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 70636: Non-ribosomal peptide synthetase modules

There are 14 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
Long-chain-fatty-acid--CoA ligase. [EC: 6.2.1.3]
ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.
  • Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity.
  • The liver enzyme acts on acids from C(6) to C(20); that from brain shows high activity up to C(24).
195 A0A059MKS2 A0A066PK87 A0A072NSP9 A0A073A6U2 A0A075R389 A0A075R6H8 A0A075WCK2 A0A075WJZ1 A0A081N553 A0A081NBF2
(185 more...)
(2,3-dihydroxybenzoyl)adenylate synthase. [EC: 2.7.7.58]
ATP + 2,3-dihydroxybenzoate = diphosphate + (2,3- dihydroxybenzoyl)adenylate.
    56 A0A022MP34 A0A022PLN5 A0A031LRT1 A0A067LX76 A0A069KAH0 A0A093B4U9 A0A094M392 A0A0A2NBA8 A0A0A7XR46 A0A0B2BFG4
    (46 more...)
    Fatty-acyl-CoA synthase. [EC: 2.3.1.86]
    Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO(2) + 2n NADP(+).
    • The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi- functional protein complex composed of two subunits.
    • One subunit catalyzes the reactions EC 1.1.1.100 and EC 2.3.1.41, while the other subunit catalyzes the reactions of EC 2.3.1.38, EC 2.3.1.39, EC 4.2.1.59, EC 1.3.1.10 and EC 1.1.1.279.
    • The enzyme differs from the animal enzyme (EC 2.3.1.85) in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid.
    8 A0QYK2 A3SZF6 A9DLD2 Q0G4I3 Q2B2B8 Q2BAP1 Q2BKB9 Q9VCC6
    4-hydroxybenzoate--CoA ligase. [EC: 6.2.1.27]
    ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate + 4-hydroxybenzoyl-CoA.
      7 A0A0D6HB86 A0A0M7H9K8 A0A0M7KYV2 A0A0M7M374 A0A0M7NPF4 A0A0M9J1Q6 A0A157RU33
      O-succinylbenzoate--CoA ligase. [EC: 6.2.1.26]
      ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 2-succinylbenzoyl- CoA.
        6 A0A063BEL7 A0A132H9A7 C3MP42 D2PGP2 F4CVG8 Q1LE18
        4-coumarate--CoA ligase. [EC: 6.2.1.12]
        ATP + 4-coumarate + CoA = AMP + diphosphate + 4-coumaroyl-CoA.
          4 A2QRH8 B8C078 Q54P77 Q54P78
          Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing). [EC: 1.13.12.7]
          Photinus luciferin + O(2) + ATP = oxidized Photinus luciferin + CO(2) + AMP + diphosphate + light.
          • Photinus (firefly) is a bioluminescent insect.
          • The first step in the reaction is the formation of an acid anhydride between the carboxylic group and AMP, with the release of diphosphate.
          • The enzyme may be assayed by measurement of light emission.
          4 B7PBP9 B7PLP2 B7QEY4 E0VSL5
          Acetoacetate--CoA ligase. [EC: 6.2.1.16]
          ATP + acetoacetate + CoA = AMP + diphosphate + acetoacetyl-CoA.
          • Also acts, more slowly, on L-3-hydroxybutanoate.
          3 A0A090TEB2 A0A0M2NBV6 A0A1G4LJM3
          Fatty-acid synthase. [EC: 2.3.1.85]
          Acetyl-CoA + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + (n+1) CoA + n CO(2) + 2n NADP(+).
          • The animal enzyme is a multifunctional protein catalyzing the reactions of EC 2.3.1.38, EC 2.3.1.39, EC 2.3.1.41, EC 1.1.1.100, EC 4.2.1.59, EC 1.3.1.39 and EC 3.1.2.14.
          2 A0A0F4XEE6 G8PXB8
          Trans-feruloyl-CoA synthase. [EC: 6.2.1.34]
          Ferulic acid + CoA + ATP = feruloyl-CoA + products of ATP breakdown.
          • It has not yet been established whether AMP + diphosphate or ADP + phosphate are formed in this reaction.
          1 B6YY78
          2-hydroxy-7-methoxy-5-methyl-1-naphthoate--CoA ligase. [EC: 6.2.1.43]
          ATP + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate + CoA = AMP + diphosphate + 2-hydroxy-7-methoxy-5-methyl-1-naphthoyl-CoA.
          • The enzyme from the bacterium Streptomyces carzinostaticus is involved in the attachment of the 2-hydroxy-7-methoxy-5-methyl-1- naphthoate moiety of the antibiotic neocarzinostatin.
          • In vitro the enzyme also catalyzes the activation of other 1-naphthoic acid analogs, e.g. 2-hydroxy-5-methyl-1-naphthoate or 2,7-dihydroxy-5-methyl-1-naphthoate.
          1 Q84HC5
          Acetate--CoA ligase. [EC: 6.2.1.1]
          ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
          • Also acts on propanoate and propenoate.
          1 A0A1M4EHN0
          Isochorismate synthase. [EC: 5.4.4.2]
          Chorismate = isochorismate.
          • The reaction is reversible.
          • Formerly EC 5.4.99.6.
          1 A0A0U1L2H4
          4-chlorobenzoate--CoA ligase. [EC: 6.2.1.33]
          4-chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate.
          • Part of the bacterial 2,4-dichlorobenzoate degradation pathway.
          1 A5JTM6