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EC 1.8.98.1 Details

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EC number

1.8.98.1

Accepted name

dihydromethanophenazine:CoB-CoM heterodisulfide reductase

Reaction

CoB + CoM + methanophenazine = CoM-S-S-CoB + dihydromethanophenazine

Other name(s)

hdrDE (gene names), CoB—CoM heterodisulfide reductase (ambiguous), heterodisulfide reductase (ambiguous), coenzyme B:coenzyme M:methanophenazine oxidoreductase

Systematic name

CoB:CoM:methanophenazine oxidoreductase

Comment

This enzyme, found in methanogenic archaea that belong to the Methanosarcinales order, regenerates CoM and CoB after the action of EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase. It is a membrane-bound enzyme that contains (per heterodimeric unit) two distinct b-type hemes and two [4Fe-4S] clusters. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.5, H₂:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase and EC 1.8.98.4, coenzyme F₄₂₀:CoB-CoM heterodisulfide,ferredoxin reductase.

History

created 2003, modified 2017

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

1.3.1 With NAD⁺ or NADP⁺ as acceptor

1.3.2 With a cytochrome as acceptor

1.3.3 With oxygen as acceptor

1.3.4 With a disulfide as acceptor

1.3.5 With a quinone or related compound as acceptor

1.3.7 With an iron-sulfur protein as acceptor

1.3.8 With a flavin as acceptor

1.3.98 With other, known, physiological acceptors

1.3.99 With unknown physiological acceptors

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

1.7 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

1.10.1 With NAD⁺ or NADP⁺ as acceptor

1.10.2 With a cytochrome as acceptor

1.10.3 With oxygen as acceptor

1.10.3.1 catechol oxidase

1.10.3.2 laccase

1.10.3.3 L-ascorbate oxidase

1.10.3.4 o-aminophenol oxidase

1.10.3.5 3-hydroxyanthranilate oxidase

1.10.3.6 rifamycin-B oxidase

1.10.3.7 created 1986, deleted 2002

1.10.3.8 created 1986, deleted 2002

1.10.3.9 photosystem II

1.10.3.10 ubiquinol oxidase (H⁺-transporting)

1.10.3.11 ubiquinol oxidase (non-electrogenic)

1.10.3.12 menaquinol oxidase (H⁺-transporting)

1.10.3.13 caldariellaquinol oxidase (H⁺-transporting)

1.10.3.14 ubiquinol oxidase (electrogenic, non H⁺-transporting)

1.10.3.15 grixazone synthase

1.10.3.16 dihydrophenazinedicarboxylate synthase

1.10.3.17 superoxide oxidase

1.10.5 With a quinone or related compound as acceptor

1.10.9 With a copper protein as acceptor

1.10.99 With unknown physiological acceptors

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

1.15.1 Acting on superoxide as acceptor (only sub-subclass identified to date)

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

1.22 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

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

3.1 Acting on ester bonds

3.2 Glycosylases

3.3 Acting on ether bonds

3.4 Acting on peptide bonds (peptidases)

3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

3.6 Acting on acid anhydrides

3.7 Acting on carbon-carbon bonds

3.8 Acting on halide bonds

3.9 Acting on phosphorus-nitrogen bonds

3.10 Acting on sulfur-nitrogen bonds

3.11 Acting on carbon-phosphorus bonds

3.12 Acting on sulfur-sulfur bonds

3.13 Acting on carbon-sulfur bonds

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Release 2023.1 (January 2023)