; Ouentmeier, A.; Fischer, J.
    Oxidation of reduced inorganic sulfur compounds by bacteria emergence of a common mechanism? (2001), Appl. Environ. Microbiol., 67, 2873-2882 .
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.6.20 periplasm
-
 Paracoccus pantotrophus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.6.20 Mn2+ contains Mn2+ Paracoccus pantotrophus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.6.20 [SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O Paracoccus pantotrophus
-
 [SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
 ?
3.1.6.20 [SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O Paracoccus pantotrophus
-
 [SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.2.6 Paracoccus pantotrophus
-
-
-
3.1.6.20 Paracoccus pantotrophus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.6.20 [SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O
-
 Paracoccus pantotrophus [SoxY protein]-S-disulfanyl-L-cysteine + sulfate
-
 ?
3.1.6.20 [SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O
-
 Paracoccus pantotrophus [SoxY protein]-S-sulfanyl-L-cysteine + sulfate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.6.20 monomer
-
 Paracoccus pantotrophus

Synonyms

EC Number Synonyms Comment Organism
1.8.2.6 SoxCD
-
 Paracoccus pantotrophus
3.1.6.20 SoxB
-
 Paracoccus pantotrophus
3.1.6.20 sulfate thiol esterase
-
 Paracoccus pantotrophus

General Information

EC Number General Information Comment Organism
1.8.2.6 physiological function overview on structure and function of the soxXYZABCD gene cluster and comparison with other organisms. The Sox system reconstituted from SoxXA, SoxYZ, SoxB, and SoxCD mediates thiosulfate-, sulfite-, sulfur-, and hydrogen sulfide-dependent cytochrome c reduction. SoxCD acts as a dehydrogenase at a protein-bound sulfur atom Paracoccus pantotrophus