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CATH Superfamily 3.20.20.70

Aldolase class I

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:

"
Aldolase class I
".

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 120894: Thiazole biosynthesis protein ThiH

There are 4 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
2-iminoacetate synthase. [EC: 4.1.99.19]
L-tyrosine + S-adenosyl-L-methionine + NADPH = 2-iminoacetate + 4-methylphenol + 5'-deoxyadenosine + L-methionine + NADP(+) + H(+).
  • Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule.
  • The first stage of catalysis is reduction of the S-adenosyl-L- methionine to produce methionine and a 5-deoxyadenosin-5-yl radical that is crucial for the conversion of the substrate.
  • Part of the pathway for thiamine biosynthesis.
  • Formerly EC 1.3.99.n2.
 612 A0A024L917 A0A024L917 A0A026USH1 A0A026USH1 A0A027TL77 A0A027TL77 A0A027ZM53 A0A027ZM53 A0A028DZE6 A0A028DZE6
(602 more...)
Methylornithine synthase. [EC: 5.4.99.58]
L-lysine = (3R)-3-methyl-D-ornithine.
  • The enzyme is a member of the superfamily of S-adenosyl-L-methionine- dependent radical (radical AdoMet) enzymes.
  • Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule.
  • The reaction is part of the biosynthesis pathway of pyrrolysine, a naturally occurring amino acid found in some archaeal methyltransferases.
 6 A0A0E3LKF2 A0A0E3LKF2 Q46E78 Q46E78 Q8TUB9 Q8TUB9
Short-chain acyl-CoA dehydrogenase. [EC: 1.3.8.1]
A short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.
  • One of several enzymes that catalyze the first step in fatty acids beta-oxidation.
  • The enzyme catalyzes the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R-hydrogen atoms.
  • The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms.
  • The highest activity was reported with either butanoyl-CoA or pentanoyl-CoA.
  • The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA.
  • Cf. EC 1.3.8.7, EC 1.3.8.8 and EC 1.3.8.9.
  • Formerly EC 1.3.2.1 and EC 1.3.99.2.
 4 A0A1B2YMH5 A0A1B2YMH5 H6RI84 H6RI84
Biotin synthase. [EC: 2.8.1.6]
Dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.
  • The enzyme binds a [4Fe-4S] and a [2Fe-2S] cluster.
  • In every reaction cycle, the enzyme consumes two molecules of AdoMet, each producing 5'-deoxyadenosine and a putative dethiobiotinyl carbon radical.
  • Reaction with another equivalent of AdoMet results in abstraction of the C6 methylene pro-(S) hydrogen atom from 9-mercaptodethiobiotin, and the resulting carbon radical is quenched via formation of an intramolecular C-S bond, thus closing the biotin thiophane ring.
  • The sulfur donor is believed to be the [2Fe-2S] cluster, which is sacrificed in the process, so that in vitro the reaction is a single turnover.
  • In vivo, the [2Fe-2S] cluster can be reassembled by the Isc or Suf iron-sulfur cluster assembly systems, to allow further catalysis.
 4 A0A068RBK7 A0A068RBK7 E0SGG4 E0SGG4
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