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CATH Superfamily 3.40.50.980

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 70436: Non-ribosomal peptide synthetase modules

There are 19 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
(2,3-dihydroxybenzoyl)adenylate synthase. [EC: 2.7.7.58]
ATP + 2,3-dihydroxybenzoate = diphosphate + (2,3- dihydroxybenzoyl)adenylate.
    		 862 A0A011U6G7 A0A011U6G7 A0A022MP34 A0A022MP34 A0A022PLN5 A0A022PLN5 A0A023P673 A0A023P673 A0A023Y396 A0A023Y396
    (852 more...)
    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).
    		 534 A0A011P369 A0A011P369 A0A059MKS2 A0A059MKS2 A0A066PK87 A0A066PK87 A0A068YUC2 A0A068YUC2 A0A069Q7H6 A0A069Q7H6
    (524 more...)
    Benzoate--CoA ligase. [EC: 6.2.1.25]
    ATP + benzoate + CoA = AMP + diphosphate + benzoyl-CoA.
    • Also acts on 2-, 3- and 4-fluorobenzoate, but only very slowly on the corresponding chlorobenzoates.
    		 188 A0A068YR46 A0A068YR46 A0A076K591 A0A076K591 A0A080NSV1 A0A080NSV1 A0A0C3ISQ4 A0A0C3ISQ4 A0A0C4Y9H6 A0A0C4Y9H6
    (178 more...)
    4-hydroxybenzoate--CoA ligase. [EC: 6.2.1.27]
    ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate + 4-hydroxybenzoyl-CoA.
      		 24 A0A0D6HB86 A0A0D6HB86 A0A0M7KYV2 A0A0M7KYV2 A0A0M7M374 A0A0M7M374 A0A0M7NPF4 A0A0M7NPF4 A0A0M9ISE8 A0A0M9ISE8
      (14 more...)
      O-succinylbenzoate--CoA ligase. [EC: 6.2.1.26]
      ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 2-succinylbenzoyl- CoA.
        		 12 A0A063BEL7 A0A063BEL7 A0A132H9A7 A0A132H9A7 B3R4Q1 B3R4Q1 B3RBD7 B3RBD7 F4CVG8 F4CVG8
        (2 more...)
        Phenylalanine racemase (ATP-hydrolyzing). [EC: 5.1.1.11]
        ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine.
          		 10 A0A0L6JGW6 A0A0L6JGW6 A0A1A5VH98 A0A1A5VH98 B4AIX0 B4AIX0 C0ZDA5 C0ZDA5 E1UL90 E1UL90
          Isochorismate synthase. [EC: 5.4.4.2]
          Chorismate = isochorismate.
          • The reaction is reversible.
          • Formerly EC 5.4.99.6.
          		 10 A0A088X566 A0A088X566 A0A0D5L4D2 A0A0D5L4D2 A0A0U1L2H4 A0A0U1L2H4 A0A1B4ACX7 A0A1B4ACX7 H0U6D6 H0U6D6
          Aspartate racemase. [EC: 5.1.1.13]
          L-aspartate = D-aspartate.
          • Also acts, at half the rate, on L-alanine.
          		 10 A0A0L6JGW6 A0A0L6JGW6 A0A0M1QH18 A0A0M1QH18 B4AIX0 B4AIX0 W3ZWE7 W3ZWE7 W4A0C9 W4A0C9
          3-phosphoshikimate 1-carboxyvinyltransferase. [EC: 2.5.1.19]
          Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O- (1-carboxyvinyl)-3-phosphoshikimate.
            		 8 A0A0D0X3X9 A0A0D0X3X9 A0A1C4X662 A0A1C4X662 A0A1C4Y8D1 A0A1C4Y8D1 A0A1C4YB78 A0A1C4YB78
            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 A9DLD7 A9DLD7 Q0G4I3 Q0G4I3 Q2B2B9 Q2B2B9 Q2BKB9 Q2BKB9
            Acetate--CoA ligase. [EC: 6.2.1.1]
            ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
            • Also acts on propanoate and propenoate.
            		 8 A0A0N0UGE1 A0A0N0UGE1 A0A1L5M1V5 A0A1L5M1V5 A0A1M4EHN0 A0A1M4EHN0 Q89VG8 Q89VG8
            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.
            		 6 A0A0F4XEE6 A0A0F4XEE6 G8PXB8 G8PXB8 G8PXB9 G8PXB9
            D-alanine--poly(phosphoribitol) ligase. [EC: 6.1.1.13]
            ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D- alanyl-poly(ribitol phosphate).
            • A thioester bond is formed transiently between D-alanine and the sulfhydryl group of the 4'-phosphopantetheine prosthetic group of D-alanyl carrier protein during the activation of the alanine.
            • Involved in the synthesis of teichoic acids.
            		 2 A0A080UAJ6 A0A080UAJ6
            Anthranilate synthase. [EC: 4.1.3.27]
            Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
            • In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of tryptophan (EC 2.4.2.18, EC 4.1.1.48, EC 4.2.1.20, and EC 5.3.1.24).
            • The native enzyme in the complex with uses either glutamine or (less efficiently) NH(3).
            • The enzyme separated from the complex uses NH(3) only.
            		 2 D8P4S5 D8P4S5
            Phytanate--CoA ligase. [EC: 6.2.1.24]
            ATP + phytanate + CoA = AMP + diphosphate + phytanoyl-CoA.
            • Not identical with EC 6.2.1.20.
            		 2 A1KA13 A1KA13
            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.
            		 2 Q84HC5 Q84HC5
            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.
            		 2 E0VSL5 E0VSL5
            Ornithine racemase. [EC: 5.1.1.12]
            L-ornithine = D-ornithine.
              		 2 E1UL88 E1UL88
              5-(carboxyamino)imidazole ribonucleotide synthase. [EC: 6.3.4.18]
              ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole + HCO(3)(-) = ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole.
              • In Escherichia coli, this enzyme, along with EC 5.4.99.18, is required to carry out the single reaction catalyzed by EC 4.1.1.21 in vertebrates.
              • Carboxyphosphate is the putative acyl phosphate intermediate.
              • Involved in the late stages of purine biosynthesis.
              		 2 U2XXV1 U2XXV1
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