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CATH Superfamily 3.40.47.10

Thiolase/Chalcone synthase

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 52247: Non-specific lipid-transfer protein-like 2

There are 6 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
3-oxoadipyl-CoA thiolase. [EC: 2.3.1.174]
Succinyl-CoA + acetyl-CoA = CoA + 3-oxoadipyl-CoA.
  • The enzyme from the bacterium Escherichia coli also has the activity of EC 2.3.1.223.
 91 A0A045JF54 A0A069JSE4 A0A0D8I1H2 A0A0D8I4R2 A0A0E4A1E8 A0A0G4E1V8 A0A0G4JN21 A0A0H2M972 A0A0H3LGX8 A0A0H3M7G5
(81 more...)
Propanoyl-CoA C-acyltransferase. [EC: 2.3.1.176]
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3-alpha,7-alpha,12-alpha-trihydroxy-24-oxo-5-beta-cholestanoyl- CoA.
  • Also acts on dihydroxy-5-beta-cholestanoyl-CoA and other branched chain acyl-CoA derivatives.
  • Catalyzes the penultimate step in the formation of bile acids.
  • The bile acid moiety is transferred from the acyl-CoA thioester (RCO- SCoA) to either glycine or taurine (NH(2)R') by EC 2.3.1.65.
  • Formerly EC 2.3.1.154.
 68 A0A049DJC2 A0A069JBP4 A0A075UYY1 A0A084G5Y7 A0A095B1Y4 A0A099KFU9 A0A0B8NCX0 A0A0E2WRT7 A0A0E9LB56 A0A0E9LFW0
(58 more...)
Acetyl-CoA C-acyltransferase. [EC: 2.3.1.16]
Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
    		 39 A0A062X0J8 A0A0A1FRC4 A0A0A1FW21 A0A0A8TK39 A0A0D6UKH4 A0A0F0LKQ4 A0A0H5CFK9 A0A0K3BP82 A0A0M8JK94 A0A0N7JT81
    (29 more...)
    Acetyl-CoA C-acetyltransferase. [EC: 2.3.1.9]
    2 acetyl-CoA = CoA + acetoacetyl-CoA.
      		 11 A0A0F0K949 A0A0M7L361 A0A0M9ITZ2 A0A0Q7LYN9 A0A157SIG9 A0A1B9EQN9 A0A1M3BW06 K9NIN4 K9NJE3 S2WQU2
      (1 more...)
      3-oxo-5,6-didehydrosuberyl-CoA thiolase. [EC: 2.3.1.223]
      2,3-didehydroadipyl-CoA + acetyl-CoA = CoA + 3-oxo-5,6-didehydrosuberyl- CoA.
      • The enzyme acts in the opposite direction.
      • The enzymes from the bacteria Escherichia coli and Pseudomonas sp. Y2 also have the activity of EC 2.3.1.174.
      • Formerly EC 2.3.1.n11.
      		 4 A0A132BXZ1 A0A1F2PSM6 A0A1J5QV39 U0FDP7
      Beta-ketoacyl-[acyl-carrier-protein] synthase I. [EC: 2.3.1.41]
      Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
      • Responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain.
      • Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids.
      • Can use fatty acyl thioesters of ACP (C(2) to C(16)) as substrates, as well as fatty acyl thioesters of Co-A (C(4) to C(16)).
      • The substrate specificity is very similar to that of EC 2.3.1.179 with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C(16)-Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature.
      		 3 A0A0L1HNC8 A0A0L1I114 A0A0N7Z0Q7