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P81445 (NIR_ALCXX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismAlcaligenes xylosoxydans xylosoxydans (Achromobacter xylosoxidans)
Taxonomic identifier85698 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeAchromobacter

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

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

FAD.

Pathway

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

Subunit structure

Homotrimer.

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.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 2 plastocyanin-like domains.

Ontologies

Keywords
   Biological processNitrate assimilation
   Cellular componentPeriplasm
   DomainRepeat
   LigandCopper
FAD
Flavoprotein
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
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

Chain1 – 330330Copper-containing nitrite reductase
PRO_0000085586

Regions

Domain1 – 165165Plastocyanin-like 1
Domain166 – 330165Plastocyanin-like 2

Sites

Metal binding851Copper 1; type 1
Metal binding901Copper 2; type 2
Metal binding1251Copper 2; type 2
Metal binding1261Copper 1; type 1
Metal binding1351Copper 1; type 1
Metal binding1401Copper 1; type 1
Metal binding2961Copper 2; type 2

Sequences

Sequence LengthMass (Da)Tools
P81445 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: E2C38C3A2CEBFCE8

FASTA33034,413
        10         20         30         40         50         60 
GLPRVAVDLV APPLVHPHSQ VAAGAPKVVQ FRMSIEEKKM VADDDGTTAQ AMTFNGSVPG 

        70         80         90        100        110        120 
PTLVVHEGDY IELTLVNPAT NSMPHNVDFH AATGALGGAG LTQVVPGQEA VLRFKADRSG 

       130        140        150        160        170        180 
TFVYHCAPAG MVPWHVVSGM NGALMVLPRD GLRDAAGAAL AYDRVYTIGE SDLYVPKAAD 

       190        200        210        220        230        240 
GNYSDYPALA SAYADTVAVM RTLTPSHAVF NGAVGALTGA NALTAAVGES VLIIHSQANR 

       250        260        270        280        290        300 
DSRPHLIGGH GDWVWTTGKF ANPPQLNMET WFIPGGSAAA ALYTFKQPGT YAYLSHNLIE 

       310        320        330 
AMELGAAAQA SVEGQWDDDL MTSVAAPGPA 

« Hide

References

[1]"Structures of a blue-copper nitrite reductase and its substrate-bound complex."
Dodd F.E., Hasnain S.S., Abraham Z.H.L., Eady R.R., Smith B.E.
Acta Crystallogr. D 53:406-418(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Strain: LMG 1865 / NCIMB 11015 / Iwasaki.
[2]"Purification and characterization of the dissimilatory nitrite reductase from Alcaligenes xylosoxidans subsp. xylosoxidans (N.C.I.M.B. 11015): evidence for the presence of both type 1 and type 2 copper centres."
Abraham Z.H.L., Lowe D.J., Smith B.E.
Biochem. J. 295:587-593(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: LMG 1865 / NCIMB 11015 / Iwasaki.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NDRX-ray3.00A/B/C1-330[»]
1NDSX-ray2.80A/B/C1-330[»]
ProteinModelPortalP81445.
SMRP81445. Positions 2-329.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP81445.
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.
[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.
ProtoNetSearch...

Other

EvolutionaryTraceP81445.

Entry information

Entry nameNIR_ALCXX
AccessionPrimary (citable) accession number: P81445
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: November 1, 1998
Last modified: October 16, 2013
This is version 69 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways