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CATH Superfamily 3.90.1230.10

Nitric Oxide Synthase; Chain A, domain 3

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Nitric Oxide Synthase; Chain A, domain 3
".

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 1: Nitric oxide synthase, brain

There are 2 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
Nitric-oxide synthase (flavodoxin). [EC: 1.14.14.47]
2 L-arginine + 3 reduced flavodoxin + 4 O(2) = 2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H(2)O.
  • The enzyme, found in bacteria and archaea, consist of only an oxygenase domain and functions together with bacterial ferredoxins or flavodoxins.
  • The orthologous enzymes from plants and animals also contain a reductase domain and use only NADPH as the electron donor (cf. EC 1.14.13.39).
  • Formerly EC 1.14.13.165.
 221 A0A0D1H6Z1 A0A0D1H6Z1 A0A0D1H6Z1 A0A0D1H6Z1 A0A0D1H6Z1 A0A0D1H6Z1 A0A0D1H6Z1 A0A0D1H6Z1 A0A0D1H6Z1 A0A0D1H6Z1
(211 more...)
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.
  • The enzyme consists of linked oxygenase and reductase domains.
  • The eukaryotic enzyme binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin, and its two domains 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.
  • The reductase domain of the enzyme from the bacterium Sorangium cellulosum utilizes a [2Fe-2S] cluster to transfer the electrons from NADPH to the active center.
  • Cf. EC 1.14.14.47.
 27 B3VK56 B3VK56 O19132 O54705 O61608 O62699 P29473 P29473 P29474 P29475
(17 more...)