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 protein alpha chain |
Enzyme Information
1.18.6.1 |
Nitrogenase.
based on mapping to UniProt P07328
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.
-!- Composed of two proteins that can be separated but are both required for nitrogenase activity. -!- Dinitrogen reductase is a [4Fe-4S] protein, which, with two molecules of ATP and ferredoxin, generates an electron. -!- The electron is transferred to the other protein, dinitrogenase (molybdoferredoxin). -!- Dinitrogenase is a molybdenum-iron protein that reduces dinitrogen in three succesive two-electron reductions from nitrogen to diimine to hydrazine to two molecules of ammonia; the molybdenum may be replaced by vanadium or iron. -!- 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). -!- Formerly EC 1.18.2.1.
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UniProtKB Entries (1)
P07329 |
NIFK_AZOVI
Azotobacter vinelandii
Nitrogenase molybdenum-iron protein beta chain
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PDB Structure
PDB | 1FP4 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Mechanistic features and structure of the nitrogenase alpha-Gln195 MoFe protein
Biochemistry
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