Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q01537 (NIR_RHIGA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 78. 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:nirU
OrganismRhizobium galegae
Taxonomic identifier399 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length379 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.

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.

Caution

It is uncertain whether Met-1 or Met-12 is the initiator.

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 – 3232Tat-type signal Potential
Chain33 – 379347Copper-containing nitrite reductase
PRO_0000002989

Regions

Domain33 – 214182Plastocyanin-like 1
Domain215 – 379165Plastocyanin-like 2

Sites

Metal binding1341Copper 1; type 1 By similarity
Metal binding1391Copper 2; type 2 By similarity
Metal binding1741Copper 2; type 2 By similarity
Metal binding1751Copper 1; type 1 By similarity
Metal binding1841Copper 1; type 1 By similarity
Metal binding1891Copper 1; type 1 By similarity
Metal binding3451Copper 2; type 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01537 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 090A3CBF6662F62F

FASTA37940,694
        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 

« Hide

References

[1]"Characterization of the structural gene encoding a copper-containing nitrite reductase and homology of this gene to DNA of other denitrifiers."
Ye R.W., Fries M.R., Bezborodnikov S.G., Averill B.A., Tiedje J.M.
Appl. Environ. Microbiol. 59:250-254(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: G-179.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97294 Genomic DNA. Translation: AAC79132.1.
PIRA48936.

3D structure databases

ProteinModelPortalQ01537.
SMRQ01537. Positions 47-378.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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_RHIGA
AccessionPrimary (citable) accession number: Q01537
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 16, 2013
This is version 78 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