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CATH Superfamily 2.40.30.10

Translation factors

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:

"
Translation factors
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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 38310: Dihydroorotate dehydrogenase, electron transfer su...

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
Ferredoxin--NADP(+) reductase. [EC: 1.18.1.2]
2 reduced ferredoxin + NADP(+) + H(+) = 2 oxidized ferredoxin + NADPH.
  • In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe- 2S] ferredoxins, but in other bacteria it can also reduce bacterial 2[4Fe-4S] ferredoxins and flavodoxin.
  • Formerly EC 1.6.7.1 and EC 1.6.99.4.
 660 A0A011WLE2 A0A011WLE2 A0A031WA72 A0A031WA72 A0A037Z7X3 A0A037Z7X3 A0A037ZDG8 A0A037ZDG8 A0A062XKF1 A0A062XKF1
(650 more...)
Glutamate synthase (NADPH). [EC: 1.4.1.13]
2 L-glutamate + NADP(+) = L-glutamine + 2-oxoglutarate + NADPH.
  • The reaction takes place in the opposite direction.
  • The protein is composed of two subunits, alpha and beta.
  • The alpha subunit is composed of two domains, one hydrolyzing L-glutamine to NH(3) and L-glutamate (cf. EC 3.5.1.2), the other combining the produced NH(3) with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4).
  • The beta subunit transfers electrons to the cosubstrate.
  • The NH(3) is channeled through a 31 A channel in the active protein.
  • In the absence of the beta subunit, coupling between the two domains of the alpha subunit is compromised and some ammonium can be produced.
  • In the intact alpha-beta complex, ammonia production only takes place as part of the overall reaction.
  • Formerly EC 2.6.1.53.
 330 A0A015S802 A0A015S802 A0A015TTI6 A0A015TTI6 A0A015UN34 A0A015UN34 A0A015VB26 A0A015VB26 A0A015VE36 A0A015VE36
(320 more...)
Dihydroorotate oxidase (fumarate). [EC: 1.3.98.1]
(S)-dihydroorotate + fumarate = orotate + succinate.
  • The reaction, which takes place in the cytosol, is the only redox reaction in the de novo biosynthesis of pyrimidine nucleotides.
  • Molecular oxygen can replace fumarate in vitro.
  • Other class 1 dihydroorotate dehydrogenases use either NAD(+) (EC 1.3.1.14) or NADP(+) (EC 1.3.1.15) as electron acceptor.
  • The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor.
  • Formerly EC 1.3.3.1.
 192 A0A083WY05 A0A083WY05 A0A083XWJ6 A0A083XWJ6 A0A0A1GT19 A0A0A1GT19 A0A0A6Y531 A0A0A6Y531 A0A0A8WH88 A0A0A8WH88
(182 more...)
Dihydroorotate dehydrogenase (quinone). [EC: 1.3.5.2]
(S)-dihydroorotate + a quinone = orotate + a quinol.
  • This Class 2 dihydroorotate dehydrogenase enzyme contains FMN.
  • The enzyme is found in eukaryotes in the mitochondrial membrane, in cyanobacteria, and in some Gram-negative and Gram-positive bacteria associated with the cytoplasmic membrane.
  • The reaction is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides.
  • The best quinone electron acceptors for the enzyme from bovine liver are ubiquinone-6 and ubiquinone-7, although simple quinones, such as benzoquinone, can also act as acceptor at lower rates.
  • Methyl-, ethyl-, tert-butyl and benzyl-(S)-dihydroorotates are also substrates, but methyl esters of (S)-1-methyl and (S)-3-methyl and (S)-1,3-dimethyldihydroorotates are not.
  • Class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1), NAD(+) (EC 1.3.1.14) or NADP(+) (EC 1.3.1.15) as electron acceptor.
  • Formerly EC 1.3.99.11.
 72 A0A0A8WH88 A0A0A8WH88 A0A0H3MYJ8 A0A0H3MYJ8 A0A0J0TUT0 A0A0J0TUT0 A0A0N8KQJ3 A0A0N8KQJ3 A0A0U5QBI8 A0A0U5QBI8
(62 more...)
Transferred entry: 1.3.98.1. [EC: 1.3.3.1]
    		48 A0A083WY05 A0A083WY05 A0A083XWJ6 A0A083XWJ6 A0A0A1GT19 A0A0A1GT19 A0A0A6Y531 A0A0A6Y531 A0A0H3MYJ8 A0A0H3MYJ8
    (38 more...)
    Glutamate synthase (NADH). [EC: 1.4.1.14]
    2 L-glutamate + NAD(+) = L-glutamine + 2-oxoglutarate + NADH.
      		 44 A0A078S1H6 A0A078S1H6 A0A139JRG5 A0A139JRG5 A0A139JRL1 A0A139JRL1 A0A173Z1N1 A0A173Z1N1 A0A173Z6R2 A0A173Z6R2
      (34 more...)
      Assimilatory sulfite reductase (NADPH). [EC: 1.8.1.2]
      H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH.
      • The enzyme, which catalyzes the six-electron reduction of sulfite to sulfide, is involved in sulfate assimilation in bacteria and yeast.
      • Different from EC 1.8.99.5, which is involved in prokaryotic sulfur- based energy metabolism.
      • Formerly EC 1.8.99.1.
      		 16 A0A099I4G4 A0A099I4G4 A0A1C7HWZ7 A0A1C7HWZ7 A5TUW2 A5TUW2 D8GL75 D8GL75 D8GM32 D8GM32
      (6 more...)
      Sulfhydrogenase. [EC: 1.12.98.4]
      H(2) + polysulfide(n) = hydrogen sulfide + polysulfide(n-1).
      • The enzyme from the hyperthermophilic archaeon Pyrococcus furiosus is part of two heterotetrameric complexes where the beta and gamma subunits function as sulfur reductase and the alpha and delta subunits function as hydrogenases (EC 1.12.1.3 and EC 1.12.1.4).
      • Sulfur can also be used as substrate, but since it is insoluble in aqueous solution and polysulfide is generated abiotically by the reaction of hydrogen sulfide and sulfur, polysulfide is believed to be the true substrate.
      • Formerly EC 1.97.1.3.
      		 16 A0A087B357 A0A087B357 A0A087D2L5 A0A087D2L5 A0A087DSJ5 A0A087DSJ5 A0A0A7LBT5 A0A0A7LBT5 E7FHW8 E7FHW8
      (6 more...)
      Cytochrome-b5 reductase. [EC: 1.6.2.2]
      NADH + 2 ferricytochrome b5 = NAD(+) + H(+) + 2 ferrocytochrome b5.
        		 12 A0A072MS93 A0A072MS93 A0A0S1XA14 A0A0S1XA14 A0A173ZFV8 A0A173ZFV8 C0BT88 C0BT88 D2QA96 D2QA96
        (2 more...)
        Sulfide dehydrogenase. [EC: 1.8.1.19]
        Hydrogen sulfide + (sulfide)(n) + NADP(+) = (sulfide)(n+1) + NADPH.
        • In the archaeon Pyrococcus furiosus the enzyme is involved in the oxidation of NADPH which is produced in peptide degradation.
        • The enzyme also catalyzes the reduction of sulfur with lower activity.
        		 10 A0A097AU68 A0A097AU68 A0A0B7GTU7 A0A0B7GTU7 A0A1G4G8Z2 A0A1G4G8Z2 E7NUY6 E7NUY6 Q8U194 Q8U194
        Adenosylcobinamide-phosphate guanylyltransferase. [EC: 2.7.7.62]
        GTP + adenosylcobinamide phosphate = diphosphate + adenosylcobinamide- GDP.
        • In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC 2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73) and CobS (EC 2.7.8.26) catalyze reactions in the nucleotide loop assembly pathway, which convert adenosylcobinamide (AdoCbi) into adenosylcobalamin (AdoCbl).
        • CobT and CobC are involved in 5,6-dimethylbenzimidazole activation whereby 5,6-dimethylbenzimidazole is converted to its riboside, alpha-ribazole.
        • The second branch of the nuclotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by the bifunctional enzyme CobU.
        • The final step in adenosylcobalamin biosynthesis is the condensation of AdoCbi-GDP with alpha-ribazole, which is catalyzed by CobS (EC 2.7.8.26), to yield adenosylcobalamin.
        • CobU is a bifunctional enzyme that has both kinase (EC 2.7.1.156) and guanylyltransferase (EC 2.7.7.62) activities.
        • However, both activities are not required at all times.
        • The kinase activity has been proposed to function only when S.typhimurium is assimilating cobinamide whereas the guanylyltransferase activity is required for both assimilation of exogenous cobinamide and for de novo synthesis of adenosylcobalamin.
        • The guanylyltransferase reaction is a two-stage reaction with formation of a CobU-GMP intermediate.
        		 6 A0A0F4W0B6 A0A0F4W0B6 A0A0F4W5A0 A0A0F4W5A0 A0A0F4WM35 A0A0F4WM35
        Ferredoxin--NAD(+) reductase. [EC: 1.18.1.3]
        Reduced ferredoxin + NAD(+) = oxidized ferredoxin + NADH.
        • The reaction is written for a [2Fe-2S] ferredoxin, which is characteristic of some mono- and dioxygenase systems.
        • some anaerobic bacteria have a 2[4Fe-4S] ferredoxin, which transfers two electrons.
        		 6 A0A0S1XFR8 A0A0S1XFR8 F7PL38 F7PL38 Q3AQA3 Q3AQA3
        Deleted entry. [EC: 1.8.99.1]
          		4 A0A0D8IEI0 A0A0D8IEI0 H6LIH3 H6LIH3
          Transferred entry: 1.8.99.5. [EC: 1.8.99.3]
            		4 S0G4P1 S0G4P1 S0G617 S0G617
            DNA ligase (ATP). [EC: 6.5.1.1]
            ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate.
            • The enzyme catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA.
            • Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a lysine residue.
            • The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA).
            • Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate.
            • RNA can also act as substrate, to some extent.
            • Cf. EC 6.5.1.2, EC 6.5.1.6 and EC 6.5.1.7.
            		 2 A8UV91 A8UV91
            Cytochrome-c3 hydrogenase. [EC: 1.12.2.1]
            H(2) + 2 ferricytochrome c3 = 2 H(+) + 2 ferrocytochrome c3.
            • Some forms of the enzyme contain nickel ([NiFe]-hydrogenases) and, of these, some contain selenocysteine ([NiFeSe]-hydrogenases).
            • Methylene blue and other acceptors can also be reduced.
            		 2 Q8KB97 Q8KB97
            Dihydroorotate dehydrogenase (NAD(+)). [EC: 1.3.1.14]
            (S)-dihydroorotate + NAD(+) = orotate + NADH.
            • The enzyme consists of two subunits, an FMN binding catalytic subunit and a FAD and iron-sulfur binding electron transfer subunit.
            • The reaction, which takes place in the cytosol, is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides.
            • Other class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1) or NADP(+) (EC 1.3.1.15) as electron acceptor.
            • The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor.
            		 2 A0A1L3TDT4 A0A1L3TDT4
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