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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 24030: Non-ribosomal peptide synthetase PstA

There are 17 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
Phenylalanine racemase (ATP-hydrolyzing). [EC: 5.1.1.11]
ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine.
    		 42 A0A068QTN6 A0A068QUR4 A0A068R289 A0A077N7Q1 A0A077NAM3 A0A077ND30 A0A077NG65 A0A077NX39 A0A077NX85 A0A077P0X1
    (32 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).
    		 31 A0A0A1I4U9 A0A0C5VL95 A0A0C5VV47 A0A0F6J097 A0A0G8BTE2 A0A0G8ED28 A0A0G8EF83 A0A0G8EYR1 A0A0G8EZ77 A0A0N7H7Y9
    (21 more...)
    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.
    		 28 A0A080UAJ6 A0A095F867 A0A095FD41 A0A0C1U9M0 A0A0C1U9M0 A0A0C1U9P3 A0A1J0JHK4 A0A1L3NX86 H0U5U2 K5BDR2
    (18 more...)
    Glutamate racemase. [EC: 5.1.1.3]
    L-glutamate = D-glutamate.
      		 27 A0A0B6X989 A0A0N1NPQ9 A0A1C4FFB3 A0A1E7ZN58 A0A1I9ZIL2 B2JBV4 B4AIX1 B4AIX2 E1UL89 E1UL89
      (17 more...)
      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.
      		 16 A0A0E1LNR6 A0A0N1NKN2 E2Q5R1 E2Q5R1 G8SBN4 I2C680 P19787 P19787 P25464 P25464
      (6 more...)
      Aspartate racemase. [EC: 5.1.1.13]
      L-aspartate = D-aspartate.
      • Also acts, at half the rate, on L-alanine.
      		 16 A0A031HPP2 A0A098BKA4 A0A098BKA4 A0A1G4LJW9 A0A1G4LJW9 F5UNY4 F6AUU5 G6FSF2 G7MBA9 K9QEG2
      (6 more...)
      Ornithine racemase. [EC: 5.1.1.12]
      L-ornithine = D-ornithine.
        		 10 A0A068QUR4 A0A068R289 A0A073CX32 A0A077QM48 A0A099K916 A7IZW3 D3UWT0 E1UL88 G3J032 Q0S5H6
        O-succinylbenzoate--CoA ligase. [EC: 6.2.1.26]
        ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 2-succinylbenzoyl- CoA.
          		 9 A0A077NAM3 A0A077NG65 A0A077NX39 A0A077P0X1 A0A077PBE6 A0A077PSE9 A0A0B6X989 D3V3G3 W1IPT8
          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.
          		 6 B2J0Y5 G3J032 G6G0G1 I8U1X2 I8U1X2 I8U1X2
          [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 A0A0F6RML1 A0A1G4LJN3 T2IWQ9
          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.
            		 3 A0A0P4UNA7 I0K3K8 Q0S5H6
            D-arabinose isomerase. [EC: 5.3.1.3]
            D-arabinose = D-ribulose.
            • The enzyme binds the closed form of the sugar and catalyzes ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene- diol mechanism.
            • The enzyme catalyzes the aldose-ketose isomerization of several sugars.
            • Most enzymes also catalyze the reaction of EC 5.3.1.25.
            • The enzyme from the bacterium Falsibacillus pallidus also converts D-altrose to D-psicose.
            • Cf. EC 5.3.1.4.
            		 3 E0RJP4 E0RJP4 E0RJP4
            [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.
            		 3 A0A0E1LNR6 A0A0N1NPQ9 I2C680
            4-hydroxybenzoate--CoA ligase. [EC: 6.2.1.27]
            ATP + 4-hydroxybenzoate + CoA = AMP + diphosphate + 4-hydroxybenzoyl-CoA.
              		 2 A0A0N1NKN2 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.
              		 1 B2JBV4
              Lovastatin nonaketide synthase. [EC: 2.3.1.161]
              9 malonyl-CoA + 11 NADPH + S-adenosyl-L-methionine + holo-[lovastatin nonaketide synthase] = dihydromonacolin L-[lovastatin nonaketide synthase] + 9 CoA + 9 CO(2) + 11 NADP(+) + S-adenosyl-L-homocysteine + 6 H(2)O.
              • This fungal enzyme system comprises a multi-functional polyketide synthase (PKS) and an enoyl reductase.
              • The PKS catalyzes many of the chain building reactions of EC 2.3.1.85, as well as a reductive methylation and a Diels-Alder reaction, while the reductase is responsible for three enoyl reductions that are necessary for dihydromonacolin L acid production.
              		 1 A0A0B6XAG6
              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.
              		 1 D2YVM7
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