IPR014285
Nitrogen fixation negative regulator NifL
InterPro entry
Short name | N_fixation_neg-reg_NifL |
Description
NifL from Azotobacter vinelandii senses both the redox and fixed nitrogen status to regulate nitrogen fixation. NifL acts by modulating the activity of the nitrogen fixation positive regulator protein NifA; NifL inhibits NifA in response to oxygen and low level of fixed nitrogen. NifA and NifL are encoded by adjacent genes. NifL is FAD-containing, and has a domain architecture similar to that of the cytoplasmic histidine protein kinases, containing two N-terminal PAS domains and a C-terminal transmitter region containing a conserved histidine residue (H domain) and a nucleotide binding GHKL domain corresponding to the catalytic core of the histidine kinases
[1]. However, NifL does not exhibit kinase activity and regulates its partner NifA by direct protein-protein interactions rather than phosphorylation.
References
1.Role of the H domain of the histidine kinase-like protein NifL in signal transmission. Little R, Martinez-Argudo I, Perry S, Dixon R. J. Biol. Chem. 282, 13429-37, (2007). View articlePMID: 17355964
GO terms
biological process
molecular function
- None
cellular component
- None
Cross References
ENZYME
Contributing Member Database Entry
- NCBIfam:TIGR02938