NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=G-179;
PubMed=8439151 [NCBI, ExPASy, EBI, Israel, Japan]
Ye R.W., Fries M.R., Bezborodnikov S.G., Averill B.A., Tiedje J.M.;
"Characterization of the structural gene encoding a copper-containing nitrite reductase and homology of this gene to DNA of other denitrifiers.";
Appl. Environ. Microbiol. 59:250-254(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 (By similarity).
COFACTOR: Binds 1 Cu(+) ion. The Cu(+) ion is bound within a single monomer (By similarity).
COFACTOR: FAD (By similarity).
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.
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 multicopper oxidase family.
SIMILARITY: Contains 2 plastocyanin-like domains.
CAUTION: It is uncertain whether Met-1 or Met-12 is the initiator.

Copyright

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Cross-references

Sequence databases

EMBL

M97294; AAC79132.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A48936; A48936.

3D structure databases

HSSP

P25006; 1NIF. [HSSP ENTRY / PDB]

SMR

Q01537; 47-378.

ModBase

Q01537.

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).

ProtoNet

Q01537.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 32`	`32`	`Tat-type signal (Potential).`
`CHAIN`	`33 379`	`347`	`Copper-containing nitrite reductase.`	`PRO_0000002989`
`DOMAIN`	`33 214`	`182`	`Plastocyanin-like 1.`
`DOMAIN`	`215 379`	`165`	`Plastocyanin-like 2.`
`METAL`	`134 134`		`Copper 1; type 1 (By similarity).`
`METAL`	`139 139`		`Copper 2; type 2 (By similarity).`
`METAL`	`174 174`		`Copper 2; type 2 (By similarity).`
`METAL`	`175 175`		`Copper 1; type 1 (By similarity).`
`METAL`	`184 184`		`Copper 1; type 1 (By similarity).`
`METAL`	`189 189`		`Copper 1; type 1 (By similarity).`
`METAL`	`345 345`		`Copper 2; type 2 (By similarity).`

Sequence information

Length: 379 AA [This is the length of the unprocessed precursor]

Molecular weight: 40694 Da [This is the MW of the unprocessed precursor]

CRC64: 090A3CBF6662F62F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSEQFRLTRR SMLAGAAVAG ALAPVVTSVA HAEGGGIKTN SAATAANIAT LERVKVELVK 

        70         80         90        100        110        120 
PPFVHAHTQK AEGEPKVVEF KMTIQEKKIV VDDKGTEVHA MTFDGSVPGP MMIVHQDDYV 

       130        140        150        160        170        180 
ELTLVNPDTN ELQHNIDFHS ATGALGGGAL TVVNPGDTAV LRFKATKAGV FVYHCAPAGM 

       190        200        210        220        230        240 
VPWHVTSGMN GAIMVLPRDG LKDHKGHELV YDKVYYVGEQ DFYVPKDENG KFKKYESAGE 

       250        260        270        280        290        300 
AYPDVLEAMK TLTPTHVVFN GAVGALTGDN ALQAKVGDRV LILHSQANRD TRPHLIGGHG 

       310        320        330        340        350        360 
DYVWATGKFA NPPELDQETW FIPGGAAGAA YYTFQQPGIY AYVNHNLIEA FELGAAGHFK 

       370 
VTGDWNDDLM TAVVSPTSG

Q01537 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