View in Gene3D

CATH Superfamily 3.30.70.250

Malonyl-CoA ACP transacylase, ACP-binding

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:

"
Malonyl-CoA ACP transacylase, ACP-binding
".

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.
« Back to all FunFams

FunFam 4138: Fatty acid synthase subunit beta

There are 3 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
[Acyl-carrier-protein] S-malonyltransferase. [EC: 2.3.1.39]
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier- protein].
  • Essential, along with EC 2.3.1.38, for the initiation of fatty-acid biosynthesis in bacteria.
  • Also provides the malonyl groups for polyketide biosynthesis.
  • The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis.
  • In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7) is the preferred substrate.
  • This enzyme also forms part of the multienzyme complexes EC 4.1.1.88 and EC 4.1.1.89.
  • Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase.
  • In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot whereas the enzyme from Pseudomonas putida can use both as substrates.
  • The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA prosthetic group.
 665 A0A017RXJ0 A0A024P1Q8 A0A024QD66 A0A061NWJ4 A0A069BFL1 A0A069QLM0 A0A072Y693 A0A072YJL9 A0A073CNN0 A0A075JQN2
(655 more...)
Enoyl-[acyl-carrier-protein] reductase (NADH). [EC: 1.3.1.9]
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl- carrier protein] + NADH.
  • The enzyme catalyzes an essential step in fatty acid biosynthesis, the reduction of the 2,3-double bond in enoyl-acyl-[acyl-carrier- protein] derivatives of the elongating fatty acid moiety.
  • The enzyme from the bacterium Escherichia coli accepts substrates with carbon chain length from 4 to 18.
  • The enzyme from the bacterium Mycobacterium tuberculosis prefers substrates with carbon chain length from 12 to 24 carbons.
 3 A0A0M1QF95 A0A150KYP4 A0A1G4LJE9
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.
 3 G6FYL6 K9PTM1 K9ZH50