CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.1980 | Nitrogenase molybdenum iron protein domain |
Domain Context
CATH Clusters
| Superfamily | Nitrogenase molybdenum iron protein domain |
| Functional Family | Nitrogenase molybdenum-iron protein beta chain |
Enzyme Information
| 1.18.6.1 |
Nitrogenase.
based on mapping to UniProt P07329
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.
|
UniProtKB Entries (1)
| P07329 |
NIFK_AZOVI
Azotobacter vinelandii
Nitrogenase molybdenum-iron protein beta chain
|
PDB Structure
| PDB | 5BVG |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor.
Elife
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