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CATH Superfamily 3.90.380.10

Naphthalene 1,2-dioxygenase Alpha Subunit; Chain A, domain 1

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Naphthalene 1,2-dioxygenase Alpha Subunit; Chain A, domain 1
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 26 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
3-phenylpropanoate dioxygenase. [EC: 1.14.12.19]
(1) 3-phenylpropanoate + NADH + O(2) = 3-(cis-5,6-dihydroxycyclohexa-1,3- dien-1-yl)propanoate + NAD(+). (2) (2E)-3-phenylprop-2-enoate + NADH + O(2) = (2E)-3-(2,3- dihydroxyphenyl)prop-2-enoate + NAD(+).
  • This enzyme catalyzes a step in the pathway of phenylpropanoid compounds degradation.
  • It catalyzes the insertion of both atoms of molecular oxygen into positions 2 and 3 of the phenyl ring of 3-phenylpropanoate or (2E)-3- phenylprop-2-enoate.
 122 A0A023Z0X1 A0A025CJ25 A0A026UK62 A0A028ASE5 A0A028E2L6 A0A069XNL2 A0A070FHC7 A0A070SU90 A0A070VB08 A0A073G524
(112 more...)
Carnitine monooxygenase. [EC: 1.14.13.239]
L-carnitine + NAD(P)H + O(2) = (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD(P)(+) + H(2)O.
  • The bacterial enzyme is a complex consisting of a reductase and an oxygenase components.
  • The reductase subunit contains a flavin and a plant-type ferredoxin [2Fe-2S] cluster, while the oxygenase subunit is a Rieske-type protein in which a [2Fe-2S] cluster is coordinated by two histidine and two cysteine residues.
 99 A0A009G9U2 A0A009N509 A0A010K8M8 A0A010W838 A0A011KSN1 A0A013T0T2 A0A013U0N1 A0A022J5N0 A0A022KIN6 A0A026V537
(89 more...)
3-ketosteroid 9-alpha-monooxygenase. [EC: 1.14.15.30]
Androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = 9-alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O.
  • The enzyme is involved in the cholesterol degradation pathway of several bacterial pathogens, such as Mycobacterium tuberculosis.
  • It forms a two-component system with a ferredoxin reductase (KshB).
  • The enzyme contains a Rieske-type iron-sulfur center and non-heme iron.
  • The product of the enzyme is unstable, and spontaneously converts to 3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione.
  • Formerly EC 1.14.13.142.
 20 A0A045KFG6 A0A0H3LG39 A0A0H3MBE7 A0A109SSQ0 A0A120IQJ6 A0A120J384 A0A1R3Y4D7 A0A1X7KNK5 A0A2U9PYD3 A0A328G4I5
(10 more...)
Naphthalene 1,2-dioxygenase. [EC: 1.14.12.12]
Naphthalene + NADH + O(2) = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + NAD(+).
  • Comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC 1.18.1.3), an iron-sulfur oxygenase, and ferredoxin.
 12 A0A010RDK6 A0A1H4ID50 A0A1Y0BCH8 O07824 O52382 P0A110 P0A111 Q05K20 Q05K30 Q51494
(2 more...)
Choline monooxygenase. [EC: 1.14.15.7]
Choline + O(2) + 2 reduced ferredoxin + 2 H(+) = betaine aldehyde hydrate + H(2)O + 2 oxidized ferredoxin.
  • Catalyzes the first step of glycine betaine synthesis.
  • In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine.
  • Different enzymes are involved in the first reaction.
  • In plants, the reaction is catalyzed by this enzyme whereas in animals and many bacteria, it is catalyzed by either membrane-bound EC 1.1.99.1 or soluble EC 1.1.3.17.
  • The enzyme involved in the second step, EC 1.2.1.8, appears to be the same in plants, animals and bacteria.
  • In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 and EC 2.1.1.157.
  • Formerly EC 1.14.14.4.
 11 A0A0K9QHB2 A0A0K9QHB2 O04121 O04121 O22553 O22553 Q93XE1 Q93XE1 Q9LKN0 Q9SZR0
(1 more...)
Chlorophyllide a oxygenase. [EC: 1.14.13.122]
Chlorophyllide a + 2 O(2) + 2 NADPH = chlorophyllide b + 3 H(2)O + 2 NADP(+).
  • Catalyzes two successive hydroxylations at the 7-methyl group of chlorophyllide a.
  • The second step yields the aldehyde hydrate, which loses H(2)O spontaneously to form chlorophyllide b.
  • Chlorophyll a and protochlorophyllide a are not substrates.
  • Formerly EC 1.13.12.14.
 7 A0A178W6L1 A8HMS2 B8BIB7 Q8S7E1 Q9MBA1 Q9XJ38 Q9ZWM5
Biphenyl 2,3-dioxygenase. [EC: 1.14.12.18]
Biphenyl + NADH + O(2) = (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD(+).
  • The enzyme from Burkholderia fungorum strain LB400 (previously Pseudomonas sp.) is part of a multicomponent system composed of an NADH:ferredoxin oxidoreductase (FAD cofactor), a [2Fe-2S] Rieske-type ferredoxin, and a terminal oxygenase that contains a [2Fe-2S] Rieske- type iron-sulfur cluster and a catalytic mononuclear nonheme iron center.
  • Chlorine-substituted biphenyls can also act as substrates.
  • Similar to the three-component enzyme systems EC 1.14.12.3 and EC 1.14.12.11.
 6 D3WHI7 P37333 Q46372 Q52028 Q52438 Q53122
Benzene 1,2-dioxygenase. [EC: 1.14.12.3]
Benzene + NADH + O(2) = cis-cyclohexa-3,5-diene-1,2-diol + NAD(+).
  • A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), an iron-sulfur oxygenase and ferredoxin.
 6 A5W4F2 I7B4T5 P0C618 Q07944 Q3LWS6 V9UYT7
7-methylxanthine demethylase. [EC: 1.14.13.128]
7-methylxanthine + O(2) + NAD(P)H = xanthine + NAD(P)(+) + H(2)O + formaldehyde.
  • NADH is the preferred cofactor.
  • Part of the caffeine degradation pathway in Pseudomonas putida.
 6 A0A177YCG1 A0A2S5I346 A0A2V4JJZ4 A0A427H683 F0E1K6 V7D3M9
Anthranilate 1,2-dioxygenase (deaminating, decarboxylating). [EC: 1.14.12.1]
Anthranilate + NAD(P)H + O(2) = catechol + CO(2) + NAD(P)(+) + NH(3).
    		 5 A0A124U544 A0A2D7VDY6 I2DU94 O85673 Q84BZ3
    Toluene dioxygenase. [EC: 1.14.12.11]
    Toluene + NADH + O(2) = (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD(+).
    • A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), an iron-sulfur oxygenase, and a ferredoxin.
    • Some other aromatic compounds, including ethylbenzene, 4-xylene and some halogenated toluenes, are converted into the corresponding cis- dihydrodiols.
    		 5 A5W4F2 I7B4T5 P0C618 Q3LWS6 V9UYT7
    Carbazole 1,9a-dioxygenase. [EC: 1.14.12.22]
    9H-carbazole + NAD(P)H + O(2) = 2'-aminobiphenyl-2,3-diol + NAD(P)(+).
    • This enzyme catalyzes the first reaction in the pathway of carbazole degradation.
    • The enzyme attacks at the 1 and 9a positions of carbazole, resulting in the formation of a highly unstable hemiaminal intermediate that undergoes a spontaneous cleavage and rearomatization, resulting in 2'-aminobiphenyl-2,3-diol.
    • In most bacteria the enzyme is a complex composed of a terminal oxygenase, a ferredoxin, and a ferredoxin reductase.
    • The terminal oxygenase component contains a nonheme iron center and a Rieske [2Fe-2S] iron-sulfur cluster.
    		 5 B7XGE8 D5IGG0 O34807 Q8G8B6 S6AKJ2
    Terephthalate 1,2-dioxygenase. [EC: 1.14.12.15]
    Terephthalate + NADH + O(2) = (1R,6S)-dihydroxycyclohexa-2,4-diene-1,4- dicarboxylate + NAD(+).
    • In Comamonas testoteroni, contains a Rieske [2Fe-2S] center.
    		 5 A0A096FF41 A0A0M2DH63 A0A0M2DI65 Q3C1D5 Q3C1E3
    P-cumate 2,3-dioxygenase. [EC: 1.14.12.25]
    p-cumate + NADH + O(2) = (2R,3S)-2,3-dihydroxy-2,3-dihydro-p-cumate + NAD(+).
    • The enzyme, characterized from several Pseudomonas strains, is involved in the degradation of p-cymene and p-cumate.
    • It comprises four components: a ferredoxin, a ferredoxin reductase, and two subunits of a catalytic component.
    • The enzyme can also act on indole, transforming it to the water- insoluble blue dye indigo.
    		 4 A5W4G8 I7C0Z7 Q51974 V9UYS2
    Methylxanthine N(1)-demethylase. [EC: 1.14.13.178]
    (1) Caffeine + O(2) + NAD(P)H = theobromine + NAD(P)(+) + H(2)O + formaldehyde. (2) Theophylline + O(2) + NAD(P)H = 3-methylxanthine + NAD(P)(+) + H(2)O + formaldehyde. (3) Paraxanthine + O(2) + NAD(P)H = 7-methylxanthine + NAD(P)(+) + H(2)O + formaldehyde.
    • The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.179, and has a 5-fold higher activity with NADH than with NADPH.
    • Also demethylate 1-methylxantine with lower efficiency.
    • Forms part of the degradation pathway of methylxanthines.
    		 2 A0A0M3CP22 H9N289
    Vanillate monooxygenase. [EC: 1.14.13.82]
    Vanillate + O(2) + NADH = 3,4-dihydroxybenzoate + NAD(+) + H(2)O + formaldehyde.
    • Forms part of the vanillin degradation pathway in Arthrobacter sp.
    • Formerly EC 1.2.3.12.
    		 2 O05616 P12609
    Methylxanthine N(3)-demethylase. [EC: 1.14.13.179]
    (1) Theobromine + O(2) + NAD(P)H = 7-methylxanthine + NAD(P)(+) + H(2)O + formaldehyde. (2) 3-methylxanthine + O(2) + NAD(P)H = xanthine + NAD(P)(+) + H(2)O + formaldehyde.
    • The enzyme from the bacterium Pseudomonas putida shares an NAD(P)H-FMN reductase subunit with EC 1.14.13.178, and has higher activity with NADH than with NADPH.
    • Also demethylates caffeine and theophylline with lower efficiency.
    • Forms part of the degradation pathway of methylxanthines.
    		 2 A0A0M3CMC5 H9N290
    Benzoate 1,2-dioxygenase. [EC: 1.14.12.10]
    Benzoate + NADH + O(2) = (1R,6S)-1,6-dihydroxycyclohexa-2,4-diene-1- carboxylate + NAD(+).
    • A system, containing a reductase which is an iron-sulfur flavoprotein (FAD), and an iron-sulfur oxygenase.
    • Formerly EC 1.13.99.2.
    		 2 A0A2D7V885 P07769
    Pheophorbide a oxygenase. [EC: 1.14.15.17]
    Pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster.
    • This enzyme catalyzes a key reaction in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants.
    • The enzyme from Arabidopsis contains a Rieske-type iron-sulfur cluster and requires reduced ferredoxin, which is generated either by NADPH through the pentose-phosphate pathway or by the action of photosystem I.
    • While still attached to this enzyme, the product is rapidly converted into primary fluorescent chlorophyll catabolite by the action of EC 1.3.7.12.
    • Pheophorbide b acts as an inhibitor.
    • In (18)O(2) labelling experiments, only the aldehyde oxygen is labelled, suggesting that the other oxygen atom may originate from H(2)O.
    • Formerly EC 1.14.12.20.
    		 1 Q9FYC2
    Methanesulfonate monooxygenase (NADH). [EC: 1.14.13.111]
    Methanesulfonate + NADH + O(2) = formaldehyde + NAD(+) + sulfite + H(2)O.
    • Methanesulfonate is the simplest of the sulfonates and is a substrate for the growth of certain methylotrophic microorganisms.
    • Compared with EC 1.14.14.5, this enzyme has a restricted substrate range that includes only the short-chain aliphatic sulfonates (methanesulfonate to butanesulfonate) and excludes all larger molecules, such as arylsulfonates.
    • The enzyme from the bacterium Methylosulfonomonas methylovora is a multicomponent system comprising an hydroxylase, a reductase (MsmD) and a ferredoxin (MsmC).
    • The hydroxylase has both large (MsmA) and small (MsmB) subunits, with each large subunit containing a Rieske-type [2Fe-2S] cluster.
    • Formerly EC 1.14.14.6.
    		 1 Q9X404
    Chloroacetanilide N-alkylformylase. [EC: 1.14.15.23]
    Butachlor + 2 reduced ferredoxin [iron-sulfur] cluster + O(2) = 2-chloro- N-(2,6-diethylphenyl)acetamide + butyl formate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O.
    • The enzyme, characterized from the bacterium Sphingomonas sp. DC-6, initiates the degradation of several chloroacetanilide herbicides, including alachlor, acetochlor, and butachlor.
    • The enzyme is a Rieske non-heme iron oxygenase, and requires a ferredoxin and EC 1.18.1.3 for activity.
    		 1 A0A059WLZ7
    Salicylate 5-hydroxylase. [EC: 1.14.13.172]
    Salicylate + NADH + O(2) = 2,5-dihydroxybenzoate + NAD(+) + H(2)O.
    • This enzyme, which was characterized from the bacterium Ralstonia sp. U2, comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC 1.18.1.7), an iron-sulfur oxygenase, and ferredoxin.
    		 1 O52379
    Cholesterol 7-desaturase. [EC: 1.14.19.21]
    Cholesterol + O(2) + NAD(P)H = cholesta-5,7-dien-3-beta-ol + NAD(P)(+) + 2 H(2)O.
    • The enzyme, characterized from several organisms including the worm Caenorhabditis elegans, the fly Drosophila melanogaster, and the ciliate Tetrahymena thermophila, is a Rieske oxygenase.
    • In insects it participates in the the biosythesis of ecdysteroid hormones.
    • The electrons are transferred from NAD(P)H via an electron transfer chain likely to include ferredoxin reductase and ferredoxin.
    • The enzyme differs from regular desaturases, such as EC 1.14.19.20, which are cytochrome b5-dependent and contain the three His-boxes that are typical to most desaturases.
    		 1 Q17938
    2-halobenzoate 1,2-dioxygenase. [EC: 1.14.12.13]
    A 2-halobenzoate + NADH + O(2) = catechol + a halide anion + NAD(+) + CO(2).
    • A multicomponent enzyme system composed of a dioxygenase component and an electron transfer component.
    • The latter contains FAD.
    • The enzyme, characterized from the bacterium Burkholderia cepacia 2CBS, has a broad substrate specificity.
    • Substrates include 2-fluorobenzoate, 2-chlorobenzoate, 2-bromobenzoate, and 2-iodobenzoate, which are processed in this order of preference.
    		 1 Q51601
    2-aminobenzenesulfonate 2,3-dioxygenase. [EC: 1.14.12.14]
    2-aminobenzenesulfonate + NADH + O(2) = 2,3-dihydroxybenzenesulfonate + NH(3) + NAD(+).
      		 1 Q9RBG5
      2,4-dinitrotoluene dioxygenase. [EC: 1.14.12.24]
      2,4-dinitrotoluene + NADH + O(2) = 4-methyl-5-nitrocatechol + nitrite + NAD(+).
      • This enzyme, characterized from the bacterium Burkholderia sp. strain DNT, is a member of the naphthalene family of bacterial Rieske non- heme iron dioxygenases.
      • It comprises a multicomponent system, containing a Rieske [2Fe-2S] ferredoxin, an NADH-dependent flavoprotein reductase (EC 1.18.1.3), and an alpha-3-beta-3 oxygenase.
      • The enzyme forms a cis-dihydroxylated product that spontaneously rearranges to form a catechol with accompanying release of nitrite.
      • It does not act on nitrobenzene.
      • Cf. EC 1.14.12.23.
      		 1 Q45695