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CATH Superfamily 3.40.50.720

NAD(P)-binding Rossmann-like Domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:

"
NAD(P)-binding Rossmann-like Domain
".

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 209: Polyketide synthase Pks12

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
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.
 26 A0A0E8NTV0 A0A0E8NTV0 A0A0E8NTV0 A0A0E8NTV0 A0A0E8NTV0 A0A0H3M9Y4 A0A0H3M9Y4 A0A0H3M9Y4 A0A0H3M9Y4 A0A0H3M9Y4
(16 more...)
Mycolipanoate synthase. [EC: 2.3.1.252]
A long-chain acyl-CoA + 3 (S)-methylmalonyl-CoA + 6 NADPH + holo- [mycolipanoate synthase] = mycolipanoyl-[mycolipanoate synthase] + 4 CoA + 3 CO(2) + 6 NADP(+) + 3 H(2)O.
  • This mycobacterial enzyme accepts long-chain fatty acyl groups from their CoA esters and extends them by incorporation of three methylmalonyl (but not malonyl) residues, forming trimethyl-branched fatty-acids such as (2S,4S,6S)-2,4,6-trimethyl-tetracosanoate (C(27)- mycolipanoate).
  • Since the enzyme lacks a thioesterase domain, the product remains bound to the enzyme and requires additional enzyme(s) for removal.
 16 A0A089QRB9 A0A089QRB9 A0A089QRB9 A0A089QRB9 A0A0E8NV99 A0A0E8NV99 A0A0E8NV99 A0A0E8NV99 A0A0H3L8P3 A0A0H3L8P3
(6 more...)
Mycocerosate synthase. [EC: 2.3.1.111]
(1) A long-chain acyl-[mycocerosic acid synthase] + 3 methylmalonyl-CoA + 6 NADPH = a trimethylated-mycocerosoyl-[mycocerosate synthase] + 3 CoA + 3 CO(2) + 6 NADP(+) + 3 H(2)O. (2) A long-chain acyl-[mycocerosate synthase] + 4 methylmalonyl-CoA + 8 NADPH = a tetramethylated-mycocerosoyl-[mycocerosate synthase] + 4 CoA + 4 CO(2) + 8 NADP(+) + 4 H(2)O.
  • The enzyme, characterized from mycobacteria, is loaded with a long- chain acyl moiety by EC 6.2.1.49 and elongates it by incorporation of three or four methylmalonyl (but not malonyl) residues, to form tri- or tetramethyl-branched fatty-acids, respectively, such as 2,4,6,8- tetramethyloctacosanoate (C(32)-mycocerosate).
  • Since the enzyme lacks a thioesterase domain, the product remains bound and requires additional enzyme(s) for removal.
  • Even though the enzyme can accept C(6) to C(20) substrates in vitro, it prefers to act on C(14)-C(20) substrates in vivo.
 4 A0A0H3MGR2 A0A0H3MGR2 Q02251 Q02251
Chalcone synthase. [EC: 2.3.1.74]
3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO(2).
  • The enzyme catalyzes the first committed step in the biosynthesis of flavonoids.
  • It can also act on dihydro-4-coumaroyl-CoA, forming phloretin.
 2 Q54FI3 Q55E72
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