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CATH Superfamily 1.10.1200.10

ACP-like

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:

"
ACP-like
".

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 23735: Non-ribosomal peptide synthetase PvdL

There are 15 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
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.
 22 A0A066ZX53 A0A067AEU8 A0A076W5T3 A0A090YBX7 A0A095EX45 A0A0B5P1P3 A0A0B5RUJ2 A0A0B5RVJ2 A0A0B6A1G1 A0A0B6A292
(12 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).
 9 A0A0F6JBG9 A0A0G8BTR0 A0A0G8BVL5 A0A0G8EN36 A0A0G8EQQ9 A0ZLL9 M1PKD9 N1LIC2 N1LMU9
Glutamate racemase. [EC: 5.1.1.3]
L-glutamate = D-glutamate.
    		 9 A0A1E8A4Z7 B2JBV4 B2JBV4 B7H7R5 F2K4D2 F5UM67 K9VWW9 K9VWW9 K9ZH24
    Aspartate racemase. [EC: 5.1.1.13]
    L-aspartate = D-aspartate.
    • Also acts, at half the rate, on L-alanine.
    		 8 B2IXK1 B2J0Z5 B2J682 B2J682 B2J685 G6FSF2 K9XF76 W6VR80
    Phenylalanine racemase (ATP-hydrolyzing). [EC: 5.1.1.11]
    ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine.
      		 5 A0A0K1EH67 B2IXJ9 K9XUB9 Q3MCQ2 Q3MCQ2
      Ornithine racemase. [EC: 5.1.1.12]
      L-ornithine = D-ornithine.
        		 3 F5UM74 K9VPK5 K9XUI8
        [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.
        		 3 A0A0F6U5V1 A0A0F6U5V1 A0A0F6U5V1
        L-aminoadipate-semialdehyde dehydrogenase. [EC: 1.2.1.31]
        (S)-2-amino-6-oxohexanoate + NAD(P)(+) + H(2)O = L-2-aminoadipate + NAD(P)H.
          		 2 B2J682 B2J682
          4-hydroxybenzoate--CoA ligase. [EC: 6.2.1.27]
          ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate + 4-hydroxybenzoyl-CoA.
            		 2 K9VWW9 K9VWW9
            Oleoyl-[acyl-carrier-protein] hydrolase. [EC: 3.1.2.14]
            Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-carrier-protein] + oleate.
            • Acts on [acyl-carrier-protein] thioesters of fatty acids from C(12) to C(18), but the derivative of oleic acid is hydrolyzed much more rapidly than any other compound tested.
            		 2 B2JBV4 B2JBV4
            N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase. [EC: 6.3.2.26]
            L-2-aminohexanedioate + L-cysteine + L-valine + 3 ATP + H(2)O = N-(L-5- amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + 3 AMP + 3 diphosphate.
            • The enzyme contains 4'-phosphopantetheine, which may be involved in the mechanism of the reaction.
            • Forms part of the penicillin biosynthesis pathway.
            		 2 K9XML5 Q3MCQ0
            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.
            		 1 B2IXK1
            O-succinylbenzoate--CoA ligase. [EC: 6.2.1.26]
            ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 2-succinylbenzoyl- CoA.
              		 1 B2IXJ9
              [Acyl-carrier-protein] S-acetyltransferase. [EC: 2.3.1.38]
              Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier- protein].
              • Essential, along with EC 2.3.1.39, for the initiation of fatty-acid biosynthesis in bacteria.
              • The substrate acetyl-CoA protects the enzyme against inhibition by N-ethylmaleimide or iodoacetamide.
              • This is one of the activities associated with EC 2.3.1.180.
              		 1 Q3MCQ0
              Long-chain-fatty-acid--[acyl-carrier-protein] ligase. [EC: 6.2.1.20]
              ATP + a long-chain fatty acid + an [acyl-carrier-protein] = AMP + diphosphate + a long-chain acyl-[acyl-carrier-protein].
              • The enzyme ligates long chain fatty acids (with aliphatic chain of 13-22 carbons) to an acyl-carrier protein.
              • Not identical with EC 6.2.1.3.
              		 1 F5UM67