Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P81445

- NIR_ALCXX

UniProt

P81445 - NIR_ALCXX

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Nitrate assimilation

    Keywords - Ligandi

    Copper, FAD, Flavoprotein, Metal-binding

    Enzyme and pathway databases

    SABIO-RKP81445.
    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

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 330330Copper-containing nitrite reductasePRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81445.

    Family & Domainsi

    Domains and Repeats

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

    Belongs to the multicopper oxidase family.Curated
    Contains 2 plastocyanin-like domains.Curated

    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...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00652 ; UER00707 .
    SABIO-RK 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: October 1, 2014
    This is version 71 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