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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_2_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 188: Nitric oxide synthase oxygenase

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 (NAD(P)H). [EC: 1.14.13.165]
2 L-arginine + 3 NAD(P)H + 4 O(2) = 2 L-citrulline + 2 nitric oxide + 3 NAD(P)(+) + 4 H(2)O.
  • Most of the bacterial and archaeal enzymes consist of only an oxidase domain and function together with bacterial ferredoxins.
  • The enzyme from the delta-proteobacterium Sorangium cellulosum also includes a reductase domain that binds FAD, FMN and a [2Fe-2S] cluster.
  • The similar enzymes from plants and animals use only NADPH as acceptor (cf. EC 1.14.13.39).
 33 A0A077VL01 A0A0D1H6Z1 A0A0E0VR54 A0A0E1AHT0 A0A0E1VP52 A0A0E1XAR9 A0A0H2XII3 A0A0H3K9F3 A0A0U1MLP1 A0A0U1MPV2
(23 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.
  • 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.
 2 A0A1K9UH61 A0A1M4RHZ3
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