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CATH Superfamily 2.60.130.10

Aromatic compound dioxygenase

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Aromatic compound dioxygenase
".

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.
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FunFam 2052: Catechol 1,2-dioxygenase 1

There are 8 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
Catechol 1,2-dioxygenase. [EC: 1.13.11.1]
Catechol + O(2) = cis,cis-muconate.
  • Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida.
  • Formerly EC 1.13.1.1 and EC 1.99.2.2.
 500 A0A009FAF6 A0A009FZL1 A0A009GV77 A0A009HPA2 A0A009HYX6 A0A009JGI0 A0A009K1S1 A0A009LVN9 A0A009MGY7 A0A009PTN0
(490 more...)
Hydroxyquinol 1,2-dioxygenase. [EC: 1.13.11.37]
Hydroxyquinol + O(2) = maleylacetate.
  • Highly specific; catechol and pyrogallol are acted on at less than 1% of the rate at which hydroxyquinol is oxidized.
 142 A0A009JKV9 A0A021WZM0 A0A024HIE3 A0A062IBL4 A0A081RF87 A0A084FVT9 A0A085G233 A0A088TCW6 A0A090DPA7 A0A090EUN6
(132 more...)
Protocatechuate 3,4-dioxygenase. [EC: 1.13.11.3]
3,4-dihydroxybenzoate + O(2) = 3-carboxy-cis,cis-muconate.
  • The enzyme, which participates in the degradation of aromatic compounds, catalyzes the intradiol addition of both oxygen atoms from molecular oxygen, resulting in ortho-cleavage of the aromatic ring.
  • The type of cleavage leads to mineralization via the intermediate 3-oxoadipate.
  • Formerly EC 1.13.1.3 and EC 1.99.2.3.
 9 A0A132HM81 D4Z420 D8IP03 D8IR18 D8IR74 M9RE14 Q0K093 Q1LM35 R7XN17
Maleylacetate reductase. [EC: 1.3.1.32]
3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H.
    		 4 A0A0N1G1F2 A0A100JQB7 A0A178WYF9 A0A1L8QBE3
    Transferred entry: 1.13.11.60 and 5.4.4.6. [EC: 1.13.11.44]
      		2 A2QNW8 G3XZ65
      Alcohol dehydrogenase. [EC: 1.1.1.1]
      (1) An alcohol + NAD(+) = an aldehyde or ketone + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH.
      • Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol.
      • The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
      		 1 A0A0K3B3Z0
      9,12-octadecadienoate 8-hydroperoxide 8S-isomerase. [EC: 5.4.4.6]
      (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate = (7S,8S,9Z,12Z)-7,8- dihydroxyoctadeca-9,12-dienoate.
      • The bifunctional enzyme from Gaeumannomyces graminis catalyzes the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12- dienoate (cf. EC 1.13.11.60), which is then isomerized to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate.
      • Formerly EC 1.13.11.44.
      		 1 A0A0F4YGA9
      Linoleate 8R-lipoxygenase. [EC: 1.13.11.60]
      Linoleate + O(2) = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate.
      • The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyze two separate reactions.
      • Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, which is subsequently isomerized by the C-terminal P450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.5).
      • The bifunctional enzyme from Gaeumannomyces graminis also catalyzes the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca- 9,12-dienoate, but its second domain isomerizes it to (7S,8S,9Z,12Z)- 5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.6).
      • Formerly EC 1.13.11.44.
      		 1 A0A0F4YGA9
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