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CATH Superfamily 3.90.470.20

4'-phosphopantetheinyl transferase domain

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:

"
4'-phosphopantetheinyl transferase 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 5827: Mitochondrial holo-[acyl-carrier-protein] synthase

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
Holo-[acyl-carrier-protein] synthase. [EC: 2.7.8.7]
CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein].
  • All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active.
  • The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain.
  • The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier- proteins from prokaryotes.
  • Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14.
 512 A0A016QNQ4 A0A016QNQ4 A0A024KT43 A0A024KT43 A0A024WDX3 A0A024WDX3 A0A037UM54 A0A037UM54 A0A060RTP3 A0A060RTP3
(502 more...)
Lysophospholipase. [EC: 3.1.1.5]
2-lysophosphatidylcholine + H(2)O = glycerophosphocholine + a carboxylate.
    		 24 A0A061HBJ1 A0A061HBJ1 A0A077R9U5 A0A077R9U5 A0A081CBZ6 A0A081CBZ6 A0A0D1DQ89 A0A0D1DQ89 A0A0F7SAR1 A0A0F7SAR1
    (14 more...)
    ADP-dependent NAD(P)H-hydrate dehydratase. [EC: 4.2.1.136]
    (1) ADP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide adenine- dinucleotide = AMP + phosphate + NADH. (2) ADP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide adenine- dinucleotide phosphate = AMP + phosphate + NADPH.
    • Acts equally well on hydrated NADH and hydrated NADPH.
    • NAD(P)H spontaneously hydrates to both the (6S)- and (6R)- isomers.
    • The enzyme from bacteria consists of two domains, one of which acts as an NAD(P)H-hydrate epimerase that interconverts the two isomers to a 60:40 ratio (cf. EC 5.1.99.6), while the other catalyzes the dehydration.
    • Hence the enzyme can restore the complete mixture of isomers into NAD(P)H.
    • The enzyme has no activity with ATP, contrary to the enzyme from eukaryotes (cf. EC 4.2.1.93).
    		 16 A0A133PQV8 A0A133PQV8 A0A134ADF0 A0A134ADF0 A0A1E9AED9 A0A1E9AED9 A0A1E9AF95 A0A1E9AF95 A0A1F0GHT7 A0A1F0GHT7
    (6 more...)
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