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CATH Superfamily 3.40.228.10

Dimethylsulfoxide Reductase, domain 2

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:

"
Dimethylsulfoxide Reductase, domain 2
".

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 5791: Nitrate reductase catalytic subunit

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
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.
 2109 A0A011MYR4 A0A011P2G0 A0A011PVE8 A0A011QYV3 A0A014QAU8 A0A017HL83 A0A017HTJ0 A0A017HWR7 A0A017IF45 A0A021XBM1
(2099 more...)
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.
 1061 A0A011QNK1 A0A011QQ59 A0A014NSI2 A0A017I929 A0A023P0C6 A0A023VC35 A0A023Z6B4 A0A024KLS4 A0A025C2Q0 A0A026S3A6
(1051 more...)
Formate dehydrogenase (acceptor). [EC: 1.1.99.33]
Formate + acceptor = CO(2) + reduced acceptor.
  • Formate dehydrogenase H is a cytoplasmic enzyme that oxidizes formate without oxygen transfer, transferring electrons to a hydrogenase.
  • The two enzymes form the formate-hydrogen lyase complex.
  • The enzyme contains a selenocysteine residue.
 196 A0A029HCX8 A0A029IGU7 A0A060V7M7 A0A060VBX9 A0A066T2D6 A0A080M9C2 A0A080SSK0 A0A081M5Q6 A0A084A1A3 A0A084XZ14
(186 more...)
Nitrate reductase (NADH). [EC: 1.7.1.1]
Nitrite + NAD(+) + H(2)O = nitrate + NADH.
  • Formerly EC 1.6.6.1.
 60 A0A024HEM6 A0A031G5M3 A0A062WT05 A0A084UD33 A0A085EXU1 A0A095ATL4 A0A095B0V2 A0A0A0HJY2 A0A0F6XAP5 A0A0H4KSW0
(50 more...)
Ferredoxin--nitrate reductase. [EC: 1.7.7.2]
Nitrite + H(2)O + 2 oxidized ferredoxin = nitrate + 2 reduced ferredoxin + 2 H(+).
    		 46 A0A073CIE5 A0A088E6S7 A0A0A7HJK2 A0A0U5GZJ8 A0A1J0ADT9 A4YF52 A5GPP2 A5GWY3 B8CQX6 D4GTE1
    (36 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.
    		 38 A0A098BMJ7 A0A0B2W3M5 A0A0B6SBV8 A0A0E1VV47 A0A0H2XUS9 A0A0N0VJE8 A0A0P0RPP3 A0A166QYG3 A0A1B4X097 A0A1M8RDZ5
    (28 more...)
    NADPH--hemoprotein reductase. [EC: 1.6.2.4]
    NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein.
    • This enzyme catalyzes the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P450 monooxygenases (e.g. EC 1.14.14.1) by stabilizing the one-electron reduced form of the flavin cofactors FAD and FMN.
    • It also reduces cytochrome b5 and cytochrome c.
    • The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction.
    		 12 A0A063BKL1 A0A0N0NC84 A0A0N1G9N5 A0A0N1NQD3 G0PRS7 G4HUY3 G4I4N0 G7LKB6 N0D0V8 Q0REZ5
    (2 more...)
    Nitrate reductase (NAD(P)H). [EC: 1.7.1.2]
    Nitrite + NAD(P)(+) + H(2)O = nitrate + NAD(P)H.
    • Formerly EC 1.6.6.2.
    		 11 A0A0H3C498 A0A1C0UMF6 A0A1L3R5P7 A0A1L3RCX9 A0A1L3RK43 A0A1L3RSS1 A3RXN7 Q0BRC9 Q9AAI1 S7U0M4
    (1 more...)
    Nitrite reductase (NAD(P)H). [EC: 1.7.1.4]
    Ammonia + 3 NAD(P)(+) + 2 H(2)O = nitrite + 3 NAD(P)H.
    • The enzymes from the fungi Neurospora crassa, Emericella nidulans and Candida nitratophila and the bacterium Aliivibrio fischeri can use either NADPH or NADH as electron donor.
    • Cf. EC 1.7.1.15.
    • Formerly EC 1.6.6.4.
    		 9 E6X8S3 F0RBU7 F4C4C8 F4KUK0 F8EFU7 G2PIF4 G8TEW8 L7ZZ54 W1B2Q1
    Formate dehydrogenase (NADP(+)). [EC: 1.2.1.43]
    Formate + NADP(+) = CO(2) + NADPH.
      		 6 A0A0L0WBE7 A0A0T6A774 A0A0T6AS21 K0B1V1 P77908 X5NUA6
      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.
      		 4 A0A0P6YQR7 A0A1C3IZI8 A3ULU6 Q8E8Y7
      Formate dehydrogenase (cytochrome). [EC: 1.2.2.1]
      Formate + 2 ferricytochrome b1 = CO(2) + 2 ferrocytochrome b1 + 2 H(+).
        		 3 B8CVG3 B8CVG7 Q5E541
        Hydrogen dehydrogenase. [EC: 1.12.1.2]
        H(2) + NAD(+) = H(+) + NADH.
          		 3 A4G245 C3MLV6 C9Y8N4
          NADH:ubiquinone reductase (H(+)-translocating). [EC: 1.6.5.3]
          NADH + ubiquinone + 5 H(+)(In) = NAD(+) + ubiquinol + 4 H(+)(Out).
          • The complex is present in mitochondria and aerobic bacteria.
          • Breakdown of the complex can release EC 1.6.99.3.
          • In photosynthetic bacteria, reversed electron transport through this enzyme can reduce NAD(+) to NADH.
          		 2 A0A1E3L692 Q1PYY4
          Rubredoxin--NAD(+) reductase. [EC: 1.18.1.1]
          2 reduced rubredoxin + NAD(+) + H(+) = 2 oxidized rubredoxin + NADH.
          • The enzyme from Clostridium acetobutylicum reduces rubredoxin, ferricyanide and dichlorophenolindophenol, but not ferredoxin or flavodoxin.
          • The reaction does not occur when NADPH is substituted for NADH.
          • Formerly EC 1.6.7.2.
          		 1 B0SN75
          DNA ligase (NAD(+)). [EC: 6.5.1.2]
          NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta- nicotinamide D-nucleotide.
          • The enzyme, typically found in bacteria, 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 NAD(+), 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 6.5.1.1, EC 6.5.1.6, and EC 6.5.1.7.
          		 1 G8Q316
          Nitric-oxide synthase (NADPH). [EC: 1.14.13.39]
          2 L-arginine + 3 NADPH + 4 O(2) = 2 L-citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O.
          • This eukaryotic enzyme, which is found in plants and animals, consists of oxygenase and reductase domains that are linked via a regulatory calmodulin-binding domain.
          • Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center.
          • May produce superoxide under certain conditions.
          • Cf. EC 1.14.13.165.
          		 1 A0A0H3KRJ1