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CATH Superfamily 3.30.70.20

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: 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.
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FunFam 39899: Nitrate reductase, beta subunit

There are 13 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
Formate dehydrogenase. [EC: 1.2.1.2]
Formate + NAD(+) = CO(2) + NADH.
  • The enzyme from most aerobic organisms is devoid of redox-active centers but that from the proteobacterium Methylosinus trichosporium contains iron-sulfur centers, flavin and a molybdenum center.
  • Together with EC 1.12.1.2, forms a system previously known as formate hydrogenlyase.
 2196 A0A017I2J8 A0A017I2J8 A0A017II69 A0A017II69 A0A023V6K6 A0A023V6K6 A0A023YWW0 A0A023YWW0 A0A023Z5H0 A0A023Z5H0
(2186 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.
 382 A0A026UKD2 A0A026UKD2 A0A027U8K0 A0A027U8K0 A0A028AES9 A0A028AES9 A0A028E798 A0A028E798 A0A037YGB5 A0A037YGB5
(372 more...)
Glycolaldehyde dehydrogenase. [EC: 1.2.1.21]
Glycolaldehyde + NAD(+) + H(2)O = glycolate + NADH.
    		 192 A0A0D6G2X9 A0A0D6G2X9 A0A0E1NIP6 A0A0E1NIP6 A0A0F5BE98 A0A0F5BE98 A0A0F6B1I2 A0A0F6B1I2 A0A0F6B9K6 A0A0F6B9K6
    (182 more...)
    Formate dehydrogenase (cytochrome). [EC: 1.2.2.1]
    Formate + 2 ferricytochrome b1 = CO(2) + 2 ferrocytochrome b1 + 2 H(+).
      		 118 A0A060V0Y0 A0A060V0Y0 A0A066SRA7 A0A066SRA7 A0A066T5A6 A0A066T5A6 A0A087FN36 A0A087FN36 A0A090NEI1 A0A090NEI1
      (108 more...)
      Nitrate reductase. [EC: 1.7.99.4]
      Nitrite + acceptor = nitrate + reduced acceptor.
      • The Pseudomonas enzyme is a cytochrome, but the enzyme from Micrococcus halodenitrificans is an iron protein containing molybdenum.
      • Reduced benzyl viologen and other dyes bring about the reduction of nitrate.
      		 114 A0A098AVJ4 A0A098AVJ4 A0A098AVN9 A0A098AVN9 A0A098AYJ8 A0A098AYJ8 A0A098AZX6 A0A098AZX6 A0A098B487 A0A098B487
      (104 more...)
      Dimethylsulfoxide reductase. [EC: 1.8.5.3]
      Dimethylsulfide + menaquinone + H(2)O = dimethylsulfoxide + menaquinol.
      • Also reduces pyridine N-oxide and trimethylamine N-oxide, with lower activity, to the corresponding amines.
      		 42 A0A059ZWW2 A0A059ZWW2 A0A059ZZ96 A0A059ZZ96 A0A069PMU3 A0A069PMU3 A0A090NI62 A0A090NI62 A0A090P418 A0A090P418
      (32 more...)
      Nitrite reductase (cytochrome; ammonia-forming). [EC: 1.7.2.2]
      NH(3) + 2 H(2)O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H(+).
      • The enzyme also reduces nitric oxide and hydroxylamine to ammonia, and sulfite to sulfide.
      		 34 A0A0B6FDC4 A0A0B6FDC4 A0A0E1NEU4 A0A0E1NEU4 A0A0E2Q6P4 A0A0E2Q6P4 A0A0F6LUR7 A0A0F6LUR7 A0A0H3NRE1 A0A0H3NRE1
      (24 more...)
      Oxoglutarate dehydrogenase (succinyl-transferring). [EC: 1.2.4.2]
      2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
      • It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, which also binds multiple copies of EC 1.8.1.4.
      • It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61.
      		 30 A0A069BC62 A0A069BC62 A0A0D5HR40 A0A0D5HR40 A0A0D6JG11 A0A0D6JG11 A0A0E1S7X4 A0A0E1S7X4 A0A0E1UKJ0 A0A0E1UKJ0
      (20 more...)
      Selenate reductase. [EC: 1.97.1.9]
      Selenite + H(2)O + acceptor = selenate + reduced acceptor.
      • The periplasmic enzyme from Thauera selenatis is a complex comprising three heterologous subunits (alpha, beta and gamma).
      • Nitrate, nitrite, chlorate and sulfate are not substrates.
      • A number of compounds, including acetate, lactate, pyruvate, and certain sugars, amino acids, fatty acids, di- and tricarboxylic acids, and benzoate can serve as electron donors.
      		 12 A0A090NI62 A0A090NI62 A0A0S1XBX3 A0A0S1XBX3 C3MLZ1 C3MLZ1 Q394K3 Q394K3 Q3AP62 Q3AP62
      (2 more...)
      Formate dehydrogenase-N. [EC: 1.1.5.6]
      Formate + a quinone = CO(2) + a quinol.
      • Formate dehydrogenase-N oxidizes formate in the periplasm, transferring electrons via the menaquinone pool in the cytoplasmic membrane to a dissimilatory nitrate reductase (EC 1.7.5.1), which transfers electrons to nitrate in the cytoplasm.
      • The system generates proton motive force under anaerobic conditions.
      		 8 A0A073KJU0 A0A073KJU0 A0A0P7JFQ6 A0A0P7JFQ6 Q8E8Z0 Q8E8Z0 Q8EKJ0 Q8EKJ0
      Ferredoxin hydrogenase. [EC: 1.12.7.2]
      H(2) + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H(+).
      • Can use molecular hydrogen for the reduction of a variety of substances.
      • Formerly EC 1.12.1.1, EC 1.12.7.1, EC 1.18.3.1, EC 1.18.99.1, and EC 1.98.1.1.
      		 6 A0A0E1NG83 A0A0E1NG83 A0A0H3NN12 A0A0H3NN12 F4N749 F4N749
      Phenylacetyl-CoA dehydrogenase. [EC: 1.17.5.1]
      Phenylacetyl-CoA + H(2)O + 2 quinone = phenylglyoxylyl-CoA + 2 quinol.
      • The enzyme is specific for phenylacetyl-CoA as substrate.
      • Phenylacetate, acetyl-CoA, benzoyl-CoA, propanoyl-CoA, crotonyl-CoA, succinyl-CoA and 3-hydroxybenzoyl-CoA cannot act as substrates.
      • The oxygen atom introduced into the product, phenylglyoxylyl-CoA, is derived from water and not molecular oxygen.
      • Duroquinone, menaquinone and 2,6-dichlorophenolindophenol (DCPIP) can act as acceptor, but the likely physiological acceptor is ubiquinone.
      • A second enzyme, EC 3.1.2.25 converts the phenylglyoxylyl-CoA formed into phenylglyoxylate.
      		 2 K0NFD2 K0NFD2
      Nitrite reductase (NO-forming). [EC: 1.7.2.1]
      Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+).
      • The reaction is catalyzed by two types of enzymes, found in the perimplasm of denitrifying bacteria.
      • One type comprises proteins containing multiple copper centers, the other a heme protein, cytochrome cd1.
      • Acceptors include c-type cytochromes such as cytochrome c-550 or cytochrome c-551 from Paracoccus denitrificans or Pseudomonas aeruginosa, and small blue copper proteins such as azurin and pseudoazurin.
      • Cytochrome cd1 also has oxidase and hydroxylamine reductase activities.
      • May also catalyze the reaction of EC 1.7.99.1 since this is a well- known activity of cytochrome cd1.
      • Formerly EC 1.6.6.5, EC 1.7.99.3 and EC 1.9.3.2.
      		 2 A0A073KTN8 A0A073KTN8
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