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CATH Superfamily 2.60.40.420

Cupredoxins - blue copper proteins

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:

"
Cupredoxins - blue copper proteins
".

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 24014: Dissimilatory copper-containing nitrite reductase

There are 4 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
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.
 1090 A0A017HSU7 A0A017HSU7 A0A021X0B0 A0A021X0B0 A0A059XHD5 A0A059XHD5 A0A059XKN5 A0A059XKN5 A0A059XRJ6 A0A059XRJ6
(1080 more...)
FAD synthetase. [EC: 2.7.7.2]
ATP + FMN = diphosphate + FAD.
  • Highly specific for ATP as phosphate donor.
  • The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates.
  • While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26.
 32 A0A0E1X816 A0A0E1X816 A0A0M1WHT5 A0A0M1WHT5 A0A0M2Y1D2 A0A0M2Y1D2 B0ZTC9 B0ZTC9 C0G9J7 C0G9J7
(22 more...)
Transferred entry: 1.7.2.1. [EC: 1.7.99.3]
    		18 Q6N2A5 Q6N2A5 Q6N4N1 Q6N4N1 Q7X565 Q7X565 Q8GIL9 Q8GIL9 Q8GIM0 Q8GIM0
    (8 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.
    		 2 X4Y5Q4 X4Y5Q4
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