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P81445

- NIR_ALCXX

UniProt

P81445 - NIR_ALCXX

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Protein
Copper-containing nitrite reductase
Gene
nirK
Organism
Alcaligenes xylosoxydans xylosoxydans (Achromobacter xylosoxidans)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi85 – 851Copper 1; type 1
Metal bindingi90 – 901Copper 2; type 2
Metal bindingi125 – 1251Copper 2; type 2
Metal bindingi126 – 1261Copper 1; type 1
Metal bindingi135 – 1351Copper 1; type 1
Metal bindingi140 – 1401Copper 1; type 1
Metal bindingi296 – 2961Copper 2; type 2

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. nitrite reductase (NO-forming) activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. denitrification pathway Source: UniProtKB-UniPathway
  2. nitrate assimilation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Nitrate assimilation

Keywords - Ligandi

Copper, FAD, Flavoprotein, Metal-binding

Enzyme and pathway databases

SABIO-RKiP81445.
UniPathwayiUPA00652; UER00707.

Names & Taxonomyi

Protein namesi
Recommended name:
Copper-containing nitrite reductase (EC:1.7.2.1)
Alternative name(s):
Cu-NIR
Gene namesi
Name:nirK
OrganismiAlcaligenes xylosoxydans xylosoxydans (Achromobacter xylosoxidans)
Taxonomic identifieri85698 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeAchromobacter

Subcellular locationi

Periplasm By similarity

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Copper-containing nitrite reductase
PRO_0000085586Add
BLAST

Interactioni

Subunit structurei

Homotrimer.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NDRX-ray3.00A/B/C1-329[»]
1NDSX-ray2.80A/B/C1-329[»]
ProteinModelPortaliP81445.
SMRiP81445. Positions 2-329.

Miscellaneous databases

EvolutionaryTraceiP81445.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 165165Plastocyanin-like 1
Add
BLAST
Domaini166 – 330165Plastocyanin-like 2
Add
BLAST

Domaini

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 similaritiesi

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.60.40.420. 2 hits.
InterProiIPR001117. Cu-oxidase.
IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
IPR001287. NO2-reductase_Cu.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
PRINTSiPR00695. CUNO2RDTASE.
SUPFAMiSSF49503. SSF49503. 2 hits.
TIGRFAMsiTIGR02376. Cu_nitrite_red. 1 hit.

Sequencei

Sequence statusi: Complete.

P81445-1 [UniParc]FASTAAdd to Basket

« Hide

GLPRVAVDLV APPLVHPHSQ VAAGAPKVVQ FRMSIEEKKM VADDDGTTAQ    50
AMTFNGSVPG PTLVVHEGDY IELTLVNPAT NSMPHNVDFH AATGALGGAG 100
LTQVVPGQEA VLRFKADRSG TFVYHCAPAG MVPWHVVSGM NGALMVLPRD 150
GLRDAAGAAL AYDRVYTIGE SDLYVPKAAD GNYSDYPALA SAYADTVAVM 200
RTLTPSHAVF NGAVGALTGA NALTAAVGES VLIIHSQANR DSRPHLIGGH 250
GDWVWTTGKF ANPPQLNMET WFIPGGSAAA ALYTFKQPGT YAYLSHNLIE 300
AMELGAAAQA SVEGQWDDDL MTSVAAPGPA 330
Length:330
Mass (Da):34,413
Last modified:November 1, 1998 - v1
Checksum:iE2C38C3A2CEBFCE8
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NDR X-ray 3.00 A/B/C 1-329 [» ]
1NDS X-ray 2.80 A/B/C 1-329 [» ]
ProteinModelPortali P81445.
SMRi P81445. Positions 2-329.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00652 ; UER00707 .
SABIO-RKi P81445.

Miscellaneous databases

EvolutionaryTracei P81445.

Family and domain databases

Gene3Di 2.60.40.420. 2 hits.
InterProi IPR001117. Cu-oxidase.
IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
IPR001287. NO2-reductase_Cu.
[Graphical view ]
Pfami PF00394. Cu-oxidase. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view ]
PRINTSi PR00695. CUNO2RDTASE.
SUPFAMi SSF49503. SSF49503. 2 hits.
TIGRFAMsi TIGR02376. Cu_nitrite_red. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiNIR_ALCXX
AccessioniPrimary (citable) accession number: P81445
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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