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Q60214 (NIR_RHISU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Copper-containing nitrite reductase

EC=1.7.2.1
Alternative name(s):
Cu-NIR
Gene names
Name:nirK
OrganismRhizobium sullae (Rhizobium hedysari)
Taxonomic identifier50338 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+.

Cofactor

Binds 1 Cu2+ ion. The Cu2+ ion is held by residues from each of 2 monomers of the trimer. Nitrite is bound to the Cu2+ ion site. Pseudoazurin is the physiological electron donor for the Cu-NIR in vitro By similarity.

Binds 1 Cu+ ion. The Cu+ ion is bound within a single monomer By similarity.

FAD By similarity.

Pathway

Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 2/4.

Subunit structure

Homotrimer By similarity.

Subcellular location

Periplasm By similarity.

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.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 2 plastocyanin-like domains.

Ontologies

Keywords
   Biological processNitrate assimilation
   Cellular componentPeriplasm
   DomainRepeat
Signal
   LigandCopper
FAD
Flavoprotein
Metal-binding
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processdenitrification pathway

Inferred from electronic annotation. Source: UniProtKB-UniPathway

nitrate assimilation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncopper ion binding

Inferred from electronic annotation. Source: InterPro

nitrite reductase (NO-forming) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535Tat-type signal Potential
Chain36 – 377342Copper-containing nitrite reductase
PRO_0000002990

Regions

Domain99 – 19496Plastocyanin-like 1
Domain259 – 360102Plastocyanin-like 2

Sites

Metal binding1321Copper 1; type 1 By similarity
Metal binding1371Copper 2; type 2 By similarity
Metal binding1721Copper 2; type 2 By similarity
Metal binding1731Copper 1; type 1 By similarity
Metal binding1821Copper 1; type 1 By similarity
Metal binding1871Copper 1; type 1 By similarity
Metal binding3431Copper 2; type 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q60214 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C7AFEE9AE639E2F8

FASTA37740,719
        10         20         30         40         50         60 
MTNTLQMTRR TMLTGAAVAG ALTPILTSGG GNASPTPVRK LSATEIAALP RRKLDLVKPP 

        70         80         90        100        110        120 
FVHVHTQKAE GGPKVVEVTL TIEEKKLVID GKGTEVNAMT FDGSVPGPLI VVHQDDYVEV 

       130        140        150        160        170        180 
TLVNPETNTL QHNIDFHSAT GALGGGALTV VNPGESAVLR FKATKAGVFV YHCAPPGMVP 

       190        200        210        220        230        240 
WHVTSGMNGA IMVLPREGLT DGHGKELVYD KVYYLGEQDF YIPRDEKGEF KKYDSPGEAY 

       250        260        270        280        290        300 
EDTVAVMRTL TPTHIVFNGA VGALTGENAL TAAVGERVLI VHSQANRDTR PHLIGGHGEY 

       310        320        330        340        350        360 
VWRTGKFVNV PDRDQETWFI PGPTRGAAYY TFEQPGIYAY VNHNLIEAFE LGAAAHFKVT 

       370 
GDWNDDLMTT VRSPSGS 

« Hide

References

[1]"Characterization of the gene encoding nitrite reductase and the physiological consequences of its expression in the nondenitrifying Rhizobium 'hedysari' strain HCNT1."
Toffanin A., Wu Q., Maskus M., Caselia S., Abruna H.D., Shapleigh J.P.
Appl. Environ. Microbiol. 62:4019-4025(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: HCNT1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U65658 Genomic DNA. Translation: AAB05880.1.

3D structure databases

ProteinModelPortalQ60214.
SMRQ60214. Positions 42-377.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycRETL1328306-WGS:GSTH-4432-MONOMER.
UniPathwayUPA00652; UER00707.

Family and domain databases

Gene3D2.60.40.420. 2 hits.
InterProIPR001117. Cu-oxidase.
IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
IPR001287. NO2-reductase_Cu.
IPR006311. TAT_signal.
[Graphical view]
PfamPF00394. Cu-oxidase. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
PRINTSPR00695. CUNO2RDTASE.
SUPFAMSSF49503. SSF49503. 2 hits.
TIGRFAMsTIGR02376. Cu_nitrite_red. 1 hit.
PROSITEPS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNIR_RHISU
AccessionPrimary (citable) accession number: Q60214
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways