NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1324835 [NCBI, ExPASy, EBI, Israel, Japan]
Zumft W.G., Dreusch A., Loechelt S., Cuypers H., Friedrich B., Schneider B.;
"Derived amino acid sequences of the nosZ gene (respiratory N2O reductase) from Alcaligenes eutrophus, Pseudomonas aeruginosa and Pseudomonas stutzeri reveal potential copper-binding residues. Implications for the CuA site of N2O reductase and cytochrome-c oxidase.";
Eur. J. Biochem. 208:31-40(1992).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0022-2836(03)00894-5; PubMed=12948488 [NCBI, ExPASy, EBI, Israel, Japan]
Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
"Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
J. Mol. Biol. 332:369-383(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 (By similarity).
COFACTOR: Binds 6 copper ions per subunit. 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 (By similarity).
PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 4/4 .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Periplasm (By similarity).
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not 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

X65278; CAA46383.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY305378; AAP86001.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S24382; S24382.

RefSeq

NP_942887.1; -.

3D structure databases

HSSP

Q51705; 1FWX. [HSSP ENTRY / PDB]

ModBase

Q59105.

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

BLOCKS

Q59105.

Genome annotation databases

GeneID

2656479; -.

GenomeReviews

AY305378_GR; PHG252.

Phylogenomic databases

HOGENOM

Q59105; -.

Genome annotation databases

CMR

Q59105; PHG252.

Other

ProtoNet

Q59105.

UniRef

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

Keywords

Calcium; Complete proteome; Copper; Metal-binding; Oxidoreductase; Periplasm; Plasmid; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 46`	`46`	`Tat-type signal (Potential).`
`CHAIN`	`47 643`	`597`	`Nitrous-oxide reductase.`	`PRO_0000019823`
`REGION`	`548 643`	`96`	`COX2-like.`
`METAL`	`138 138`		`Copper Z2 (By similarity).`
`METAL`	`139 139`		`Copper Z3 (By similarity).`
`METAL`	`187 187`		`Copper Z2 (By similarity).`
`METAL`	`269 269`		`Calcium 2 (via carbonyl oxygen) (By similarity).`
`METAL`	`272 272`		`Calcium 2 (By similarity).`
`METAL`	`280 280`		`Calcium 2 (via carbonyl oxygen) (By similarity).`
`METAL`	`286 286`		`Calcium 2 (By similarity).`
`METAL`	`339 339`		`Calcium 2 (By similarity).`
`METAL`	`341 341`		`Copper Z1 (By similarity).`
`METAL`	`397 397`		`Copper Z1 (By similarity).`
`METAL`	`449 449`		`Copper Z3 (By similarity).`
`METAL`	`470 470`		`Calcium 1 (via carbonyl oxygen) (By similarity).`
`METAL`	`485 485`		`Calcium 1 (By similarity).`
`METAL`	`510 510`		`Copper Z4 (By similarity).`
`METAL`	`589 589`		`Copper A1 (By similarity).`
`METAL`	`624 624`		`Copper A1 (By similarity).`
`METAL`	`624 624`		`Copper A2 (By similarity).`
`METAL`	`626 626`		`Copper A2 (via carbonyl oxygen) (By similarity).`
`METAL`	`628 628`		`Copper A1 (By similarity).`
`METAL`	`628 628`		`Copper A2 (By similarity).`
`METAL`	`632 632`		`Copper A2 (By similarity).`
`METAL`	`635 635`		`Copper A1 (By similarity).`

Sequence information

Length: 643 AA [This is the length of the unprocessed precursor]

Molecular weight: 70085 Da [This is the MW of the unprocessed precursor]

CRC64: 42845B13497E4984 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKEKASIGN GPGGIGRRQF LGTAALAGLA GVVACTDKGA APAAAAVGAP ASGAHGAAHG 

        70         80         90        100        110        120 
AGASVHLKPG ELDTYYGLWS GGHTGDMRVL GLPSGREILR IPCFVPDALV GWGITNESKK 

       130        140        150        160        170        180 
VMGARPDGTL RYTVADTHHT HASYKDGNYD GRYAWVNDKI NSRIARIRLD YFICDKITEL 

       190        200        210        220        230        240 
PNVQGFHGIF PDKRDPVDTK INYTTRVFCG GEFGIPLPSA PTEDAGKYRS LFTCVDAETM 

       250        260        270        280        290        300 
AVRWQVLIDG NCDLVATSYD GKLAATNQYN TENGAHFEDM MSAERDACVF FNIARIEAAV 

       310        320        330        340        350        360 
QAGKFKTYGD SKVPVVDGTQ AANKDPKTAL TAYVSVPKNP HGVNASPDQK YFICAGKLSP 

       370        380        390        400        410        420 
TATVIELSRV LGWFDGKQEK LDDAIVAEVE LGLGPLHTAF DGRGNAYTTL FLDSQLVKWN 

       430        440        450        460        470        480 
LDAAIKFHKG DKNAKYVVDR LDLQYQPGHV NASQSETVAA DGKYLAVGCK FSKDRFLPVG 

       490        500        510        520        530        540 
PLHPENEQLI DISGQKMVLM ADHPVRGEPH DFIIFKRELV RPKQVYALDD FPLAIKDPKE 

       550        560        570        580        590        600 
SGVFRNGRKV TVKITSQAPA FSLREFKLKK GDEVTLILTN LDKIEDLTHG FAIPKYNVNF 

       610        620        630        640 
IVNPQETASV TFVADKPGVF WCYCTHFCHA LHLEMRTRMI VEA

Q59105 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