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EC 1.13.11.76 Details

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EC number

1.13.11.76

Accepted name

2-amino-5-chlorophenol 1,6-dioxygenase

Reaction

2-amino-5-chlorophenol + O₂ = 2-amino-5-chloromuconate 6-semialdehyde

Other name(s)

cnbC (gene name), 2-amino-5-chlorophenol:oxygen 1,6-oxidoreductase (decyclizing)

Systematic name

2-amino-5-chlorophenol:oxygen 1,6-oxidoreductase (ring-opening)

Comment

The enzyme, a member of the nonheme-iron(II)-dependent dioxygenase family, is an extradiol-type dioxygenase that utilizes a non-heme ferrous iron to cleave the aromatic ring at the meta position (relative to the hydroxyl substituent). The enzyme from the bacterium Comamonas testosteroni CNB-1 also has the activity of EC 1.13.11.74, 2-aminophenol 1,6-dioxygenase.

History

created 2013

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)

1.6.8 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

1.9 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)

1.98.1. undefined

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

3.6.1 In phosphorus-containing anhydrides

3.6.2 In sulfonyl-containing anhydrides

3.6.3 Acting on acid anhydrides to catalyse transmembrane movement of substances

3.6.3.1 phospholipid-translocating ATPase

3.6.3.2 Mg²⁺-importing ATPase

3.6.3.3 Cd²⁺-exporting ATPase

3.6.3.4 Cu²⁺-exporting ATPase

3.6.3.5 Zn²⁺-exporting ATPase

3.6.3.6 H⁺-exporting ATPase

3.6.3.7 Na⁺-exporting ATPase

3.6.3.8 Ca²⁺-transporting ATPase

3.6.3.9 Na⁺/K⁺-exchanging ATPase

3.6.3.10 H⁺/K⁺-exchanging ATPase

3.6.3.11 Cl^--transporting ATPase

3.6.3.12 K⁺-transporting ATPase

3.6.3.13 created 2000, deleted 2001

3.6.3.14 H⁺-transporting two-sector ATPase

3.6.3.15 Na⁺-transporting two-sector ATPase

3.6.3.16 arsenite-transporting ATPase

3.6.3.17 monosaccharide-transporting ATPase

3.6.3.18 oligosaccharide-transporting ATPase

3.6.3.19 maltose-transporting ATPase

3.6.3.20 glycerol-3-phosphate-transporting ATPase

3.6.3.21 polar-amino-acid-transporting ATPase

3.6.3.22 nonpolar-amino-acid-transporting ATPase

3.6.3.23 oligopeptide-transporting ATPase

3.6.3.24 nickel-transporting ATPase

3.6.3.25 sulfate-transporting ATPase

3.6.3.26 nitrate-transporting ATPase

3.6.3.27 phosphate-transporting ATPase

3.6.3.28 phosphonate-transporting ATPase

3.6.3.29 molybdate-transporting ATPase

3.6.3.30 Fe³⁺-transporting ATPase

3.6.3.31 polyamine-transporting ATPase

3.6.3.32 quaternary-amine-transporting ATPase

3.6.3.33 vitamin B₁₂-transporting ATPase

3.6.3.34 iron-chelate-transporting ATPase

3.6.3.35 manganese-transporting ATPase

3.6.3.36 taurine-transporting ATPase

3.6.3.37 guanine-transporting ATPase

3.6.3.38 capsular-polysaccharide-transporting ATPase

3.6.3.39 lipopolysaccharide-transporting ATPase

3.6.3.40 teichoic-acid-transporting ATPase

3.6.3.41 heme-transporting ATPase

3.6.3.42 β-glucan-transporting ATPase

3.6.3.43 peptide-transporting ATPase

3.6.3.44 xenobiotic-transporting ATPase

3.6.3.45 steroid-transporting ATPase

3.6.3.46 cadmium-transporting ATPase

3.6.3.47 fatty-acyl-CoA-transporting ATPase

3.6.3.48 α-factor-transporting ATPase

3.6.3.49 channel-conductance-controlling ATPase

3.6.3.50 protein-secreting ATPase

3.6.3.51 mitochondrial protein-transporting ATPase

3.6.3.52 chloroplast protein-transporting ATPase

3.6.3.53 Ag⁺-exporting ATPase

3.6.3.54 Cu⁺-exporting ATPase

3.6.3.55 tungstate-importing ATPase

3.6.4 Acting on acid anhydrides to facilitate cellular and subcellular movement

3.6.5 Acting on GTP to facilitate cellular and subcellular movement

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)