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CATH Superfamily 3.10.129.10

Hotdog Thioesterase

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:

"
Hotdog Thioesterase
".

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 242: Polyunsaturated fatty acid synthase PfaC

There are 2 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-hydroxyacyl-[acyl-carrier-protein] dehydratase. [EC: 4.2.1.59]
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl- carrier protein] + H(2)O.
  • This enzyme is responsible for the dehydration step of the dissociated (type II) fatty-acid biosynthesis system that occurs in plants and bacteria.
  • The enzyme uses fatty acyl thioesters of ACP in vivo.
  • Different forms of the enzyme may have preferences for substrates with different chain length.
  • For example, the activity of FabZ, the ubiquitous enzyme in bacteria, decreases with increasing chain length.
  • Gram-negative bacteria that produce unsaturated fatty acids, such as Escherichia coli, have another form (FabA) that prefers intermediate chain length, and also catalyzes EC 5.3.3.14.
  • Despite the differences both forms can catalyze all steps leading to the synthesis of palmitate (C16:0).
  • FabZ, but not FabA, can also accept unsaturated substrates.
  • Formerly EC 4.2.1.58, EC 4.2.1.60 and EC 4.2.1.61.
 1 A0A099KJC7
6-deoxyerythronolide-B synthase. [EC: 2.3.1.94]
Propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH = 6-deoxyerythronolide B + 7 CoA + 6 CO(2) + H(2)O + 6 NADP(+).
  • The product, 6-deoxyerythronolide B, contains a 14-membered lactone ring and is an intermediate in the biosynthesis of erythromycin antibiotics.
  • Biosynthesis of 6-deoxyerythronolide B requires 28 active sites that are precisely arranged along three large polypeptides, denoted DEBS1, -2 and -3.
  • The polyketide product is synthesized by the processive action of a loading didomain, six extension modules and a terminal thioesterase domain.
  • Each extension module contains a minimum of a ketosynthase (KS), an acyltransferase (AT) and an acyl-carrier protein (ACP).
  • The KS domain both accepts the growing polyketide chain from the previous module and catalyzes the subsequent decarboxylative condensation between this substrate and an ACP-bound methylmalonyl extender unit, introduce by the AT domain.
  • This combined effort gives rise to a new polyketide intermediate that has been extended by two carbon atoms.
 1 A0A099KJC7