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CATH Superfamily 3.30.465.10

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: waiting to be named.

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 17104: Cytokinin dehydrogenase 4

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
Alditol oxidase. [EC: 1.1.3.41]
An alditol + O(2) = an aldose + H(2)O(2).
  • While xylitol (five carbons) and sorbitol (6 carbons) are the preferred substrates, other alditols, including L-threitol (four carbons), D-arabinitol (five carbons), D-galactitol (six carbons) and D-mannitol (six carbons) can also act as substrates, but more slowly.
 87 A0A045IUM0 A0A076LUJ3 A0A089Z618 A0A0C7DUZ5 A0A0D8HV00 A0A0E8TK92 A0A0F5R719 A0A0F6FLL2 A0A0F6J509 A0A0G4DZU1
(77 more...)
Cytokinin dehydrogenase. [EC: 1.5.99.12]
N(6)-dimethylallyladenine + acceptor + H(2)O = adenine + 3-methylbut-2- enal + reduced acceptor.
  • Converts zeatin and related cytokinins.
  • Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is a dimethylallyl or other prenyl group.
  • Although this activity was previously thought to be catalyzed by a hydrogen-peroxide-forming oxidase, this enzyme does not require oxygen for activity and does not form hydrogen peroxide.
  • 2,6-dichloroindophenol, methylene blue, nitroblue tetrazolium, phenazine methosulfate and Cu(2+) in the presence of imidazole can act as acceptors.
 84 A0A0B2PG68 A0A0B2PGB5 A0A0B2PHZ1 A0A0B2PVG3 A0A0B2Q0C2 A0A0B2Q4K9 A0A0B2QCB7 A0A0B2QD16 A0A0B2QRC5 A0A0B2RJ83
(74 more...)
L-gulonolactone oxidase. [EC: 1.1.3.8]
L-gulono-1,4-lactone + O(2) = L-ascorbate + H(2)O(2).
  • The product spontaneously isomerizes to L-ascorbate.
  • While most higher animals can synthesize ascorbic acid, primates and guinea pigs cannot.
 43 A0A059MT46 A0A062X1T2 A0A088MS33 A0A0D8BEZ6 A0A0G3V0S0 A0A0J0YI73 A0A0N0ML90 A0A0N0N256 A0A0N1H630 A0A0N1NL18
(33 more...)
D-arabinono-1,4-lactone oxidase. [EC: 1.1.3.37]
D-arabinono-1,4-lactone + O(2) = dehydro-D-arabinono-1,4-lactone + H(2)O(2).
    		 30 A0A0B0DTV2 A0A0F4Z0X7 A0A0F8BVY7 A0A0L1HIV2 A0A0P4UA74 A0A1H6PWT8 B3LLH0 B8M2X2 B9WMY6 C4YN06
    (20 more...)
    UDP-N-acetylmuramate dehydrogenase. [EC: 1.3.1.98]
    UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP-N-acetyl-3- O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH.
    • NADH can to a lesser extent replace NADPH.
    • Formerly EC 1.1.1.158.
    		 2 A0A0L1HIV2 A0A0P4UA74
    D-mannitol oxidase. [EC: 1.1.3.40]
    Mannitol + O(2) = mannose + H(2)O(2).
    • Also catalyzes the oxidation of D-arabinitol and, to a lesser extent, D-glucitol (sorbitol), whereas L-arabinitol is not a good substrate.
    • The enzyme from the snails Helix aspersa and Arion ater is found in a specialized tubular organelle that has been termed the mannosome.
    		 2 L1L2T7 L7ESE9
    Calcium-transporting ATPase. [EC: 3.6.3.8]
    ATP + H(2)O + Ca(2+)(Side 1) = ADP + phosphate + Ca(2+)(Side 2).
    • P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
    • This enzyme family comprises three types of Ca(2+)-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum and in Saccharomyces cerevisiae.
    • The first and third transport one ion per ATP hydrolyzed, whereas the second transports two ions.
    • Formerly EC 3.6.1.38.
    		 1 A0A1J7HGU2
    (R)-6-hydroxynicotine oxidase. [EC: 1.5.3.6]
    (R)-6-hydroxynicotine + H(2)O + O(2) = 1-(6-hydroxypyridin-3-yl)-4- (methylamino)butan-1-one + H(2)O(2).
    • The enzyme, which participates in nicotine degradation, is specific for (R) isomer of 6-hydroxynicotine, derived from the uncommon (R)- nicotine.
    • The bacterium Arthrobacter nicotinovorans, in which this enzyme was originally discovered, has a different enzyme that catalyzes a similar reaction with the (S)-isomer (cf. EC 1.5.3.5).
    		 1 A0A0T9M2S7
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