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)

Q60214

- NIR_RHISU

UniProt

Q60214 - NIR_RHISU

Protein

Copper-containing nitrite reductase

Gene

nirK

Organism
Rhizobium sullae (Rhizobium hedysari)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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 By similarity.By similarity
    Binds 1 Cu+ ion. The Cu+ ion is bound within a single monomer By similarity.By similarity
    FAD.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi132 – 1321Copper 1; type 1By similarity
    Metal bindingi137 – 1371Copper 2; type 2By similarity
    Metal bindingi172 – 1721Copper 2; type 2By similarity
    Metal bindingi173 – 1731Copper 1; type 1By similarity
    Metal bindingi182 – 1821Copper 1; type 1By similarity
    Metal bindingi187 – 1871Copper 1; type 1By similarity
    Metal bindingi343 – 3431Copper 2; type 2By similarity

    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

    BioCyciRETL1328306-WGS:GSTH-4432-MONOMER.
    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
    OrganismiRhizobium sullae (Rhizobium hedysari)
    Taxonomic identifieri50338 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

    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
    Signal peptidei1 – 3535Tat-type signalPROSITE-ProRule annotationAdd
    BLAST
    Chaini36 – 377342Copper-containing nitrite reductasePRO_0000002990Add
    BLAST

    Post-translational modificationi

    Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

    Interactioni

    Subunit structurei

    Homotrimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ60214.
    SMRiQ60214. Positions 42-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini99 – 19496Plastocyanin-like 1Add
    BLAST
    Domaini259 – 360102Plastocyanin-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, Signal

    Family and domain databases

    Gene3Di2.60.40.420. 2 hits.
    InterProiIPR001117. Cu-oxidase.
    IPR011707. Cu-oxidase_3.
    IPR008972. Cupredoxin.
    IPR001287. NO2-reductase_Cu.
    IPR006311. TAT_signal.
    [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.
    PROSITEiPS51318. TAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q60214-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTNTLQMTRR TMLTGAAVAG ALTPILTSGG GNASPTPVRK LSATEIAALP    50
    RRKLDLVKPP FVHVHTQKAE GGPKVVEVTL TIEEKKLVID GKGTEVNAMT 100
    FDGSVPGPLI VVHQDDYVEV TLVNPETNTL QHNIDFHSAT GALGGGALTV 150
    VNPGESAVLR FKATKAGVFV YHCAPPGMVP WHVTSGMNGA IMVLPREGLT 200
    DGHGKELVYD KVYYLGEQDF YIPRDEKGEF KKYDSPGEAY EDTVAVMRTL 250
    TPTHIVFNGA VGALTGENAL TAAVGERVLI VHSQANRDTR PHLIGGHGEY 300
    VWRTGKFVNV PDRDQETWFI PGPTRGAAYY TFEQPGIYAY VNHNLIEAFE 350
    LGAAAHFKVT GDWNDDLMTT VRSPSGS 377
    Length:377
    Mass (Da):40,719
    Last modified:November 1, 1996 - v1
    Checksum:iC7AFEE9AE639E2F8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U65658 Genomic DNA. Translation: AAB05880.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U65658 Genomic DNA. Translation: AAB05880.1 .

    3D structure databases

    ProteinModelPortali Q60214.
    SMRi Q60214. Positions 42-377.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00652 ; UER00707 .
    BioCyci RETL1328306-WGS:GSTH-4432-MONOMER.

    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.
    IPR006311. TAT_signal.
    [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.
    PROSITEi PS51318. TAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the gene encoding nitrite reductase and the physiological consequences of its expression in the nondenitrifying Rhizobium 'hedysari' strain HCNT1."
      Toffanin A., Wu Q., Maskus M., Caselia S., Abruna H.D., Shapleigh J.P.
      Appl. Environ. Microbiol. 62:4019-4025(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: HCNT1.

    Entry informationi

    Entry nameiNIR_RHISU
    AccessioniPrimary (citable) accession number: Q60214
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3