NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 25-41.
STRAIN=ATCC 13985 / DSM 50082 / NRRL B-1576 / Stanier 38;
PubMed=8352648 [NCBI, ExPASy, EBI, Israel, Japan]
Glockner A.B., Juengst A., Zumft W.G.;
"Copper-containing nitrite reductase from Pseudomonas aureofaciens is functional in a mutationally cytochrome cd1-free background (NirS-) of Pseudomonas stutzeri.";
Arch. Microbiol. 160:18-26(1993).

Comments

CATALYTIC ACTIVITY: Nitric oxide + H₂O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H⁺.
COFACTOR: Binds 1 Cu(2+) ion. The Cu(2+) ion is held by residues from each of 2 monomers of the trimer. Nitrite is bound to the Cu(2+) ion site. Pseudoazurin is the physiological electron donor for the Cu-NIR in vitro.
COFACTOR: Binds 1 Cu(+) ion. The Cu(+) ion is bound within a single monomer.
COFACTOR: FAD.
PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 2/4 .
SUBUNIT: Homotrimer (By similarity).
SUBCELLULAR LOCATION: Periplasm.
DOMAIN: The type I copper site in NIR plays a crucial role for electron transfer from pseudoazurin to the type II copper site of NIR, which comprises the catalytic center of NIR for the reduction of nitrite.
SIMILARITY: Belongs to the multicopper oxidase family.
SIMILARITY: Contains 2 plastocyanin-like domains.

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

Z21945; CAA79939.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S32112; S32112.

3D structure databases

HSSP

O68601; 1OE2. [HSSP ENTRY / PDB]

SMR

Q06006; 27-358.

ModBase

Q06006.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
GO:0050421;	Molecular function: nitrite reductase (NO-forming) activity (inferred from electronic annotation from InterPro).
GO:0042128;	Biological process: nitrate assimilation (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001117; Cu-oxidase.
IPR011707; Cu-oxidase_3.
IPR001287; Cu_NO2-reductase_N.
IPR008972; Cupredoxin.
IPR012746; Nitrite_red_Cu.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.420; Cupredoxin; 2.

Pfam

PF00394; Cu-oxidase; 1.
PF07732; Cu-oxidase_3; 1.
Pfam graphical view of domain structure.

PRINTS

PR00695; CUNO2RDTASE.

ProDom

PD001235; Copper_blue_sub; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR02376; Cu_nitrite_red; 1.

ProtoNet

Q06006.

Other

UniRef

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

Keywords

Copper; Direct protein sequencing; FAD; Flavoprotein; Metal-binding; Nitrate assimilation; Oxidoreductase; Periplasm; Repeat; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`
`CHAIN`	`25 363`	`339`	`Copper-containing nitrite reductase.`	`PRO_0000002988`
`DOMAIN`	`25 193`	`169`	`Plastocyanin-like 1.`
`DOMAIN`	`194 363`	`170`	`Plastocyanin-like 2.`
`METAL`	`113 113`		`Copper 1; type 1 (By similarity).`
`METAL`	`118 118`		`Copper 2; type 2 (By similarity).`
`METAL`	`153 153`		`Copper 2; type 2 (By similarity).`
`METAL`	`154 154`		`Copper 1; type 1 (By similarity).`
`METAL`	`163 163`		`Copper 1; type 1 (By similarity).`
`METAL`	`168 168`		`Copper 1; type 1 (By similarity).`
`METAL`	`324 324`		`Copper 2; type 2 (By similarity).`

Sequence information

Length: 363 AA [This is the length of the unprocessed precursor]

Molecular weight: 39248 Da [This is the MW of the unprocessed precursor]

CRC64: 50DDB60CC4DC3E00 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVFRSVLGA CVLLGSCASS LALAGGAEGL QRVKVDLVAP PLVHPHEQVV SGPPKVVQFR 

        70         80         90        100        110        120 
MSIEEKKMVI DDQGTTLQAM TFNGSMPGPT LVVHEGDYIE LTLVNPATNS MPHNVDFHAA 

       130        140        150        160        170        180 
TGALGGAGLT QVVPGQEVVL RFKADRSGTF VYHCAPQGMV PWHVVSGMNG ALMVLPRDGL 

       190        200        210        220        230        240 
RDPQGKLLHY DRVYTIGESD LYIPKDKDGH YKDYPDLASS YQDTRAVMRT LTPSHVVFNG 

       250        260        270        280        290        300 
RVGALTGANA LTSKVGESVL FIHSQANRDS RPHLIGGHGD WVWTTGKFAN PPQRNMETWF 

       310        320        330        340        350        360 
IPGGSAVAAL YTFKQPGTYV YLSHNLIEAM ELGALAQIKV EGQWDDDLMT QVKAPGPIVE 


PKQ

Q06006 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