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CATH Superfamily 1.10.405.10

Guanine Nucleotide Dissociation Inhibitor, domain 1

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:

"
Guanine Nucleotide Dissociation Inhibitor, 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.
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FunFam 917: Amine oxidase [flavin-containing] A

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
Monoamine oxidase. [EC: 1.4.3.4]
RCH(2)NHR' + H(2)O + O(2) = RCHO + R'NH(2) + H(2)O(2).
  • Catalyzes the oxidative deamination of neurotransmitters and biogenic amines.
  • Acts on primary amines, and also on some secondary and tertiary amines.
  • It differs from EC 1.4.3.21, as it can oxidize secondary and tertiary amines but not methylamine.
  • Inhibited by acetylenic compounds such as chlorgyline, 1-deprenyl and pargyline but, unlike EC 1.4.3.21 and EC 1.4.3.22, it is not inhibited by semicarbazide.
  • Formerly EC 1.4.3.9.
 178 A0A068MT52 A0A068MT52 A0A073CL15 A0A073CL15 A0A098G3G7 A0A098G3G7 A0A0A1DGM1 A0A0A1DGM1 A0A0A1FLX3 A0A0A1FLX3
(168 more...)
Putrescine oxidase. [EC: 1.4.3.10]
Putrescine + O(2) + H(2)O = 4-aminobutanal + NH(3) + H(2)O(2).
  • 4-aminobutanal condenses non-enzymically to 1-pyrroline.
 86 A0A0E8NLJ8 A0A0E8NLJ8 A0A0F0LYM1 A0A0F0LYM1 A0A0G4E031 A0A0G4E031 A0A0H3LDZ4 A0A0H3LDZ4 A0A0J6VB72 A0A0J6VB72
(76 more...)
Tryptophan 2-monooxygenase. [EC: 1.13.12.3]
L-tryptophan + O(2) = (indol-3-yl)acetamide + CO(2) + H(2)O.
    		 62 A0A084J6L1 A0A084J6L1 A0A0B5S593 A0A0B5S593 A0A0D6RZV2 A0A0D6RZV2 A0A0F6JA05 A0A0F6JA05 A0A0G8BXS3 A0A0G8BXS3
    (52 more...)
    4,4'-diapophytoene desaturase (4,4'-diapolycopene-forming). [EC: 1.3.8.2]
    15-cis-4,4'-diapophytoene + 4 FAD = all-trans-4,4'-diapolycopene + 4 FADH(2).
    • The enzyme catalyzes four successive dehydrogenations, resulting in production of 4,4'-diapolycopene.
    • While the enzyme from Staphylococcus aureus was only shown to produce 4,4'-diaponeurosporene in vivo, it is able to catalyze the last reaction in vitro.
    		 58 A0A023P620 A0A023P620 A0A0F6JA05 A0A0F6JA05 A0A0J7JSU6 A0A0J7JSU6 A0A0K0S698 A0A0K0S698 A0A0T8E0U0 A0A0T8E0U0
    (48 more...)
    L-amino-acid oxidase. [EC: 1.4.3.2]
    An L-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2).
      		 38 A0A023P620 A0A023P620 A0A0K0S698 A0A0K0S698 A0A0M1QKP5 A0A0M1QKP5 A0A0U0N321 A0A0U0N321 A0A135X0J9 A0A135X0J9
      (28 more...)
      7-chloro-L-tryptophan oxidase. [EC: 1.4.3.23]
      7-chloro-L-tryptophan + O(2) = 2-imino-3-(7-chloroindol-3-yl)propanoate + H(2)O(2).
      • This enzyme catalyzes a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes.
      • During catalysis, the bound FAD is reoxidized at the expense of molecular oxygen, producing one molecule of hydrogen peroxide.
      • The enzyme shows significant preference for 7-chloro-L-tryptophan over L-tryptophan.
      		 14 A0A0K6JBK4 A0A0K6JBK4 A0A0K6JY93 A0A0K6JY93 A0A0K6KGC5 A0A0K6KGC5 A0A0K6KLV9 A0A0K6KLV9 A0A0K6KN08 A0A0K6KN08
      (4 more...)
      L-pipecolate oxidase. [EC: 1.5.3.7]
      L-pipecolate + O(2) = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H(2)O(2).
      • The product reacts with water to form (S)-2-amino-6-oxohexanoate.
      		 2 Q54EW2 Q54EW2
      Sarcosine oxidase. [EC: 1.5.3.1]
      Sarcosine + H(2)O + O(2) = glycine + formaldehyde + H(2)O(2).
      • The flavin is both covalently and non-covalently bound in a molar ratio of 1:1.
      		 2 Q54EW2 Q54EW2