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Literature summary extracted from

  • Maher, M.J.; Santini, J.; Pickering, I.J.; Prince, R.C.; Macy, J.M.; George, G.N.
    X-ray absorption spectroscopy of selenate reductase (2004), Inorg. Chem., 43, 402-404.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.97.1.9 periplasm
-
 Thauera selenatis
-
-
1.97.1.9 soluble
-
 Thauera selenatis
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.97.1.9 Iron iron-sulfur centre Thauera selenatis
1.97.1.9 Molybdenum Mo-S, Mo=O and Mo-O bound to enzyme Thauera selenatis
1.97.1.9 selenium isolated enzyme contains a reduced form of selenium, probably as selenocysteine Thauera selenatis
1.97.1.9 sulfur iron-sulfur centre Thauera selenatis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.97.1.9 160000
-
-
 Thauera selenatis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.97.1.9 selenate + H2 Thauera selenatis
-
 selenite + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.97.1.9 Thauera selenatis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.97.1.9 selenate + H2
-
 Thauera selenatis selenite + H2O
-
 ?
1.97.1.9 selenate + reduced acceptor
-
 Thauera selenatis selenite + H2O + acceptor
-
 ?

Subunits

EC Number Subunits Comment Organism
1.97.1.9 trimer alpha, beta, gamma Thauera selenatis

Cofactor

EC Number Cofactor Comment Organism Structure
1.97.1.9 cytochrome b
-
 Thauera selenatis
1.97.1.9 molybdopterin
-
 Thauera selenatis