[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=NL1B8944; PubMed=8243476 [NCBI, ExPASy, EBI, Israel, Japan] Hoeren F.U., Berks B.C., Ferguson S.J., McCarthy J.E.G.; "Sequence and expression of the gene encoding the respiratory nitrous-oxide reductase from Paracoccus denitrificans. New and conserved structural and regulatory motifs."; Eur. J. Biochem. 218:49-57(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Pd 1222; DOI=10.1128/JB.182.18.5211-5217.2000; PubMed=10960107 [NCBI, ExPASy, EBI, Israel, Japan] Saunders N.F.W., Hornberg J.J., Reijnders W.N.M., Westerhoff H.V., de Vries S., van Spanning R.J.M.; "The NosX and NirX proteins of Paracoccus denitrificans are functional homologues: their role in maturation of nitrous oxide reductase."; J. Bacteriol. 182:5211-5217(2000).
[3]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 60-650, AND PROTEIN SEQUENCE OF 58-63. STRAIN=1657; DOI=10.1042/BJ20020782; PubMed=12356332 [NCBI, ExPASy, EBI, Israel, Japan] Haltia T., Brown K., Tegoni M., Cambillau C., Saraste M., Mattila K., Djinovic-Carugo K.; "Crystal structure of nitrous oxide reductase from Paracoccus denitrificans at 1.6 A resolution."; Biochem. J. 369:77-88(2003).

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.
SUBCELLULAR LOCATION: Periplasm.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
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

X74792; CAA52798.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ010260; CAB53351.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S39409; S39409.

3D structure databases

PDB

1FWX; X-ray; 1.60 A; A/B/C/D=58-652.

[ExPASy / RCSB / EBI]

PDBsum

1FWX; -.

ModBase

Q51705.

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:0031404;	Molecular function: chloride ion binding (inferred from electronic annotation from UniProtKB-KW).
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).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00716; -; 1.
PBIL [Tree]

InterPro

IPR001505; Copper_CuA.
IPR002429; COX2_C.
IPR008972; Cupredoxin.
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.

PROSITE

PS00078; COX2; FALSE_NEG.
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

3D-structure; Calcium; Chloride; Copper; Direct protein sequencing; Metal-binding; Oxidoreductase; Periplasm; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 57`	`57`	`Tat-type signal.`
`CHAIN`	`58 652`	`595`	`Nitrous-oxide reductase.`	`PRO_0000019827`
`REGION`	`554 652`	`99`	`COX2-like.`
`METAL`	`145 145`		`Copper Z2.`
`METAL`	`146 146`		`Copper Z3.`
`METAL`	`194 194`		`Copper Z2.`
`METAL`	`271 271`		`Calcium 2; via carbonyl oxygen.`
`METAL`	`274 274`		`Calcium 2.`
`METAL`	`282 282`		`Calcium 2; via carbonyl oxygen.`
`METAL`	`288 288`		`Calcium 2.`
`METAL`	`335 335`		`Calcium 2.`
`METAL`	`337 337`		`Copper Z1.`
`METAL`	`392 392`		`Copper Z1.`
`METAL`	`443 443`		`Copper Z3.`
`METAL`	`464 464`		`Calcium 1; via carbonyl oxygen.`
`METAL`	`479 479`		`Calcium 1.`
`METAL`	`504 504`		`Copper Z4.`
`METAL`	`595 595`		`Copper A1.`
`METAL`	`630 630`		`Copper A1.`
`METAL`	`630 630`		`Copper A2.`
`METAL`	`632 632`		`Copper A2; via carbonyl oxygen.`
`METAL`	`634 634`		`Copper A1.`
`METAL`	`634 634`		`Copper A2.`
`METAL`	`638 638`		`Copper A2.`
`METAL`	`641 641`		`Copper A1.`
`BINDING`	`197 197`		`Chloride.`
`BINDING`	`339 339`		`Chloride; via amide nitrogen.`
`BINDING`	`340 340`		`Chloride.`
`BINDING`	`392 392`		`Chloride.`
`STRAND`	`71 76`	`6`
`STRAND`	`84 89`	`6`
`STRAND`	`94 98`	`5`
`STRAND`	`100 102`	`3`
`TURN`	`105 107`	`3`
`TURN`	`109 111`	`3`
`HELIX`	`113 120`	`8`
`HELIX`	`126 133`	`8`
`STRAND`	`147 152`	`6`
`STRAND`	`155 165`	`11`
`TURN`	`166 169`	`4`
`STRAND`	`170 175`	`6`
`TURN`	`176 179`	`4`
`STRAND`	`180 186`	`7`
`STRAND`	`192 198`	`7`
`STRAND`	`201 203`	`3`
`STRAND`	`205 211`	`7`
`STRAND`	`220 223`	`4`
`STRAND`	`231 238`	`8`
`TURN`	`239 242`	`4`
`STRAND`	`243 252`	`10`
`STRAND`	`257 259`	`3`
`STRAND`	`261 271`	`11`
`HELIX`	`279 282`	`4`
`STRAND`	`286 294`	`9`
`HELIX`	`295 304`	`10`
`STRAND`	`307 310`	`4`
`STRAND`	`313 317`	`5`
`STRAND`	`326 335`	`10`
`STRAND`	`339 341`	`3`
`STRAND`	`345 351`	`7`
`STRAND`	`355 362`	`8`
`HELIX`	`363 365`	`3`
`HELIX`	`366 371`	`6`
`HELIX`	`377 379`	`3`
`STRAND`	`380 382`	`3`
`STRAND`	`390 395`	`6`
`STRAND`	`399 405`	`7`
`TURN`	`406 409`	`4`
`STRAND`	`410 415`	`6`
`HELIX`	`416 424`	`9`
`STRAND`	`431 436`	`6`
`STRAND`	`441 446`	`6`
`TURN`	`447 450`	`4`
`STRAND`	`456 464`	`9`
`STRAND`	`479 485`	`7`
`STRAND`	`487 490`	`4`
`STRAND`	`492 501`	`10`
`STRAND`	`506 509`	`4`
`TURN`	`511 516`	`6`
`HELIX`	`526 528`	`3`
`HELIX`	`529 537`	`9`
`STRAND`	`549 552`	`4`
`STRAND`	`555 563`	`9`
`STRAND`	`566 568`	`3`
`STRAND`	`570 575`	`6`
`STRAND`	`579 586`	`8`
`STRAND`	`595 599`	`5`
`TURN`	`600 603`	`4`
`STRAND`	`604 608`	`5`
`STRAND`	`613 619`	`7`
`STRAND`	`624 629`	`6`
`STRAND`	`642 648`	`7`

Sequence information

Length: 652 AA [This is the length of the unprocessed precursor]

Molecular weight: 71414 Da [This is the MW of the unprocessed precursor]

CRC64: 40492A4FDE7EDEA8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MESKQEKGLS RRALLGATAG GAAVAGAFGG RLALGPAALG LGTAGVATVA GSGAALAASG 

        70         80         90        100        110        120 
DGSVAPGQLD DYYGFWSSGQ SGEMRILGIP SMRELMRVPV FNRCSATGWG QTNESVRIHE 

       130        140        150        160        170        180 
RTMSERTKKF LAANGKRIHD NGDLHHVHMS FTEGKYDGRF LFMNDKANTR VARVRCDVMK 

       190        200        210        220        230        240 
CDAILEIPNA KGIHGLRPQK WPRSNYVFCN GEDETPLVND GTNMEDVANY VNVFTAVDAD 

       250        260        270        280        290        300 
KWEVAWQVLV SGNLDNCDAD YEGKWAFSTS YNSEKGMTLP EMTAAEMDHI VVFNIAEIEK 

       310        320        330        340        350        360 
AIAAGDYQEL NGVKVVDGRK EASSLFTRYI PIANNPHGCN MAPDKKHLCV AGKLSPTATV 

       370        380        390        400        410        420 
LDVTRFDAVF YENADPRSAV VAEPELGLGP LHTAFDGRGN AYTSLFLDSQ VVKWNIEDAI 

       430        440        450        460        470        480 
RAYAGEKVDP IKDKLDVHYQ PGHLKTVMGE TLDATNDWLV CLSKFSKDRF LNVGPLKPEN 

       490        500        510        520        530        540 
DQLIDISGDK MVLVHDGPTF AEPHDAIAVH PSILSDIKSV WDRNDPMWAE TRAQAEADGV 

       550        560        570        580        590        600 
DIDNWTEEVI RDGNKVRVYM SSVAPSFSIE SFTVKEGDEV TVIVTNLDEI DDLTHGFTMG 

       610        620        630        640        650 
NYGVAMEIGP QMTSSVTFVA ANPGVYWYYC QWFCHALHME MRGRMLVEPK EA

Q51705 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