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Q92Z29

- NIRK_RHIME

UniProt

Q92Z29 - NIRK_RHIME

Protein

Copper-containing nitrite reductase

Gene

nirK

Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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 bindingi131 – 1311Copper 1; type 1By similarity
    Metal bindingi136 – 1361Copper 2; type 2By similarity
    Metal bindingi171 – 1711Copper 2; type 2By similarity
    Metal bindingi172 – 1721Copper 1; type 1By similarity
    Metal bindingi181 – 1811Copper 1; type 1By similarity
    Metal bindingi186 – 1861Copper 1; type 1By similarity
    Metal bindingi342 – 3421Copper 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

    BioCyciSMEL266834:GJF6-5689-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
    Ordered Locus Names:RA0681
    ORF Names:SMa1250
    Encoded oniPlasmid pSymA (megaplasmid 1)0 Publication
    OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
    Taxonomic identifieri266834 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
    ProteomesiUP000001976: Plasmid pSymA

    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 – 3333Tat-type signalPROSITE-ProRule annotationAdd
    BLAST
    Chaini34 – 376343Copper-containing nitrite reductasePRO_0000002991Add
    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

    Protein-protein interaction databases

    STRINGi266834.SMa1250.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92Z29.
    SMRiQ92Z29. Positions 45-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini98 – 19396Plastocyanin-like 1Add
    BLAST
    Domaini258 – 359102Plastocyanin-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

    Phylogenomic databases

    eggNOGiCOG2132.
    HOGENOMiHOG000217143.
    KOiK00368.
    OMAiNIDFHSA.
    OrthoDBiEOG66B40C.

    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.

    Q92Z29-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEQFQMTRR SMLAGAAIAG AVTPLIGAVS AHAEEAVAKT AHINVASLPR    50
    VKVDLVKPPF VHAHTQKAEG GPKVVEFTLT IEEKKIVIDE QGTELHAMTF 100
    NGSVPGPLMV VHQDDYVELT LINPDTNTLQ HNIDFHSATG ALGGGALTVV 150
    NPGDTTVLRF KASKAGVFVY HCAPPGMVPW HVTSGMNGAI MVLPREGLTD 200
    GKGNSITYDK VYYVGEQDFY VPRDANGKFK KYESVGEAYA DTLEVMRTLT 250
    PSHIVFNGAV GALTGDSALK AAVGEKVLIV HSQANRDTRP HLIGGHGDYV 300
    WATGKFRNAP DVDQETWFIP GGTAGAAFYT FEQPGIYAYV NHNLIEAFEL 350
    GAAAHFAVTG DWNDDLMTSV RAPSGT 376
    Length:376
    Mass (Da):40,259
    Last modified:December 1, 2001 - v1
    Checksum:i9B7999273001DC63
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006469 Genomic DNA. Translation: AAK65339.1.
    PIRiA95347.
    RefSeqiNP_435927.1. NC_003037.1.

    Genome annotation databases

    EnsemblBacteriaiAAK65339; AAK65339; SMa1250.
    GeneIDi1235717.
    KEGGisme:SMa1250.
    PATRICi23627844. VBISinMel96828_0701.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006469 Genomic DNA. Translation: AAK65339.1 .
    PIRi A95347.
    RefSeqi NP_435927.1. NC_003037.1.

    3D structure databases

    ProteinModelPortali Q92Z29.
    SMRi Q92Z29. Positions 45-376.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 266834.SMa1250.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK65339 ; AAK65339 ; SMa1250 .
    GeneIDi 1235717.
    KEGGi sme:SMa1250.
    PATRICi 23627844. VBISinMel96828_0701.

    Phylogenomic databases

    eggNOGi COG2132.
    HOGENOMi HOG000217143.
    KOi K00368.
    OMAi NIDFHSA.
    OrthoDBi EOG66B40C.

    Enzyme and pathway databases

    UniPathwayi UPA00652 ; UER00707 .
    BioCyci SMEL266834:GJF6-5689-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 1021.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 1021.

    Entry informationi

    Entry nameiNIRK_RHIME
    AccessioniPrimary (citable) accession number: Q92Z29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 87 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

    Complete proteome, Plasmid, Reference proteome

    Documents

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

    External Data

    Dasty 3