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CATH Superfamily 3.60.130.10

Clavaminate synthase-like

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:

"
Clavaminate synthase-like
".

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 2626: Putative alpha-ketoglutarate-dependent taurine dio...

There are 11 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
Taurine dioxygenase. [EC: 1.14.11.17]
Taurine + 2-oxoglutarate + O(2) = sulfite + aminoacetaldehyde + succinate + CO(2).
  • The enzyme from Escherichia coli also acts on pentanesulfonate, 3-(N-morpholino)propanesulfonate and 2-(1,3-dioxoisoindolin-2- yl)ethanesulfonate, but at lower rates.
 1626 A0A009GJA3 A0A009GW89 A0A009I133 A0A009IMG3 A0A009JI62 A0A009KQ71 A0A009LQ48 A0A009MIJ5 A0A009QCN6 A0A009R620
(1616 more...)
Gamma-butyrobetaine dioxygenase. [EC: 1.14.11.1]
4-trimethylammoniobutanoate + 2-oxoglutarate + O(2) = 3-hydroxy-4- trimethylammoniobutanoate + succinate + CO(2).
    		 70 A0A088TUZ9 A0A088X2Q9 A0A090E926 A0A090EHF2 A0A090GEU4 A0A095DLY2 A0A095EBF2 A0A095GCM7 A0A0A1HTI4 A0A0C5ESQ9
    (60 more...)
    Trimethyllysine dioxygenase. [EC: 1.14.11.8]
    N(6),N(6),N(6)-trimethyl-L-lysine + 2-oxoglutarate + O(2) = 3-hydroxy- N(6),N(6),N(6)-trimethyl-L-lysine + succinate + CO(2).
      		 9 A0A075B0I0 A5DCB6 K7DHL4 L8IA16 Q0VC74 Q5F4B3 Q91ZE0 Q91ZW6 Q9NVH6
      (R)-dichlorprop dioxygenase (2-oxoglutarate). [EC: 1.14.11.44]
      (1) (R)-2-(4-chloro-2-methylphenoxy)propanoate + 2-oxoglutarate + O(2) = 4-chloro-2-methylphenol + pyruvate + succinate + CO(2). (2) (R)-(2,4-dichlorophenoxy)propanoate + 2-oxoglutarate + O(2) = 2,4- dichlorophenol + pyruvate + succinate + CO(2).
      • The enzymes from the Gram-negative bacteria Delftia acidovorans MC1 and Sphingomonas herbicidovorans MH are involved in the degradation of the (R)-enantiomer of the phenoxyalkanoic acid herbicides mecoprop and dichlorprop.
      		 4 G9FCB0 P83310 Q8KSC8 Q8KSC9
      Pentalenolactone F synthase. [EC: 1.14.11.36]
      Pentalenolactone D + 2 2-oxoglutarate + 2 O(2) = pentalenolactone F + 2 succinate + 2 CO(2) + H(2)O.
      • Isolated from the bacteria Streptomyces exfoliatus, Streptomyces arenae and Streptomyces avermitilis.
      • Part of the pentalenolactone biosynthesis pathway.
      		 3 E3VWI8 E3VWK4 Q82IY7
      Clavaminate synthase. [EC: 1.14.11.21]
      (1) Deoxyamidinoproclavaminate + 2-oxoglutarate + O(2) = amidinoproclavaminate + succinate + CO(2). (2) Proclavaminate + 2-oxoglutarate + O(2) = dihydroclavaminate + succinate + CO(2) + H(2)O. (3) Dihydroclavaminate + 2-oxoglutarate + O(2) = clavaminate + succinate + CO(2) + H(2)O.
      • Catalyzes three separate oxidative reactions in the pathway for the biosythesis of the beta-lactamase inhibitor clavulanate in Streptomyces clavuligerus.
      • The first step (hydroxylation) is separated from the latter two (oxidative cyclization and desaturation) by the action of EC 3.5.3.22.
      • The three reactions are all catalyzed at the same nonheme iron site.
      		 3 E2Q5Q5 Q05582 Q53939
      L-asparagine oxygenase. [EC: 1.14.11.39]
      L-asparagine + 2-oxoglutarate + O(2) = (2S,3S)-3-hydroxyasparagine + succinate + CO(2).
      • The enzyme is only able to hydroxylate free L-asparagine.
      • It is not active toward D-asparagine.
      • The beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non- ribosomally synthesized acidic lipopeptide lactone.
      • Formerly EC 1.14.11.n1.
      		 3 A0A1H2BCA2 D6ES33 Q9Z4Z5
      Homoaconitate hydratase. [EC: 4.2.1.36]
      (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate = (Z)-but-1-ene-1,2,4- tricarboxylate + H(2)O.
      • The enzyme from the hyperthermophilic eubacterium Thermus thermophilus can catalyze the reaction shown above but cannot catalyze the previously described reaction, i.e. formation of homocitrate by hydration of cis-homoaconitate.
      • The enzyme responsible for the conversion of cis-homoaconitate into homocitrate in T.thermophilus is unknown at present but the reaction can be catalyzed in vitro using EC 4.2.1.3 from pig.
      		 2 A0A164TLZ1 A0A166GYD7
      NAD(+) ADP-ribosyltransferase. [EC: 2.4.2.30]
      NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D- ribosyl)(n+1)-acceptor.
      • The ADP-D-ribosyl group of NAD(+) is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP- ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.
      		 1 D0NWS2
      Adenosinetriphosphatase. [EC: 3.6.1.3]
      ATP + H(2)O = ADP + phosphate.
      • Many enzymes previously listed under this number are now listed separately as EC 3.6.1.32 to EC 3.6.1.39.
      • The remaining enzymes, not separately listed on the basis of some function coupled with hydrolyzes of ATP, include enzymes dependent on Ca(2+), Mg(2+), anions, H(+) or DNA.
      • Formerly EC 3.6.1.4.
      		 1 G8Q2G0
      Enoyl-CoA hydratase. [EC: 4.2.1.17]
      (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O.
      • Acts in the reverse direction.
      • With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74).
      		 1 U2WU38
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