[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16. STRAIN=ATCC 14405 / 218 / ZoBell; PubMed=7508388 [NCBI, ExPASy, EBI, Israel, Japan] Zumft W.G., Braun C., Cuypers H.; "Nitric oxide reductase from Pseudomonas stutzeri. Primary structure and gene organization of a novel bacterial cytochrome bc complex."; Eur. J. Biochem. 219:481-490(1994).
[2]	EPR SPECTROSCOPY. STRAIN=ATCC 14405 / 218 / ZoBell; PubMed=2542222 [NCBI, ExPASy, EBI, Israel, Japan] Heiss B., Frunzke K., Zumft W.G.; "Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri."; J. Bacteriol. 171:3288-3297(1989).
[3]	EPR SPECTROSCOPY. STRAIN=ATCC 14405 / 218 / ZoBell; DOI=10.1021/bi972437y; PubMed=9521721 [NCBI, ExPASy, EBI, Israel, Japan] Cheesman M.R., Zumft W.G., Thomson A.J.; "The MCD and EPR of the heme centers of nitric oxide reductase from Pseudomonas stutzeri: evidence that the enzyme is structurally related to the heme-copper oxidases."; Biochemistry 37:3994-4000(1998).

Comments

FUNCTION: Component of the anaerobic respiratory chain that transforms nitrate to dinitrogen (denitrification). NorB is the catalytic subunit of the enzyme complex. Shows proton pump activity across the membrane in denitrifying bacterial cells. The mononitrogen reduction is probably coupled to electron transport phosphorylation.
CATALYTIC ACTIVITY: Nitrous oxide + acceptor + H₂O = 2 nitric oxide + reduced acceptor.
PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 3/4 .
SUBUNIT: Heterodimer of cytochromes b (large subunit) and c (small subunit).
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein (Potential).
INDUCTION: By nitric oxide (Probable).
SIMILARITY: Belongs to the heme-copper respiratory oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X53676; CAA82229.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S41117; S41117.

3D structure databases

ModBase

P98008.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-241; -.

Family and domain databases

InterPro

IPR000883; COX1.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.210.10; COX1; 1.

Pfam

PF00115; COX1; 1.
Pfam graphical view of domain structure.

PROSITE

PS50855; COX1; 1.
PS00077; COX1_CUB; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell membrane; Direct protein sequencing; Electron transport; Heme; Iron; Membrane; Metal-binding; Oxidoreductase; Respiratory chain; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 474`	`473`	`Nitric oxide reductase subunit B.`	`PRO_0000183473`
`TRANSMEM`	`19 39`	`21`	`Potential.`
`TRANSMEM`	`61 81`	`21`	`Potential.`
`TRANSMEM`	`95 115`	`21`	`Potential.`
`TRANSMEM`	`145 165`	`21`	`Potential.`
`TRANSMEM`	`169 189`	`21`	`Potential.`
`TRANSMEM`	`207 227`	`21`	`Potential.`
`TRANSMEM`	`243 263`	`21`	`Potential.`
`TRANSMEM`	`270 290`	`21`	`Potential.`
`TRANSMEM`	`308 328`	`21`	`Potential.`
`TRANSMEM`	`348 368`	`21`	`Potential.`
`TRANSMEM`	`390 410`	`21`	`Potential.`
`TRANSMEM`	`433 453`	`21`	`Potential.`
`METAL`	`60 60`		`Iron (low-spin heme axial ligand) (Probable).`
`METAL`	`207 207`		`Iron B (Probable).`
`METAL`	`258 258`		`Iron B (Probable).`
`METAL`	`259 259`		`Iron B (Probable).`
`METAL`	`347 347`		`Iron (high-spin heme axial ligand) (Probable).`
`METAL`	`349 349`		`Iron (low-spin heme axial ligand) (Probable).`

Sequence information

Length: 474 AA [This is the length of the unprocessed precursor]

Molecular weight: 53137 Da [This is the MW of the unprocessed precursor]

CRC64: 6455FC53DCB27896 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSFNPHLKF QSQAVAKPYF VFALILFVGQ VLFGLIMGLQ YVVGDFLFPL LPFNVARMVH 

        70         80         90        100        110        120 
TNLLIVWLLF GFMGAAYYLI PEESDCELHS PKLAIILFWV FAAAGVLTIL GYLFVPYAAL 

       130        140        150        160        170        180 
AEMTRNDLLP TMGREFLEQP TITKIGIVVV ALGFLYNIGM TMLKGRKTVV STVMMTGLIG 

       190        200        210        220        230        240 
LAVFFLFAFY NPENLSRDKF YWWFVVHLWV EGVWELIMGA MLAFVLIKVT GVDREVIEKW 

       250        260        270        280        290        300 
LYVIIAMALI TGIIGTGHHF FWIGAPTVWL WVGSIFSALE PLPFFAMVLF ALNMVNRRRR 

       310        320        330        340        350        360 
EHPNKAASLW AIGTTVTAFL GAGVWGFMHT LAPVNYYTHG SQLTAAHGHL AFYGAYAMIV 

       370        380        390        400        410        420 
MTMISYAMPR LRGLGEAPDA RAQRIEVWGF WLMTISMIAI TLFLTAAGVV QIWLQRIPAD 

       430        440        450        460        470 
GAAMSFMNTA DQLAIFFWLR FIAGVFFLIG LVCYLYSFRQ RGRVPVVVAA PAAA

P98008 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools