PMID:2200672

Citation	Peakman, T, Crouzet, J, Mayaux, JF, Busby, S, Mohan, S, Harborne, N, Wootton, J, Nicolson, R and Cole, J (1990) Nucleotide sequence, organisation and structural analysis of the products of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome. Eur. J. Biochem. 191:315-23
Abstract	The DNA sequence and derived amino-acid sequence of a 5618-base region in the 74-min area of the Escherichia coli chromosome has been determined in order to locate the structural gene, nirB, for the NADH-dependent nitrite reductase and a gene, cysG, required for the synthesis of the sirohaem prosthetic group. Three additional open reading frames, nirD, nirE and nirC, were found between nirB and cysG. Potential binding sites on the NirB protein for NADH and FAD, as well as conserved central core and interface domains, were deduced by comparing the derived amino-acid sequence with those of database proteins. A directly repeated sequence, which includes the motif -Cys-Xaa-Xaa-Cys-, is suggested as the binding site for either one [4Fe-4S] or two [2Fe-2S] clusters. The nirD gene potentially encodes a soluble, cytoplasmic protein of unknown function. No significant similarities were found between the derived amino-acid sequence of NirD and either NirB or any other protein in the database. If the nirE open reading frame is translated, it would encode a 33-amino-acid peptide of unknown function which includes 8 phenylalanyl residues. The product of the nirC gene is a highly hydrophobic protein with regions of amino-acid sequence similar to cytochrome oxidase polypeptide 1.
Links	PubMed
Keywords	Amino Acid Sequence; Bacterial Proteins/genetics; Base Sequence; Chromosomes, Bacterial/analysis; Escherichia coli/genetics; Escherichia coli/ultrastructure; Gene Expression; Genes, Bacterial; Molecular Sequence Data; Nitrate Reductase; Nitrate Reductases/genetics; Promoter Regions, Genetic; Repetitive Sequences, Nucleic Acid
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
ECOLI:NIRC	part_of	GO:0016021: integral component of membrane	ECO:0000255: match to sequence model evidence used in manual assertion		C		Seeded From UniProt	Missing: with/from
ECOLI:NIRC		GO:0016021: integral to membrane	ECO:0000255:	PMID:3945310	C		Figure 5: shows the hydrophobicity of a few nitrate reductase proteins. NirB, NirD, and CysG had relatively equal values of hydrophobic and hydrophilic residues, which indicated that it more closely resembled a protein found inside the cell such as a cytoplasmic protein. On the other hand, NirC had an abundance of hydrophobic residues, which indicates it may be part of the membrane. NirC has also been found to be comparable to a subunit that is part of the cytochrome oxidase polypeptide 1, which is a membrane bound chain of amino acids. Eisenberg and McLachlan created a model to calculate hydrophobicity and amphiphilcity that was used to determine the hydrophobicity of all of these proteins.	complete CACAO 2291

References

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