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CATH Superfamily 3.40.50.720

NAD(P)-binding Rossmann-like 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:

"
NAD(P)-binding Rossmann-like 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 291021: Type I polyketide synthase

There are 20 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
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.
 170 A0A011QU70 A0A011QU70 A0A063BLL2 A0A063BLL2 A0A073C9W9 A0A073C9W9 A0A086LSF6 A0A086LSF6 A0A0C5PRK7 A0A0C5PRK7
(160 more...)
Mycocerosate synthase. [EC: 2.3.1.111]
(1) A long-chain acyl-CoA + 3 methylmalonyl-CoA + 6 NADPH + a holo- [mycocerosate synthase] = a trimethylated-mycocerosoyl-[mycocerosate synthase] + 4 CoA + 3 CO(2) + 6 NADP(+) + 3 H(2)O. (2) A long-chain acyl-CoA + 4 methylmalonyl-CoA + 8 NADPH + a holo- [mycocerosate synthase] synthase = a tetramethylated-mycocerosoyl- [mycocerosate synthase] + 5 CoA + 4 CO(2) + 8 NADP(+) + 4 H(2)O.
  • This mycobacterial enzyme loads long-chain fatty acyl groups from their CoA esters and extends them by incorporation of three or four methylmalonyl (but not malonyl) residues, to form tri- or tetramethyl-branched fatty-acids, respectively, such as 2,4,6,8- tetramethyloctacosanoate (C(32)-mycocerosate).
  • Since the enzyme lacks a thioesterase domain, the products remain bound to the enzyme and require additional enzyme(s) for removal.
  • Even though the enzyme can accept C(6) to C(20) substrates in vitro, it prefers to act on C(14)-C(20) substrates in vivo.
 170 A0A086LSF6 A0A086LSF6 A0A0C5PRK7 A0A0C5PRK7 A0A0C5PRK7 A0A0C5PRK7 A0A0C5PRK7 A0A0C5PRK7 A0A0C5Q128 A0A0C5Q128
(160 more...)
[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.
 160 A0A060Q8N5 A0A060Q8N5 A0A086LSF6 A0A086LSF6 A0A0A1FDT8 A0A0A1FDT8 A0A0A1FDT8 A0A0A1FDT8 A0A0A1FIB3 A0A0A1FIB3
(150 more...)
Beta-ketoacyl-[acyl-carrier-protein] synthase I. [EC: 2.3.1.41]
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
  • Responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain.
  • Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids.
  • Can use fatty acyl thioesters of ACP (C(2) to C(16)) as substrates, as well as fatty acyl thioesters of Co-A (C(4) to C(16)).
  • The substrate specificity is very similar to that of EC 2.3.1.179 with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C(16)-Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature.
 84 A0A0D6I7K8 A0A0D6I7K8 A0A0E8NTV0 A0A0E8NTV0 A0A0E8TX81 A0A0E8TX81 A0A0H3LK68 A0A0H3LK68 A0A0H3M9Y4 A0A0H3M9Y4
(74 more...)
3-oxoacyl-[acyl-carrier-protein] reductase. [EC: 1.1.1.100]
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl- carrier-protein] + NADPH.
  • Exhibits a marked preference for [acyl-carrier-protein] derivatives over CoA derivatives as substrates.
 22 A0A086LSF6 A0A086LSF6 A0A0C5Q0M9 A0A0C5Q0M9 A0A125YWR8 A0A125YWR8 A0A125YWR9 A0A125YWR9 A0A1J1KIQ4 A0A1J1KIQ4
(12 more...)
Beta-ketoacyl-[acyl-carrier-protein] synthase II. [EC: 2.3.1.179]
(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier- protein] = (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
  • Involved in the dissociated (or type II) fatty acid biosynthesis system that occurs in plants and bacteria.
  • While the substrate specificity of this enzyme is very similar to that of EC 2.3.1.41, it differs in that palmitoleoyl-ACP is not a good substrate of EC 2.3.1.41 but is an excellent substrate of this enzyme.
  • The fatty-acid composition of Escherichia coli changes as a function of growth temperature, with the proportion of unsaturated fatty acids increasing with lower growth temperature.
  • Controls the temperature-dependent regulation of fatty-acid composition, with mutants lacking this acivity being deficient in the elongation of palmitoleate to cis-vaccenate at low temperatures.
 18 A0A080URI7 A0A080URI7 A0A095G6H9 A0A095G6H9 A0A0B5P0D7 A0A0B5P0D7 A0A0B5P0D7 A0A0B5P0D7 A0A0H3E374 A0A0H3E374
(8 more...)
NADPH:quinone reductase. [EC: 1.6.5.5]
NADPH + 2 quinone = NADP(+) + 2 semiquinone.
  • Specific for NADPH.
  • Catalyzes the one-electron reduction of certain quinones, with the orthoquinones 1,2-naphthoquinone and 9,10-phenanthrenequinone being the best substrates.
  • Dicoumarol (cf. EC 1.6.5.2) and nitrofurantoin are competitive inhibitors with respect to the quinone substrate.
  • The semiquinone free-radical product may be non-enzymically reduced to the hydroquinone or oxidized back to quinone in the presence of O(2).
  • Abundant in the lens of the eye of some mammalian species.
 18 A0A063BLL2 A0A063BLL2 A0A0D5M5S0 A0A0D5M5S0 B2J016 B2J016 G3J044 G3J044 G4HYP5 G4HYP5
(8 more...)
Phenylalanine racemase (ATP-hydrolyzing). [EC: 5.1.1.11]
ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine.
    		 16 A0A073CGA8 A0A073CGA8 A0A0S4TW17 A0A0S4TW17 A0A0S4TW17 A0A0S4TW17 A0A1J1KKI6 A0A1J1KKI6 A0A1J1KUP4 A0A1J1KUP4
    (6 more...)
    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.
    		 12 A0A086LSF6 A0A086LSF6 A0A125YWR8 A0A125YWR8 A0A125YWR9 A0A125YWR9 B8MEL0 B8MEL0 B8MPC7 B8MPC7
    (2 more...)
    6-methylsalicylic acid synthase. [EC: 2.3.1.165]
    Acetyl-CoA + 3 malonyl-CoA + NADPH = 6-methylsalicylate + 4 CoA + 3 CO(2) + NADP(+).
    • A multienzyme complex with a 4'-phosphopantetheine prosthetic group on the acyl carrier protein.
    • It has a similar sequence to vertebrate type I fatty acid synthase.
    • Acetoacetyl-CoA can also act as a starter molecule.
    		 12 A0A073CMC6 A0A073CMC6 B2IYP4 B2IYP4 B2J539 B2J539 C7PSF7 C7PSF7 F0SIS4 F0SIS4
    (2 more...)
    Mycolipanoate synthase. [EC: 2.3.1.252]
    A long-chain acyl-CoA + 3 (R)-methylmalonyl-CoA + 6 NADPH + holo- [mycolipanoate synthase] = mycolipanoyl-[mycolipanoate synthase] + 4 CoA + 3 CO(2) + 6 NADP(+) + 3 H(2)O.
    • This mycobacterial enzyme accepts long-chain fatty acyl groups from their CoA esters and extends them by incorporation of three methylmalonyl (but not malonyl) residues, forming trimethyl-branched fatty-acids such as (2S,4S,6S)-2,4,6-trimethyl-tetracosanoate (C(27)- mycolipanoate).
    • Since the enzyme lacks a thioesterase domain, the product remains bound to the enzyme and requires additional enzyme(s) for removal.
    		 10 A0A089QRB9 A0A089QRB9 A0A0E8NV99 A0A0E8NV99 A0A0H3L8P3 A0A0H3L8P3 A5U1M9 A5U1M9 M8D8M3 M8D8M3
    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.
    		 10 A0A086LSF6 A0A086LSF6 A0A125YWR8 A0A125YWR8 A0A125YWR9 A0A125YWR9 B9PYE4 B9PYE4 G3J034 G3J034
    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).
    		 10 A0A150KYP0 A0A150KYP0 A0A150KZ21 A0A150KZ21 A0A150KZ21 A0A150KZ21 A0A150KZ21 A0A150KZ21 K9XYL3 K9XYL3
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase. [EC: 6.3.2.13]
    ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6- diaminoheptanedioate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L- alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate.
    • Involved in the synthesis of a cell-wall peptide.
    • This enzyme adds diaminopimelate in Gram-negative organisms and in some Gram-positive organisms; in others EC 6.3.2.7 adds lysine instead.
    • It is the amino group of the L-center of the diaminopimelate that is acylated.
    		 6 A0A0E1U4U9 A0A0E1U4U9 A0A0E1UX21 A0A0E1UX21 B1H622 B1H622
    (S)-2-hydroxy-acid oxidase. [EC: 1.1.3.15]
    (S)-2-hydroxy acid + O(2) = 2-oxo acid + H(2)O(2).
    • Exists as two major isoenzymes; the A form preferentially oxidizes short-chain aliphatic hydroxy acids; the B form preferentially oxidizes long-chain and aromatic hydroxy acids.
    • The rat isoenzyme B also acts as EC 1.4.3.2.
    • Formerly EC 1.1.3.1.
    		 4 A0A0E1LP60 A0A0E1LP60 I2C4I9 I2C4I9
    Aspartate racemase. [EC: 5.1.1.13]
    L-aspartate = D-aspartate.
    • Also acts, at half the rate, on L-alanine.
    		 4 A0A0C5PUC2 A0A0C5PUC2 A0A0C5PUC2 A0A0C5PUC2
    Glutamate racemase. [EC: 5.1.1.3]
    L-glutamate = D-glutamate.
      		 4 A0A0C5QFG3 A0A0C5QFG3 I8U1X2 I8U1X2
      Phenylalanine--tRNA ligase. [EC: 6.1.1.20]
      ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl- tRNA(Phe).
        		 2 G4EW23 G4EW23
        2-dehydro-3-deoxy-phosphogluconate aldolase. [EC: 4.1.2.14]
        2-dehydro-3-deoxy-6-phosphate-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate.
        • The enzyme shows no activity with 2-dehydro-3-deoxy-6-phosphate-D- galactonate (cf. EC 4.1.2.55).
        • Also acts on 2-oxobutanoate.
        		 2 A9ECY5 A9ECY5
        8-amino-7-oxononanoate synthase. [EC: 2.3.1.47]
        Pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO(2) + holo-[acyl-carrier protein].
        • The enzyme catalyzes the decarboxylative condensation of L-alanine and pimeloyl-[acyl-carrier protein], a key step in the pathway for biotin biosynthesis.
        • Pimeloyl-CoA can be used with lower efficiency.
        		 2 K9XRL8 K9XRL8
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