Respiratory nitrate/nitrite reductase; Bifunctional enzyme involved in the denitrification processes (nitrate respiration). It contains in its N-terminal part a nitrate reductase module required for nitrate assimilation (reducing nitrate to nitrite) using molybdopterin and 1 4Fe-4S cluster as cofactors and in its C-terminal part a nitrite reductase module required for nitrite assimilation (reducing nitrite to ammonia) using FAD, 4Fe-4S cluster and siroheme as cofactors; Belongs to Belongs to the prokaryotic molybdopterin-containing oxidoreductase family and to the nitrite and sulfite r [...]

Nitrite reductase, small subunit; Protein that consists of a Rieske domain; The rieske domain has a 2Fe-2S centre; Associates with NirB and is required for activity reductase of NirB; High confidence in function and specificity.

Periplasmic nitrate reductase, catalytic subunit; Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.

2-Nitropropane dioxygenase catalyzes the oxidation of nitroalkanes to produce the corresponding carbonyl compounds. It acts on 2-nitropropane better than on nitroethane and 1-nitropropane, and anionic forms of nitroalkanes are much better substrates than are neutral forms. It forms a homodimer and uses FMN as cofactor; Localized in the cytoplasm; High confidence in function and specificity.

The diheme cytochrome c napB is the small subunit of the periplasmic nitrate reductase (NAP). NapAB complex receives electrons from the membrane-anchored tetraheme napC protein, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism. Features four consensus sequence Cys-x-x-Cys-His, where the histidine residue is one of the two axial ligands of the heme iron. Binds two hemes. Features an uncleaved signal peptide. Localized in the cytoplasmic membrane; High confidence in function and specificity.

Rubredoxin family protein; Conserved protein containing a C-terminal Rubredoxin-like domain. The most conserved feature of the rubredoxin-like domain is the cluster of four cysteines involved in iron binding (Cys-x-x-Cys-x(n)-Cys-x-x-Cys). This domain folds into a short three-stranded antiparallel beta-sheet and a number of loops; Localized in the cytoplasm; Family membership.

cAMP-binding dependent transcriptionnal regulator; This protein complexes with cAMP via an N-terminal cyclic nucleotide-binding domain and binds to specific DNA sites, via a C-terminal crp-type HTH domain, near the promoter to regulate the transcription of several catabolite-sensitive operons. The protein induces a severe bend in the DNA; Family membership.

Conserved hypothetical periplasmic protein; Contains a signal peptide cleaved between the residues 20 and 21; Localized in the periplasmic space; Conserved hypothetical protein.

The sensor histidine kinase belongs to two-component signal transduction systems. It catalyzes the ATP dependent autophosphorylation of a conserved histidine in its phosphoacceptor domain and the signal dependent phosphorylation of a conserved aspartic acid present in the response regulator receiver domain; Contains two transmembrane segments and an N-terminal PAS/PAC domain involved in many signalling proteins where they are used as a signal sensor domain; Localized in the cytoplasmic membrane; Family membership.