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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

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.2 With a cytochrome as acceptor

1.1.3 With oxygen as acceptor

1.1.3.1 created 1961, deleted 1984

1.1.3.2 L-lactate oxidase

1.1.3.3 malate oxidase

1.1.3.4 glucose oxidase

1.1.3.5 hexose oxidase

1.1.3.6 cholesterol oxidase

1.1.3.7 aryl-alcohol oxidase

1.1.3.8 L-gulonolactone oxidase

1.1.3.9 galactose oxidase

1.1.3.10 pyranose oxidase

1.1.3.11 L-sorbose oxidase

1.1.3.12 pyridoxine 4-oxidase

1.1.3.13 alcohol oxidase

1.1.3.14 catechol oxidase (dimerizing)

1.1.3.15 (S)-2-hydroxy-acid oxidase

1.1.3.16 ecdysone oxidase

1.1.3.17 choline oxidase

1.1.3.18 secondary-alcohol oxidase

1.1.3.19 4-hydroxymandelate oxidase (decarboxylating)

1.1.3.20 long-chain-alcohol oxidase

1.1.3.21 glycerol-3-phosphate oxidase

1.1.3.22 created 1961 as EC 1.2.3.2, transferred 1984 to EC 1.1.3.22, modified 1989, deleted 2004

1.1.3.23 thiamine oxidase

1.1.3.24 L-galactonolactone oxidase

1.1.3.25 created 1986, deleted 2005

1.1.3.26 created 1989, deleted 2002

1.1.3.27 hydroxyphytanate oxidase

1.1.3.28 nucleoside oxidase

1.1.3.29 N-acylhexosamine oxidase

1.1.3.30 polyvinyl-alcohol oxidase

1.1.3.31 created 1992, deleted 2003

1.1.3.32 created 1999, deleted 2002

1.1.3.33 created 1999, deleted 2002

1.1.3.34 created 1999, deleted 2002

1.1.3.35 created 1999, deleted 2002

1.1.3.36 created 1999, deleted 2002

1.1.3.37 D-arabinono-1,4-lactone oxidase

1.1.3.38 vanillyl-alcohol oxidase

1.1.3.39 nucleoside oxidase (H₂O₂-forming)

1.1.3.40 D-mannitol oxidase

1.1.3.41 alditol oxidase

1.1.3.42 prosolanapyrone-II oxidase

1.1.3.43 paromamine 6′-oxidase

1.1.3.44 6′′′-hydroxyneomycin C oxidase

1.1.3.45 aclacinomycin-N oxidase

1.1.3.46 4-hydroxymandelate oxidase

1.1.3.47 5-(hydroxymethyl)furfural oxidase

1.1.3.48 3-deoxy-α-D-manno-octulosonate 8-oxidase

1.1.3.49 (R)-mandelonitrile oxidase

1.1.3.50 C-glycoside oxidase

1.1.4 With a disulfide as acceptor

1.1.5 With a quinone or similar compound as acceptor

1.1.7 With an iron-sulfur protein as acceptor

1.1.9 With a copper protein as acceptor

1.1.98 With other, known, physiological acceptors

1.1.99 With unknown physiological acceptors

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)

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

1.6.99 With unknown physiological acceptors

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.8.1 With NAD⁺ or NADP⁺ as acceptor

1.8.2 With a cytochrome as acceptor

1.8.3 With oxygen as acceptor

1.8.4 With a disulfide as acceptor

1.8.5 With a quinone or similar compound as acceptor

1.8.6 With a nitrogenous group as acceptor (deleted sub-subclass)

1.8.7 With an iron-sulfur protein as acceptor

1.8.98 With other, known, physiological acceptors

1.8.98.1 dihydromethanophenazine:CoB-CoM heterodisulfide reductase

1.8.98.2 sulfiredoxin

1.8.98.3 sulfite reductase (coenzyme F₄₂₀)

1.8.98.4 coenzyme F₄₂₀:CoB-CoM heterodisulfide,ferredoxin reductase

1.8.98.5 H₂:CoB-CoM heterodisulfide,ferredoxin reductase

1.8.98.6 formate:CoB-CoM heterodisulfide,ferredoxin reductase

1.8.98.7 cysteine-type anaerobic sulfatase-maturating enzyme

1.8.99 With unknown physiological acceptors

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

1.98 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)