NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=JJ1c10;
PubMed=8626275 [NCBI, ExPASy, EBI, Israel, Japan]
Holloway P., McCormick W., Watson R.J., Chan Y.K.;
"Identification and analysis of the dissimilatory nitrous oxide reduction genes, nosRZDFY, of Rhizobium meliloti.";
J. Bacteriol. 178:1505-1514(1996).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1021;
DOI=10.1073/pnas.161294798; PubMed=11481432 [NCBI, ExPASy, EBI, Israel, Japan]
Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C., Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A., Long S.R.;
"Nucleotide sequence and predicted functions of the entire Sinorhizobium meliloti pSymA megaplasmid.";
Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(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 (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

U47133; AAC44023.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE006469; AAK65301.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C95342; C95342.

RefSeq

NP_435889.1; -.

3D structure databases

HSSP

Q51705; 1FWX. [HSSP ENTRY / PDB]

ModBase

Q59746.

Enzyme and pathway databases

BioCyc

SMEL266834:SMA1182-MON; -.

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.
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).

BLOCKS

Q59746.

Genome annotation databases

1235679; -.

AE006469_GR; RA0643.

sme:SMa1182; -.

fig|266834.1.peg.643; -.

Phylogenomic databases

HOGENOM

Q59746; -.

Genome annotation databases

CMR

Q59746; RA0643.

Other

ProtoNet

Q59746.

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`	`47 639`	`593`	`Nitrous-oxide reductase.`	`PRO_0000019833`
`REGION`	`541 639`	`99`	`COX2-like.`
`METAL`	`136 136`		`Copper Z2 (By similarity).`
`METAL`	`137 137`		`Copper Z3 (By similarity).`
`METAL`	`185 185`		`Copper Z2 (By similarity).`
`METAL`	`262 262`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`265 265`		`Calcium 2 (By similarity).`
`METAL`	`273 273`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`279 279`		`Calcium 2 (By similarity).`
`METAL`	`324 324`		`Calcium 2 (By similarity).`
`METAL`	`326 326`		`Copper Z1 (By similarity).`
`METAL`	`381 381`		`Copper Z1 (By similarity).`
`METAL`	`432 432`		`Copper Z3 (By similarity).`
`METAL`	`453 453`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`468 468`		`Calcium 1 (By similarity).`
`METAL`	`493 493`		`Copper Z4 (By similarity).`
`METAL`	`582 582`		`Copper A1 (By similarity).`
`METAL`	`617 617`		`Copper A1 (By similarity).`
`METAL`	`617 617`		`Copper A2 (By similarity).`
`METAL`	`619 619`		`Copper A2; via carbonyl oxygen (By similarity).`
`METAL`	`621 621`		`Copper A1 (By similarity).`
`METAL`	`621 621`		`Copper A2 (By similarity).`
`METAL`	`625 625`		`Copper A2 (By similarity).`
`METAL`	`628 628`		`Copper A1 (By similarity).`

Sequence information

Length: 639 AA [This is the length of the unprocessed precursor]

Molecular weight: 70760 Da [This is the MW of the unprocessed precursor]

CRC64: EBCF5EDFAFF70B96 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSNEETKMRL NRRQMLGTTA FMAAAGAVGA GGALTLSGGT ATPARAQETS GSSYEVKPGE 

        70         80         90        100        110        120 
LDEYYVFFSS GQSGEIRIVG APSMREMMRI PVFNRCSATG WGQTNESRKV MTEGLLPETV 

       130        140        150        160        170        180 
EFLKDQGGLY LNGDLHHPHP SFTDGTYDGR YLYANDKSNS RVCRIRLDVM KCDKIIQLPN 

       190        200        210        220        230        240 
QHTVHGLRVQ KYPKTGYVFC NGEDAVPVPN DGKTMGDKNS YQAIFTAVDG ETMEVAWQVM 

       250        260        270        280        290        300 
VDGNLDNVDA DYQGKYCFAT CYNSEEGFTL ADMMASEQDW VVIFNLKRIE EAVAKGDYKE 

       310        320        330        340        350        360 
IGGVPVLDGR KGSPYTRYVP VPNSPHGINT APDGIHVVAN GKLSPTVTVF DVRKFDDLFD 

       370        380        390        400        410        420 
DKIQARDTVV AEPELGLGPL HTAYDGKGNA YTTLFIDSQV CKWNIEDAKR AYAGEKVDPI 

       430        440        450        460        470        480 
RHKLDVHYQP GHNHTSMGQT KEADGKWLIS LNKFSKDRYL NVGPLKPEND QLIDISGDEM 

       490        500        510        520        530        540 
VLVHDNPTFA EPHDATIVHA SKINPVHVWN RDDPFFADAV AQAKADNIDL MVDSEVIRDG 

       550        560        570        580        590        600 
NKVRVYMTSA APAFGLDDFT VKQGDEVTVY VTNIDEVEDL THGFCIVNYG INMEVAPQAT 

       610        620        630 
ASVTFKASRP GVYWYYCTWF CHAMHMEMKG RMLVEAQGA

Q59746 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