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Literature summary extracted from

  • Low, L.; Ryan Kilmartin, J.; Bernhardt, P.; Kappler, U.
    How are "atypical" sulfite dehydrogenases linked to cell metabolism? Interactions between the sort sulfite dehydrogenase and small redox proteins (2011), Front. Microbiol., 2, 58.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.3.1 expression in Escherichia coli Sinorhizobium meliloti

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.3.1 cytoplasm
-
 Sinorhizobium meliloti 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.3.1 Molybdenum recombinant enzyme contains 0.69 molecules of Mo per protein subunit Sinorhizobium meliloti

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.8.3.1 42669
-
 2 * 42669, mass spectrometry, 2 * 42791, calculated Sinorhizobium meliloti
1.8.3.1 42791
-
 2 * 42669, mass spectrometry, 2 * 42791, calculated Sinorhizobium meliloti
1.8.3.1 71000
-
 gel filtration Sinorhizobium meliloti

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.1 Sinorhizobium meliloti F7X8Y3
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.1 sulfite + cytochrome c substrates horse heart cytochrome c, and recombinant Starkeya novella cytochrome c are only reduced to about 40% while Sinorhizobium meliloti cytochrome c is almost completely reduced. Enzyme interacts with two small redox proteins, a cytochrome c and a Cu containing pseudoazurin, that are encoded in the same operon and are co-transcribed with the sorT gene Sinorhizobium meliloti sulfate + reduced cytochrome c
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.3.1 dimer 2 * 42669, mass spectrometry, 2 * 42791, calculated Sinorhizobium meliloti

Synonyms

EC Number Synonyms Comment Organism
1.8.3.1 SorT
-
 Sinorhizobium meliloti

General Information

EC Number General Information Comment Organism
1.8.3.1 physiological function enzyme is able to couple efficiently to a cytochrome c isolated from the same organism despite being unable to efficiently reduce horse heart cytochrome c. Enzyme interacts with two small redox proteins, a cytochrome c and a Cu containing pseudoazurin, that are encoded in the same operon and are co-transcribed with the sorT gene. The pseudoazurin may act as an intermediate electron shuttle between. The protein system appears to couple directly to the respiratory chain, most likely to a cytochrome oxidase Sinorhizobium meliloti