[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 21921 / IAM 1013; DOI=10.1006/bbrc.1996.0249; PubMed=8605003 [NCBI, ExPASy, EBI, Israel, Japan] Chen J.-Y., Chang W.-C., Chang T., Chang W.-C., Liu M.-Y., Payne W.J., le Gall J.; "Cloning, characterization, and expression of the nitric oxide-generating nitrite reductase and of the blue copper protein genes of Achromobacter cycloclastes."; Biochem. Biophys. Res. Commun. 219:423-428(1996).
[2]	PROTEIN SEQUENCE OF 39-378. STRAIN=ATCC 21921 / IAM 1013; DOI=10.1021/bi00243a020; PubMed=1830217 [NCBI, ExPASy, EBI, Israel, Japan] Fenderson F.F., Kumar S., Adman E.T., Liu M.-Y., Payne W.J., le Gall J.; "Amino acid sequence of nitrite reductase: a copper protein from Achromobacter cycloclastes."; Biochemistry 30:7180-7185(1991).
[3]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). PubMed=1862344 [NCBI, ExPASy, EBI, Israel, Japan] Godden J.W., Turley S., Teller D.C., Adman E.T., Liu M.-Y., Payne W.J., le Gall J.; "The 2.3-A X-ray structure of nitrite reductase from Achromobacter cycloclastes."; Science 253:438-442(1991).
[4]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). DOI=10.1074/jbc.270.46.27458; PubMed=7499203 [NCBI, ExPASy, EBI, Israel, Japan] Adman E.T., Godden J.W., Turley S.; "The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2-bound and with type II copper depleted."; J. Biol. Chem. 270:27458-27474(1995).

Comments

CATALYTIC ACTIVITY: Nitric oxide + H₂O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H⁺.
COFACTOR: Binds 1 Cu(+) ion.
COFACTOR: Binds 1 Cu(2+) ion.
COFACTOR: FAD.
PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 2/4 .
SUBUNIT: Homotrimer.
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.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
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

Z48635; CAA88564.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC4648; JC4648.

3D structure databases

PDB

1KCB; X-ray; 1.65 A; A=39-378.	[ExPASy / RCSB / EBI]
1NIA; X-ray; 2.50 A; A/B/C=39-378.	[ExPASy / RCSB / EBI]
1NIB; X-ray; 2.70 A; A/B/C=39-378.	[ExPASy / RCSB / EBI]
1NIC; X-ray; 1.90 A; A=39-378.	[ExPASy / RCSB / EBI]
1NID; X-ray; 2.20 A; A=39-378.	[ExPASy / RCSB / EBI]
1NIE; X-ray; 1.90 A; A=39-378.	[ExPASy / RCSB / EBI]
1NIF; X-ray; 1.70 A; A=39-378.	[ExPASy / RCSB / EBI]
1RZP; X-ray; 1.90 A; A/B/C=39-373.	[ExPASy / RCSB / EBI]
1RZQ; X-ray; 2.20 A; A/B/C=39-373.	[ExPASy / RCSB / EBI]
2AVF; X-ray; 2.60 A; A/B/C/D/E/F=39-367.	[ExPASy / RCSB / EBI]
2BW4; X-ray; 0.90 A; A=39-378.	[ExPASy / RCSB / EBI]
2BW5; X-ray; 1.12 A; A=39-378.	[ExPASy / RCSB / EBI]
2BWD; X-ray; 1.15 A; A=39-378.	[ExPASy / RCSB / EBI]
2BWI; X-ray; 1.10 A; A=39-378.	[ExPASy / RCSB / EBI]
2NRD; X-ray; 2.10 A; A=39-378.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1KCB; -.
1NIA; -.
1NIB; -.
1NIC; -.
1NID; -.
1NIE; -.
1NIF; -.
1RZP; -.
1RZQ; -.
2AVF; -.
2BW4; -.
2BW5; -.
2BWD; -.
2BWI; -.
2NRD; -.

ModBase

P25006.

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.
IPR006311; Tat.
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.
TIGR01409; TAT_signal_seq; 1.

PROSITE

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

Other

P25006; -.

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

Keywords

3D-structure; 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 38`	`38`	`Tat-type signal.`
`CHAIN`	`39 378`	`340`	`Copper-containing nitrite reductase.`	`PRO_0000002986`
`DOMAIN`	`39 213`	`175`	`Plastocyanin-like 1.`
`DOMAIN`	`214 378`	`165`	`Plastocyanin-like 2.`
`METAL`	`133 133`		`Copper 1; type 1.`
`METAL`	`138 138`		`Copper 2; type 2.`
`METAL`	`173 173`		`Copper 2; type 2.`
`METAL`	`174 174`		`Copper 1; type 1.`
`METAL`	`183 183`		`Copper 1; type 1.`
`METAL`	`188 188`		`Copper 1; type 1.`
`METAL`	`344 344`		`Copper 2; type 2.`
`HELIX`	`47 49`	`3`
`STRAND`	`52 54`	`3`
`STRAND`	`71 73`	`3`
`STRAND`	`76 89`	`14`
`STRAND`	`96 102`	`7`
`STRAND`	`105 107`	`3`
`STRAND`	`110 114`	`5`
`STRAND`	`118 125`	`8`
`HELIX`	`143 149`	`7`
`STRAND`	`156 163`	`8`
`STRAND`	`168 173`	`6`
`HELIX`	`180 185`	`6`
`STRAND`	`189 195`	`7`
`STRAND`	`211 221`	`11`
`HELIX`	`237 249`	`13`
`STRAND`	`254 258`	`5`
`TURN`	`262 265`	`4`
`HELIX`	`267 269`	`3`
`STRAND`	`271 274`	`4`
`STRAND`	`278 288`	`11`
`STRAND`	`292 295`	`4`
`STRAND`	`299 303`	`5`
`STRAND`	`313 317`	`5`
`STRAND`	`325 332`	`8`
`STRAND`	`337 345`	`9`
`HELIX`	`346 350`	`5`
`STRAND`	`355 362`	`8`
`TURN`	`366 368`	`3`
`STRAND`	`369 376`	`8`

Sequence information

Length: 378 AA [This is the length of the unprocessed precursor]

Molecular weight: 40771 Da [This is the MW of the unprocessed precursor]

CRC64: A70B52B814090EA5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTEQLQMTRR TMLAGAALAG AVAPLLHTAQ AHAAGAAAAA GAAPVDISTL PRVKVDLVKP 

        70         80         90        100        110        120 
PFVHAHDQVA KTGPRVVEFT MTIEEKKLVI DREGTEIHAM TFNGSVPGPL MVVHENDYVE 

       130        140        150        160        170        180 
LRLINPDTNT LLHNIDFHAA TGALGGGALT QVNPGEETTL RFKATKPGVF VYHCAPEGMV 

       190        200        210        220        230        240 
PWHVTSGMNG AIMVLPRDGL KDEKGQPLTY DKIYYVGEQD FYVPKDEAGN YKKYETPGEA 

       250        260        270        280        290        300 
YEDAVKAMRT LTPTHIVFNG AVGALTGDHA LTAAVGERVL VVHSQANRDT RPHLIGGHGD 

       310        320        330        340        350        360 
YVWATGKFRN PPDLDQETWL IPGGTAGAAF YTFRQPGVYA YVNHNLIEAF ELGAAGHFKV 

       370 
TGEWNDDLMT SVVKPASM

P25006 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