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CATH Superfamily 3.40.50.1970

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 29 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
3-dehydroquinate synthase. [EC: 4.2.3.4]
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate.
  • The hydrogen atoms on C-7 of the substrate are retained on C-2 of the products.
  • Formerly EC 4.6.1.3.
 1245 A0A009G8Y2 A0A009KMR4 A0A009QPR5 A0A009SAK7 A0A009T8N9 A0A026V6I7 A0A029HHG0 A0A029IJV8 A0A045GU34 A0A049DDN0
(1235 more...)
5-(carboxyamino)imidazole ribonucleotide mutase. [EC: 5.4.99.18]
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxylate.
  • In eubacteria, fungi and plants, this enzyme, along with EC 6.3.4.18, is required to carry out the single reaction catalyzed by EC 4.1.1.21 in vertebrates.
  • In the absence of EC 6.3.2.6, the reaction is reversible.
  • The substrate is readily converted into 5-amino-1-(5-phospho-D- ribosyl)imidazole by non-enzymic decarboxylation.
 232 A0A023YSS6 A0A025C9J7 A0A026UGE1 A0A027ZQ43 A0A028DK66 A0A045JT63 A0A063XG44 A0A069XNQ9 A0A070SYY7 A0A070UHW6
(222 more...)
Alcohol dehydrogenase. [EC: 1.1.1.1]
(1) A primary alcohol + NAD(+) = an aldehyde + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH.
  • Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol.
  • The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
 159 A0A023YWD7 A0A025CD77 A0A026V8A2 A0A028A9Z9 A0A028E6I5 A0A069XIN3 A0A069XKQ8 A0A070SHM3 A0A070UZF6 A0A073FYU1
(149 more...)
Acetaldehyde dehydrogenase (acetylating). [EC: 1.2.1.10]
Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH.
  • Also acts, more slowly, on glycolaldehyde, propanal and butanal.
  • In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39.
  • The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87.
  • Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols.
  • NADP(+) can replace NAD(+) but the rate of reaction is much slower.
 124 A0A023YWD7 A0A025CD77 A0A026V8A2 A0A028A9Z9 A0A028E6I5 A0A069XKQ8 A0A070UZF6 A0A073FYU1 A0A073HWC3 A0A073UK46
(114 more...)
Sn-glycerol-1-phosphate dehydrogenase. [EC: 1.1.1.261]
sn-glycerol 1-phosphate + NAD(P)(+) = glycerone phosphate + NAD(P)H.
  • Responsible for the formation of archaea-specific sn-glycerol-1- phosphate, the first step in the biosynthesis of polar lipids in archaea.
  • It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryotes.
  • The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 2.5.1.41 and EC 2.5.1.42, which together alkylate the hydroxy groups of glycerol 1-phosphate to give unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 to form CDP- unsaturated archaeol.
  • The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine.
  • Activity of the enzyme is stimulated by K(+).
 90 A0A075WHM4 A0A088E7N6 A0A0B5GPM9 A0A0E3MD35 A0A0F8I922 A0A0U2NEY6 A0A162S197 A0A1D2WJA2 A0A1D2WTP7 A0A1D8FKX3
(80 more...)
Glycerol dehydrogenase. [EC: 1.1.1.6]
Glycerol + NAD(+) = glycerone + NADH.
  • Also acts on 1,2-propanediol.
 87 A0A023Z5P2 A0A025C1E3 A0A026US52 A0A027ZR72 A0A028E257 A0A029HDX8 A0A029IIC8 A0A069XJQ0 A0A070FAU5 A0A070T1W7
(77 more...)
Shikimate kinase. [EC: 2.7.1.71]
ATP + shikimate = ADP + shikimate 3-phosphate.
    		 85 A0A083X0N5 A0A083XWA7 A0A0A0UFJ5 A0A0A1GR12 A0A0B0DHB1 A0A0M0VNG4 A0A1D9QLW8 A0A1H6PWB9 A0A1Q2ZZI1 A0A3M7K8K1
    (75 more...)
    Shikimate dehydrogenase. [EC: 1.1.1.25]
    Shikimate + NADP(+) = 3-dehydroshikimate + NADPH.
    • NAD(+) cannot replace NADP(+).
    • In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10.
    		 71 A0A0B0DHB1 A0A1D9QLW8 A0A1H6PWB9 A0A1Q2ZZI1 A0A3M7K8K1 A1CP85 A1D244 A3LSZ2 A4RD09 A5H2P4
    (61 more...)
    3-phosphoshikimate 1-carboxyvinyltransferase. [EC: 2.5.1.19]
    Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O- (1-carboxyvinyl)-3-phosphoshikimate.
      		 71 A0A0B0DHB1 A0A1D9QLW8 A0A1H6PWB9 A0A1Q2ZZI1 A0A3M7K8K1 A1CP85 A1D244 A3LSZ2 A4RD09 A5H2P4
      (61 more...)
      3-dehydroquinate dehydratase. [EC: 4.2.1.10]
      3-dehydroquinate = 3-dehydroshikimate + H(2)O.
        		 71 A0A0B0DHB1 A0A1D9QLW8 A0A1H6PWB9 A0A1Q2ZZI1 A0A3M7K8K1 A1CP85 A1D244 A3LSZ2 A4RD09 A5H2P4
        (61 more...)
        Lactaldehyde reductase. [EC: 1.1.1.77]
        (1) (R)-propane-1,2-diol + NAD(+) = (R)-lactaldehyde + NADH. (2) (S)-propane-1,2-diol + NAD(+) = (S)-lactaldehyde + NADH.
          		 63 A0A025CVW8 A0A026V998 A0A028A6S7 A0A028ECH3 A0A070FDJ5 A0A070STZ0 A0A070URM7 A0A073FR68 A0A073UV83 A0A074HVA0
          (53 more...)
          Maleylacetate reductase. [EC: 1.3.1.32]
          3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H.
            		 41 A0A024HJE8 A0A1B1KI51 A0A1H6PNZ4 A0A1M6YEZ9 A0A1M6YG72 A0A1P9YF24 A0A1T5F9R1 A0A2Z6IT91 A0A2Z6ITA6 A0A2Z6ITG5
            (31 more...)
            Phosphoribosylaminoimidazole carboxylase. [EC: 4.1.1.21]
            5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1- (5-phospho-D-ribosyl)imidazole + CO(2).
            • While this is the reaction that occurs in vertebrates during purine biosynthesis, two enzymes are required to carry out the same reaction in Escherichia coli, namely EC 6.3.4.18 and EC 5.4.99.18.
            • 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole is not a substrate.
            		 26 A0A024RD93 A0A0F6MM25 A6ZNX5 M2CAY7 M2CMK9 N1NVS9 O28997 O74197 P0C017 P0CQ36
            (16 more...)
            1,3-propanediol dehydrogenase. [EC: 1.1.1.202]
            Propane-1,3-diol + NAD(+) = 3-hydroxypropanal + NADH.
              		 18 A0A0E1C832 A0A0H3H3A3 A0A1D3KE64 A0A1R0FTL1 A0A2I8SBF8 A0A2X3IF95 A0A3V3HTA7 A0A3V3R5A1 A0A3V5P702 A0A401ASZ5
              (8 more...)
              Hydroxyacid-oxoacid transhydrogenase. [EC: 1.1.99.24]
              (1) (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2- hydroxyglutarate. (2) 4-hydroxybutanoate + 2-oxoglutarate = succinic semialdehyde + (R)-2- hydroxyglutarate.
                		 15 A6QP15 A8WTJ7 B4GHJ1 Q08B39 Q17EN4 Q28XT3 Q4QQW3 Q54GJ7 Q5RF11 Q6P371
                (5 more...)
                2-deoxy-scyllo-inosose synthase. [EC: 4.2.3.124]
                D-glucose-6-phosphate = 2-deoxy-L-scyllo-inosose + phosphate.
                • Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin.
                • Requires an NAD(+) cofactor, which is transiently reduced during the reaction.
                • The enzyme from the bacterium Bacillus circulans forms a complex with the glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase (EC 4.3.3.6), which appears to stabilize the complex.
                		 10 A0A1C4WLZ3 A0A1Y2NSL7 Q2MF16 Q2MF70 Q2MFP1 Q4R0W3 Q53U19 Q6L738 Q70KD0 Q9S5E2
                Phosphoribosylaminoimidazolesuccinocarboxamide synthase. [EC: 6.3.2.6]
                ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamido)succinate.
                • Forms part of the purine biosynthesis pathway.
                		 9 A0A024RD93 P22234 P38024 P51583 Q10457 Q54QE4 Q5RB59 Q9DCL9 Q9I7S8
                Alcohol dehydrogenase (NADP(+)). [EC: 1.1.1.2]
                An alcohol + NADP(+) = an aldehyde + NADPH.
                • Some members of this group oxidize only primary alcohols; others act also on secondary alcohols.
                • May be identical with EC 1.1.1.19, EC 1.1.1.33 and EC 1.1.1.55.
                • Re-specific with respect to NADPH.
                		 6 A0A3F3EGK5 B0K3U7 C7ITL3 F1ZWV1 Q24857 Q9F282
                Long-chain-alcohol dehydrogenase. [EC: 1.1.1.192]
                A long-chain alcohol + 2 NAD(+) + H(2)O = a long-chain carboxylate + 2 NADH.
                • Hexadecanol is a good substrate.
                		 6 A0A0Q0UF98 A0A0Q1EJF7 A0A1W6VS82 A0A1W6VV45 A4IP64 A4ISB9
                2-epi-5-epi-valiolone synthase. [EC: 4.2.3.152]
                D-sedoheptulose 7-phosphate = 2-epi-5-epi-valiolone + phosphate.
                • The enzyme is highly specific for alpha-D-sedoheptulopyranose 7-phosphate.
                • It requires a divalent metal ion (Zn(2+) or Co(2+)) and an NAD(+) cofactor, which is transiently reduced during the reaction.
                • The enzyme is involved in the biosynthesis of C(7)N-aminocyclitol natural products, such as the valienamine moiety of the antidiabetic drug acarbose and the crop protectant validamycin A.
                • Cf. EC 4.2.3.154 and EC 4.2.3.155.
                		 6 A1YPR2 A8D7K2 B0B0T7 E3FKM2 H2K887 Q9ZAE9
                Methanol dehydrogenase (nicotinoprotein). [EC: 1.1.99.37]
                Methanol + acceptor = formaldehyde + reduced acceptor.
                • Nicotinoprotein methanol dehydrogenases have a tightly bound NADP+/NADPH cofactor that does not dissociate during the catalytic process.
                • Instead, the cofactor is regenerated by a second substrate or electron carrier.
                • While the in vivo electron acceptor is not known, N,N-dimethyl-4- nitrosoaniline (NDMA) can serve this function in vitro.
                • The enzyme has been detected in several Gram-positive methylotrophic bacteria, including Amycolatopsis methanolica, Rhodococcus rhodochrous and Rhodococcus erythropolis.
                • These enzymes are decameric, and possess a 5-fold symmetry.
                • Some of the enzymes can also dismutate formaldehyde to methanol and formate.
                		 5 A0A1Q4TVU7 C5MRT8 Q53062 Q9RCG0 X5KSS9
                Demethyl-4-deoxygadusol synthase. [EC: 4.2.3.154]
                D-sedoheptulose 7-phosphate = demethyl-4-deoxygadusol + phosphate + H(2)O.
                • The enzyme, characterized from the cyanobacterium Nostoc punctiforme PCC 73102, is involved in the biosynthesis of the sunscreen compound shinorine.
                • Cf. EC 4.2.3.152 and EC 4.2.3.155.
                		 3 A0A1W5CLR4 B2J6X9 Q3M6C3
                Aldehyde dehydrogenase (NAD(+)). [EC: 1.2.1.3]
                An aldehyde + NAD(+) + H(2)O = a carboxylate + NADH.
                • Wide specificity, including oxidation of D-glucuronolactone to D-glucarate.
                • Formerly EC 1.1.1.70.
                		 3 A0A0K2A0G4 A0A2P8MA19 P33744
                2-epi-valiolone synthase. [EC: 4.2.3.155]
                D-sedoheptulose 7-phosphate = 2-epi-valiolone + phosphate.
                • The enzyme, characterized from the bacteria Actinosynnema mirum and Stigmatella aurantiaca DW4/3-1, produces 2-epi-valiolone, which is believed to function as a precursor in aminocyclitol biosynthesis.
                • Cf. EC 4.2.3.152 and EC 4.2.3.154.
                		 3 A0A347PX92 C6WFL3 Q08VU0
                4-hydroxybutyrate dehydrogenase. [EC: 1.1.1.61]
                4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH.
                  		 2 B9E5D8 P38945
                  Pyridinium-3,5-biscarboxylic acid mononucleotide synthase. [EC: 2.5.1.143]
                  Deamido-NAD(+) + hydrogencarbonate = AMP + pyridinium-3,5-biscarboxylate mononucleotide.
                  • This enzyme, found in the bacterium Lactobacillus plantarum, is involved in the biosynthesis of a nickel-pincer cofactor.
                  • It carboxylates the pyridinium ring of deamido-NAD(+) and cleaves the phosphoanhydride bond to release AMP and generate pyridinium-3,5- biscarboxylic acid mononucleotide (P2CMN).
                  		 1 F9UST0
                  Methanol dehydrogenase. [EC: 1.1.1.244]
                  Methanol + NAD(+) = formaldehyde + NADH.
                    		 1 P31005
                    3-deoxy-alpha-D-manno-octulosonate 8-oxidase. [EC: 1.1.3.48]
                    3-deoxy-alpha-D-manno-octulopyranosonate + O(2) = 3,8-dideoxy-8-oxo- alpha-D-manno-octulosonate + H(2)O(2).
                    • The enzyme, characterized from the bacterium Shewanella oneidensis, is involved in the formation of 8-amino-3,8-dideoxy-alpha-D-manno- octulosonate, an aminated form of Kdo found in lipopolysaccharides of members of the Shewanella genus.
                    • Cf. EC 2.6.1.109.
                    		 1 Q8EEB0
                    Phosphonoacetaldehyde reductase (NADH). [EC: 1.1.1.309]
                    2-hydroxyethylphosphonate + NAD(+) = phosphonoacetaldehyde + NADH.
                    • The enzyme from Streptomyces viridochromogenes catalyzes a step in the biosynthesis of phosphinothricin tripeptide, the reduction of phosphonoacetaldehyde to 2-hydroxyethylphosphonate.
                    • The preferred cofactor is NADH, lower activity with NADPH.
                    		 1 D9XF45