[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=ATCC 14405 / 218 / ZoBell; PubMed=3049543 [NCBI, ExPASy, EBI, Israel, Japan] Viebrock A., Zumft W.G.; "Molecular cloning, heterologous expression, and primary structure of the structural gene for the copper enzyme nitrous oxide reductase from denitrifying Pseudomonas stutzeri."; J. Bacteriol. 170:4658-4668(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 14405 / 218 / ZoBell; PubMed=2170125 [NCBI, ExPASy, EBI, Israel, Japan] Zumft W.G., Viebrock-Sambale A., Braun C.; "Nitrous oxide reductase from denitrifying Pseudomonas stutzeri. Genes for copper-processing and properties of the deduced products, including a new member of the family of ATP/GTP-binding proteins."; Eur. J. Biochem. 192:591-599(1990).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26. STRAIN=ATCC 14405 / 218 / ZoBell; PubMed=1644760 [NCBI, ExPASy, EBI, Israel, Japan] Cuypers H., Viebrock-Sambale A., Zumft W.G.; "NosR, a membrane-bound regulatory component necessary for expression of nitrous oxide reductase in denitrifying Pseudomonas stutzeri."; J. Bacteriol. 174:5332-5339(1992).
[4]	CHARACTERIZATION. PubMed=2542963 [NCBI, ExPASy, EBI, Israel, Japan] Scott R.A., Zumft W.G., Coyle C.L., Dooley D.M.; "Pseudomonas stutzeri N2O reductase contains CuA-type sites."; Proc. Natl. Acad. Sci. U.S.A. 86:4082-4086(1989).
[5]	CHARACTERIZATION. DOI=10.1021/ja994322i; PubMed=11456570 [NCBI, ExPASy, EBI, Israel, Japan] Alvarez M.L., Ai J., Zumft W.G., Sanders-Loehr J., Dooley D.M.; "Characterization of the copper-sulfur chromophores in nitrous oxide reductase by resonance Raman spectroscopy: evidence for sulfur coordination in the catalytic cluster."; J. Am. Chem. Soc. 123:576-587(2001).

Comments

FUNCTION: Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide.
CATALYTIC ACTIVITY: N₂ + H₂O + acceptor = N₂O + reduced acceptor.
COFACTOR: Binds 2 calcium ions per subunit.
COFACTOR: Binds 6 copper ions Each subunit contains 2 copper centers; Cu(A) (binuclear) and Cu(Z) (tetranuclear). Cu(Z) is thought to be the site of nitrous oxide reduction.
PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 4/4 .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Periplasm.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
PTM: The N-terminus is blocked.
SIMILARITY: Belongs to the nosZ family.
SIMILARITY: In the C-terminal section; belongs to the cytochrome c oxidase subunit 2 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; CAA37714.2; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A31845; A31845.

3D structure databases

HSSP

Q51705; 1FWX. [HSSP ENTRY / PDB]

ModBase

P19573.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-243; -.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from HAMAP).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from HAMAP).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from HAMAP).
GO:0050304;	Molecular function: nitrous-oxide reductase activity (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00716; -; 1.
PBIL [Tree]

InterPro

IPR001505; Copper_CuA.
IPR002429; COX2_C.
IPR008972; Cupredoxin.
IPR006311; Tat.
IPR015943; WD40/YVTN_repeat-like.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.420; Cupredoxin; 1.
G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.

Pfam

PF00116; COX2; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01409; TAT_signal_seq; 1.

PROSITE

PS00078; COX2; 1.
PS50857; COX2_CUA; 1.
PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

Calcium; Copper; Direct protein sequencing; Metal-binding; Oxidoreductase; Periplasm; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 52`	`52`	`Tat-type signal (Potential).`
`CHAIN`	`53 638`	`586`	`Nitrous-oxide reductase.`	`PRO_0000019831`
`REGION`	`542 638`	`97`	`COX2-like.`
`METAL`	`129 129`		`Copper Z2 (By similarity).`
`METAL`	`130 130`		`Copper Z3 (By similarity).`
`METAL`	`178 178`		`Copper Z2 (By similarity).`
`METAL`	`256 256`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`259 259`		`Calcium 2 (By similarity).`
`METAL`	`267 267`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`273 273`		`Calcium 2 (By similarity).`
`METAL`	`324 324`		`Calcium 2 (By similarity).`
`METAL`	`326 326`		`Copper Z1 (By similarity).`
`METAL`	`382 382`		`Copper Z1 (By similarity).`
`METAL`	`433 433`		`Copper Z3 (By similarity).`
`METAL`	`454 454`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`469 469`		`Calcium 1 (By similarity).`
`METAL`	`494 494`		`Copper Z4 (By similarity).`
`METAL`	`583 583`		`Copper A1 (By similarity).`
`METAL`	`618 618`		`Copper A1 (By similarity).`
`METAL`	`618 618`		`Copper A2 (By similarity).`
`METAL`	`620 620`		`Copper A2; via carbonyl oxygen (By similarity).`
`METAL`	`622 622`		`Copper A1 (By similarity).`
`METAL`	`622 622`		`Copper A2 (By similarity).`
`METAL`	`626 626`		`Copper A2 (By similarity).`
`METAL`	`629 629`		`Copper A1 (By similarity).`
`CONFLICT`	`14 14`		`E -> EE (in Ref. 3).`

Sequence information

Length: 638 AA [This is the length of the unprocessed precursor]

Molecular weight: 70822 Da [This is the MW of the unprocessed precursor]

CRC64: C2CA79CCB556061B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDKDSKNTP QVPEKLGLSR RGFLGASAVT GAAVAATALG GAVMTRESWA QAVKESKQKI 

        70         80         90        100        110        120 
HVGPGELDDY YGFWSGGHQG EVRVLGVPSM RELMRIPVFN VDSATGWGLT NESRHIMGDS 

       130        140        150        160        170        180 
AKFLNGDCHH PHISMTDGKY DGKYLFINDK ANSRVARIRL DIMKCDKMIT VPNVQAIHGL 

       190        200        210        220        230        240 
RLQKVPHTKY VFANAEFIIP HPNDGKVFDL QDENSYTMYN AIDAETMEMA FQVIVDGNLD 

       250        260        270        280        290        300 
NTDADYTGRF AAATCYNSEK AFDLGGMMRN ERDWVVVFDI HAVEAAVKAG DFITLGDSKT 

       310        320        330        340        350        360 
PVLDGRKKDG KDSKFTRYVP VPKNPHGCNT SSDGKYFIAA GKLSPTCSMI AIDKLPDLFA 

       370        380        390        400        410        420 
GKLADPRDVI VGEPELGLGP LHTTFDGRGN AYTTLFIDSQ VVKWNMEEAV RAYKGEKVNY 

       430        440        450        460        470        480 
IKQKLDVHYQ PGHLHASLCE TNEADGKWLV ALSKFSKDRF LPVGPLHPEN DQLIDISGDE 

       490        500        510        520        530        540 
MKLVHDGPTF AEPHDCIMAR RDQIKTKKIW DRNDPFFAPT VEMAKKDGIN LDTDNKVIRD 

       550        560        570        580        590        600 
GNKVRVYMTS MAPAFGVQEF TVKQGDEVTV TITNIDQIED VSHGFVVVNH GVSMEISPQQ 

       610        620        630 
TSSITFVADK PGLHWYYCSW FCHALHMEMV GRMMVEPA

P19573 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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