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Q92Z29 (NIRK_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 86. 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
Ordered Locus Names:RA0681
ORF Names:SMa1250
Encoded onPlasmid pSymA (megaplasmid 1)
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length376 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
   Technical termComplete proteome
Plasmid
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 – 3333Tat-type signal Potential
Chain34 – 376343Copper-containing nitrite reductase
PRO_0000002991

Regions

Domain98 – 19396Plastocyanin-like 1
Domain258 – 359102Plastocyanin-like 2

Sites

Metal binding1311Copper 1; type 1 By similarity
Metal binding1361Copper 2; type 2 By similarity
Metal binding1711Copper 2; type 2 By similarity
Metal binding1721Copper 1; type 1 By similarity
Metal binding1811Copper 1; type 1 By similarity
Metal binding1861Copper 1; type 1 By similarity
Metal binding3421Copper 2; type 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92Z29 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 9B7999273001DC63

FASTA37640,259
        10         20         30         40         50         60 
MSEQFQMTRR SMLAGAAIAG AVTPLIGAVS AHAEEAVAKT AHINVASLPR VKVDLVKPPF 

        70         80         90        100        110        120 
VHAHTQKAEG GPKVVEFTLT IEEKKIVIDE QGTELHAMTF NGSVPGPLMV VHQDDYVELT 

       130        140        150        160        170        180 
LINPDTNTLQ HNIDFHSATG ALGGGALTVV NPGDTTVLRF KASKAGVFVY HCAPPGMVPW 

       190        200        210        220        230        240 
HVTSGMNGAI MVLPREGLTD GKGNSITYDK VYYVGEQDFY VPRDANGKFK KYESVGEAYA 

       250        260        270        280        290        300 
DTLEVMRTLT PSHIVFNGAV GALTGDSALK AAVGEKVLIV HSQANRDTRP HLIGGHGDYV 

       310        320        330        340        350        360 
WATGKFRNAP DVDQETWFIP GGTAGAAFYT FEQPGIYAYV NHNLIEAFEL GAAAHFAVTG 

       370 
DWNDDLMTSV RAPSGT 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006469 Genomic DNA. Translation: AAK65339.1.
PIRA95347.
RefSeqNP_435927.1. NC_003037.1.

3D structure databases

ProteinModelPortalQ92Z29.
SMRQ92Z29. Positions 45-376.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266834.SMa1250.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK65339; AAK65339; SMa1250.
GeneID1235717.
KEGGsme:SMa1250.
PATRIC23627844. VBISinMel96828_0701.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2132.
HOGENOMHOG000217143.
KOK00368.
OMANIDFHSA.
OrthoDBEOG66B40C.

Enzyme and pathway databases

BioCycSMEL266834:GJF6-5689-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 nameNIRK_RHIME
AccessionPrimary (citable) accession number: Q92Z29
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: December 1, 2001
Last modified: May 14, 2014
This is version 86 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