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CATH Superfamily 1.20.89.10

Nitrogenase Molybdenum-iron Protein, subunit B, domain 4

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:

"
Nitrogenase Molybdenum-iron Protein, subunit B, domain 4
".

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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 1 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
Nitrogenase. [EC: 1.18.6.1]
8 reduced ferredoxin + 8 H(+) + N(2) + 16 ATP + 16 H(2)O = 8 oxidized ferredoxin + H(2) + 2 NH(3) + 16 ADP + 16 phosphate.
  • The enzyme is a complex of two components (namely dinitrogen reducatse and dinitrogenase).
  • Dinitrogen reductase is a [4Fe-4S] protein, which, in the presence of two molecules of ATP, transfers an electron from ferredoxin to the dinitrogenase component.
  • Dinitrogenase is a molybdenum-iron protein that reduces dinitrogen to two molecules of ammonia in three successive two-electron reductions via diazene and hydrazine.
  • The reduction is initiated by formation of hydrogen in stoichiometric amounts.
  • Acetylene is reduced to ethylene (but only very slowly to ethane), azide to nitrogen and ammonia, and cyanide to methane and ammonia.
  • In the absence of a suitable substrate, hydrogen is slowly formed.
  • Ferredoxin may be replaced by flavodoxin (see EC 1.19.6.1).
  • The enzyme does not reduce CO (cf. EC 1.18.6.2).
  • Formerly EC 1.18.2.1.
 43 A0A023XXU5 A0A0H3J0Y6 A0A0M9B5V1 A0A1D9N247 A0A1W5CDG5 A0A2A6MMB2 A0A2U8P1R9 A0A2Z5PPK2 C1DGZ8 C1DI23
(33 more...)