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EC 1.1.98.7 Details

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EC number

1.1.98.7

Accepted name

serine-type anaerobic sulfatase-maturating enzyme

Reaction

S-adenosyl-L-methionine + a [sulfatase]-L-serine = a [sulfatase]-3-oxo-L-alanine + 5′-deoxyadenosine + L-methionine

Other name(s)

atsB (gene name)

Systematic name

[sulfatase]-L-serine:S-adenosyl-L-methionine oxidoreductase (3-oxo-L-alanine-forming)

Comment

A bacterial radical S-adenosyl-L-methionine (AdoMet) enzyme that contains three [4Fe-4S] clusters. The enzyme, found in some bacteria, activates a type I sulfatase enzyme (EC 3.1.6.1) by converting a conserved L-serine residue in the active site to a unique 3-oxo-L-alanine residue that is essential for the sulfatase activity. While the enzyme from Klebsiella pneumoniae is specific for L-serine, the enzyme from Clostridium perfringens can also act on L-cysteine, see EC 1.8.98.7, cysteine-type anaerobic sulfatase-maturating enzyme.

History

created 2020

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

1.1.4 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

1.1.98.1 alcohol dehydrogenase (azurin)

1.1.98.2 glucose-6-phosphate dehydrogenase (coenzyme-F₄₂₀)

1.1.98.3 decaprenylphospho-β-D-ribofuranose 2-dehydrogenase

1.1.98.4 F₄₂₀H₂:quinone oxidoreductase

1.1.98.5 secondary-alcohol dehydrogenase (coenzyme-F₄₂₀)

1.1.98.6 ribonucleoside-triphosphate reductase (formate)

1.1.98.7 serine-type anaerobic sulfatase-maturating enzyme

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

1.5.1 With NAD⁺ or NADP⁺ as acceptor

1.5.1.1 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H]

1.5.1.2 pyrroline-5-carboxylate reductase

1.5.1.3 dihydrofolate reductase

1.5.1.4 created 1961, deleted 1976

1.5.1.5 methylenetetrahydrofolate dehydrogenase (NADP⁺)

1.5.1.6 formyltetrahydrofolate dehydrogenase

1.5.1.7 saccharopine dehydrogenase (NAD⁺, L-lysine-forming)

1.5.1.8 saccharopine dehydrogenase (NADP⁺, L-lysine-forming)

1.5.1.9 saccharopine dehydrogenase (NAD⁺, L-glutamate-forming)

1.5.1.10 saccharopine dehydrogenase (NADP⁺, L-glutamate-forming)

1.5.1.11 D-octopine dehydrogenase

1.5.1.12 1-pyrroline-5-carboxylate dehydrogenase

1.5.1.13 created 1972, deleted 2004

1.5.1.14 created 1976, deleted 1989

1.5.1.15 methylenetetrahydrofolate dehydrogenase (NAD⁺)

1.5.1.16 D-lysopine dehydrogenase

1.5.1.17 alanopine dehydrogenase

1.5.1.18 ephedrine dehydrogenase

1.5.1.19 D-nopaline dehydrogenase

1.5.1.20 methylenetetrahydrofolate reductase [NAD(P)H]

1.5.1.21 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH)

1.5.1.22 strombine dehydrogenase

1.5.1.23 tauropine dehydrogenase

1.5.1.24 N⁵-(carboxyethyl)ornithine synthase

1.5.1.25 thiomorpholine-carboxylate dehydrogenase

1.5.1.26 β-alanopine dehydrogenase

1.5.1.27 1,2-dehydroreticulinium reductase (NADPH)

1.5.1.28 opine dehydrogenase

1.5.1.29 FMN reductase [NAD(P)H]

1.5.1.30 flavin reductase (NADPH)

1.5.1.31 berberine reductase

1.5.1.32 vomilenine reductase

1.5.1.33 pteridine reductase

1.5.1.34 6,7-dihydropteridine reductase

1.5.1.35 1-pyrroline dehydrogenase

1.5.1.36 flavin reductase (NADH)

1.5.1.37 FAD reductase (NADH)

1.5.1.38 FMN reductase (NADPH)

1.5.1.39 FMN reductase [NAD(P)H]

1.5.1.40 8-hydroxy-5-deazaflavin:NADPH oxidoreductase

1.5.1.41 riboflavin reductase [NAD(P)H]

1.5.1.42 FMN reductase (NADH)

1.5.1.43 carboxynorspermidine synthase

1.5.1.44 festuclavine dehydrogenase

1.5.1.45 FAD reductase [NAD(P)H]

1.5.1.46 agroclavine dehydrogenase

1.5.1.47 dihydromethanopterin reductase [NAD(P)⁺]

1.5.1.48 2-methyl-1-pyrroline reductase

1.5.1.49 1-pyrroline-2-carboxylate reductase [NAD(P)H]

1.5.1.50 dihydromonapterin reductase

1.5.1.51 N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase

1.5.1.52 staphylopine dehydrogenase

1.5.1.53 methylenetetrahydrofolate reductase (NADPH)

1.5.1.54 methylenetetrahydrofolate reductase (NADH)

1.5.3 With oxygen as acceptor

1.5.3.1 sarcosine oxidase (formaldehyde-forming)

1.5.3.2 N-methyl-L-amino-acid oxidase

1.5.3.3 created 1961, deleted 1972

1.5.3.4 N⁶-methyl-lysine oxidase

1.5.3.5 (S)-6-hydroxynicotine oxidase

1.5.3.6 (R)-6-hydroxynicotine oxidase

1.5.3.7 L-pipecolate oxidase

1.5.3.8 created 1989, deleted 1992

1.5.3.9 created 1989, modified 1999, deleted 2002

1.5.3.10 dimethylglycine oxidase

1.5.3.11 polyamine oxidase

1.5.3.12 dihydrobenzophenanthridine oxidase

1.5.3.13 N¹-acetylpolyamine oxidase

1.5.3.14 polyamine oxidase (propane-1,3-diamine-forming)

1.5.3.15 N⁸-acetylspermidine oxidase (propane-1,3-diamine-forming)

1.5.3.16 spermine oxidase

1.5.3.17 non-specific polyamine oxidase

1.5.3.18 L-saccharopine oxidase

1.5.3.19 4-methylaminobutanoate oxidase (formaldehyde-forming)

1.5.3.20 N-alkylglycine oxidase

1.5.3.21 4-methylaminobutanoate oxidase (methylamine-forming)

1.5.3.22 coenzyme F₄₂₀H₂ oxidase

1.5.3.23 glyphosate oxidoreductase

1.5.3.24 sarcosine oxidase (5,10-methylenetetrahydrofolate-forming)

1.5.3.25 fructosyl amine oxidase (glucosone-forming)

1.5.3.26 fructosyl amine oxidase (fructosamine-forming)

1.5.4 With a disulfide as acceptor

1.5.5 With a quinone or similar compound as acceptor

1.5.7 With an iron-sulfur protein as acceptor

1.5.8 With a flavin or flavoprotein as acceptor

1.5.98 With other, known, physiological acceptors

1.5.99 With unknown physiological acceptors

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

1.11 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)

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Release 2023.1 (January 2023)