CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 1 | Mainly Alpha | 
|   | 1.20 | Up-down Bundle | 
|   | 1.20.89 | Nitrogenase Molybdenum-iron Protein, subunit B; domain 4 | 
|   | 1.20.89.10 | Nitrogenase Molybdenum-iron Protein, subunit B, domain 4 | 
Domain Context
CATH Clusters
| Superfamily | Nitrogenase Molybdenum-iron Protein, subunit B, domain 4 | 
| Functional Family | 
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)
| P07328 | NIFD_AZOVI Azotobacter vinelandii Nitrogenase molybdenum-iron protein alpha chain | 
PDB Structure
| PDB | 1G20 | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | MgATP-Bound and nucleotide-free structures of a nitrogenase protein complex between the Leu 127 Delta-Fe-protein and the MoFe-protein. Biochemistry | 
