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CATH Superfamily 3.40.50.80

Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module

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:

"
Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module
".

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 12699: Dihydroorotate dehydrogenase electron transfer sub...

There are 9 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.
 291 A0A011WLE2 A0A031WA72 A0A037Z7X3 A0A037ZDG8 A0A062XKF1 A0A076I832 A0A085LC59 A0A088RCA6 A0A095YE88 A0A097AU68
(281 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.
 147 A0A015P676 A0A015S802 A0A015TTI6 A0A015UN34 A0A015VB26 A0A015VE36 A0A015VSS6 A0A015XGS5 A0A015XLE2 A0A015ZMS7
(137 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.
 27 A0A0S1XDD9 A0A0S2W8J4 A0A0W8E5A4 A0A0W8F713 A0A0Y4CPL8 A0A139MGU4 A0A139NZJ9 A0A139PTN3 A0A139RFD1 A0A160VRH1
(17 more...)
Glutamate synthase (NADH). [EC: 1.4.1.14]
2 L-glutamate + NAD(+) = L-glutamine + 2-oxoglutarate + NADH.
    		 22 A0A078S1H6 A0A139JRG5 A0A139JRL1 A0A173Z1N1 A0A173Z6R2 A0A174GNU2 A0A174MW27 A0A174NW34 A0A174QAI7 A0A174UDE3
    (12 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.
    		 12 A0A0B5HII0 A0A0N8KQJ3 A0A0Z8HR60 A0A158LKZ6 A0A175A6I3 A0A1M4M4A5 A5LKK2 D3HVF1 E4LQC5 E6K7W6
    (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.
    		 5 A0A097AU68 A0A0B7GTU7 A0A0G4K9Q6 E7NUY6 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.
    		 3 A0A0F4W0B6 A0A0F4W5A0 A0A0F4WM35
    Transferred entry: 1.3.98.1. [EC: 1.3.3.1]
      		1 K0NHL2
      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.
      		 1 A0A1L3TDT4
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