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EC 1.97.1.9 Details

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EC number

1.97.1.9

Accepted name

selenate reductase

Reaction

selenite + H₂O + acceptor = selenate + reduced acceptor

Systematic name

selenite:reduced acceptor oxidoreductase

CAS registry number

146359-71-9

Comment

The periplasmic enzyme from Thauera selenatis is a complex comprising three heterologous subunits (α, β and γ) that contains molybdenum, iron, acid-labile sulfide and heme b as cofactor constituents. Nitrate, nitrite, chlorate and sulfate are not substrates. A number of compounds, including acetate, lactate, pyruvate, and certain sugars, amino acids, fatty acids, di- and tricarboxylic acids, and benzoate can serve as electron donors.

History

created 2003

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.6.1 With NAD⁺ or NADP⁺ as acceptor

1.6.2 With a heme protein as acceptor

1.6.3 With oxygen as acceptor

1.6.4 With a disulfide as acceptor (deleted sub-subclass)

1.6.5 With a quinone or similar compound as acceptor

1.6.6 With a nitrogenous group as acceptor

1.6.7 With an iron-sulfur protein as acceptor (deleted sub-subclass)

1.6.7.1 created 1972, deleted 1978

1.6.7.2 created 1972, deleted 1978

1.6.7.3 created 1978, deleted 1978

1.6.8 With a flavin as acceptor (deleted sub-subclass)

1.6.99 With unknown physiological acceptors

1.6.99.1 NADPH dehydrogenase

1.6.99.2 created 1961 as EC 1.6.5.2, transferred 1965 to EC 1.6.99.2, deleted 2005

1.6.99.3 NADH dehydrogenase

1.6.99.4 created 1965, deleted 1972

1.6.99.5 NADH dehydrogenase (quinone)

1.6.99.6 NADPH dehydrogenase (quinone)

1.6.99.7 created 1972, modified 1981 (EC 1.6.99.10 created 1978, incorporated 1981), deleted 2003

1.6.99.8 created 1972, deleted 2002

1.6.99.9 created 1972, deleted 2002

1.6.99.10 created 1978, deleted 1981

1.6.99.11 created 1989, deleted 2002

1.6.99.12 created 1989, deleted 2002

1.6.99.13 created 1992, deleted 2002

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the other subclasses

1.97.1.1 chlorate reductase

1.97.1.2 pyrogallol hydroxytransferase

1.97.1.3 sulfur reductase

1.97.1.4 [formate-C-acetyltransferase]-activating enzyme

1.97.1.5 created 2000 deleted 2001

1.97.1.6 created 2000 deleted 2001

1.97.1.7 created 2000, deleted 2001

1.97.1.8 tetrachloroethene reductive dehalogenase

1.97.1.9 selenate reductase

1.97.1.10 thyroxine 5′-deiodinase

1.97.1.11 thyroxine 5-deiodinase

1.97.1.12 photosystem I

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

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Release 2023.1 (January 2023)