CATH Classification
Level | CATH Code | Description |
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3 | Alpha Beta |
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3.40 | 3-Layer(aba) Sandwich |
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3.40.50 | Rossmann fold |
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3.40.50.300 | P-loop containing nucleotide triphosphate hydrolases |
Domain Context
CATH Clusters
Superfamily | P-loop containing nucleotide triphosphate hydrolases |
Functional Family | Nitrogenase iron protein 4 |
Enzyme Information
1.18.6.1 |
Nitrogenase.
based on mapping to UniProt P00456
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)
P00456 |
NIFH1_CLOPA
Clostridium pasteurianum
Nitrogenase iron protein 1
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PDB Structure
PDB | 1CP2 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum.
J.Mol.Biol.
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