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Q9JYE1

- ANIA_NEIMB

UniProt

Q9JYE1 - ANIA_NEIMB

Protein

Copper-containing nitrite reductase

Gene

aniA

Organism
Neisseria meningitidis serogroup B (strain MC58)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the reduction of nitrite to nitric oxide (NO). It could be essential for growth and survival in oxygen-depleted environments.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 1 Cu+ ion.By similarity
    Binds 1 Cu2+ ion.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi134 – 1341Copper 1; type 1By similarity
    Metal bindingi139 – 1391Copper 2; type 2By similarity
    Binding sitei139 – 1391SubstrateBy similarity
    Metal bindingi174 – 1741Copper 2; type 2By similarity
    Metal bindingi175 – 1751Copper 1; type 1By similarity
    Metal bindingi183 – 1831Copper 1; type 1By similarity
    Metal bindingi188 – 1881Copper 1; type 1By similarity
    Binding sitei280 – 2801SubstrateBy similarity
    Metal bindingi329 – 3291Copper 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. nitrogen compound metabolic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding

    Enzyme and pathway databases

    BioCyciNMEN122586:GHGG-1672-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Copper-containing nitrite reductase (EC:1.7.2.1)
    Gene namesi
    Name:aniA
    Ordered Locus Names:NMB1623
    OrganismiNeisseria meningitidis serogroup B (strain MC58)
    Taxonomic identifieri122586 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
    ProteomesiUP000000425: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cell outer membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell outer membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818PROSITE-ProRule annotationAdd
    BLAST
    Chaini19 – 390372Copper-containing nitrite reductasePRO_0000002999Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi19 – 191N-palmitoyl cysteineCurated
    Lipidationi19 – 191S-diacylglycerol cysteineCurated

    Keywords - PTMi

    Lipoprotein, Palmitate

    Interactioni

    Subunit structurei

    Homotrimer.By similarity

    Protein-protein interaction databases

    STRINGi122586.NMB1623.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JYE1.
    SMRiQ9JYE1. Positions 53-354.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini101 – 19595Plastocyanin-like 1Add
    BLAST
    Domaini245 – 346102Plastocyanin-like 2Add
    BLAST
    Repeati371 – 37551
    Repeati376 – 38052
    Repeati381 – 38553

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni371 – 385153 X 5 AA tandem repeats of A-A-S-A-PAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG2132.
    HOGENOMiHOG000217143.
    KOiK00368.
    OMAiVEKTMKM.
    OrthoDBiEOG61ZTJ4.

    Family and domain databases

    Gene3Di2.60.40.420. 2 hits.
    InterProiIPR011707. Cu-oxidase_3.
    IPR008972. Cupredoxin.
    IPR001287. NO2-reductase_Cu.
    [Graphical view]
    PfamiPF07732. Cu-oxidase_3. 1 hit.
    [Graphical view]
    PRINTSiPR00695. CUNO2RDTASE.
    SUPFAMiSSF49503. SSF49503. 2 hits.
    TIGRFAMsiTIGR02376. Cu_nitrite_red. 1 hit.
    PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9JYE1-1 [UniParc]FASTAAdd to Basket

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    MKRQALAAMI ASLFALAACG GEPAAQAPAE TPAAAAEAAS SAAQTAAETP    50
    SGELPVIDAV TTHAPEVPPA IDRDYPAKVR VKMETVEKTM TMEDGVEYRY 100
    WTFDGDVPGR MIRVREGDTV EVEFSNNPSS TVPHNVDFHA ATGQGGGAAA 150
    TFTAPGRTST FSFKALQPGL YIYHCAVAPV GMHIANGMYG LILVEPKEGL 200
    PKVDKEFYIV QGDFYTKGKK GAQGLQPFDM DKAVAEQPEY VVFNGHVGAI 250
    AGDNALKAKA GETVRMYVGN GGPNLVSSFH VIGEIFDKVY VEGGKLINEN 300
    VQSTIVPAGG SAIVEFKVDI PGSYTLVDHS IFRAFNKGAL GQLKVEGAEN 350
    PEIMTQKLSD TAYAGNGAAP AASAPAASAP AASASEKSVY 390
    Length:390
    Mass (Da):40,763
    Last modified:October 1, 2000 - v1
    Checksum:iC503F9D47DD1169D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE002098 Genomic DNA. Translation: AAF41975.1.
    PIRiE81062.
    RefSeqiNP_274629.1. NC_003112.2.

    Genome annotation databases

    EnsemblBacteriaiAAF41975; AAF41975; NMB1623.
    GeneIDi904036.
    KEGGinme:NMB1623.
    PATRICi20359146. VBINeiMen85645_2084.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE002098 Genomic DNA. Translation: AAF41975.1 .
    PIRi E81062.
    RefSeqi NP_274629.1. NC_003112.2.

    3D structure databases

    ProteinModelPortali Q9JYE1.
    SMRi Q9JYE1. Positions 53-354.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 122586.NMB1623.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF41975 ; AAF41975 ; NMB1623 .
    GeneIDi 904036.
    KEGGi nme:NMB1623.
    PATRICi 20359146. VBINeiMen85645_2084.

    Phylogenomic databases

    eggNOGi COG2132.
    HOGENOMi HOG000217143.
    KOi K00368.
    OMAi VEKTMKM.
    OrthoDBi EOG61ZTJ4.

    Enzyme and pathway databases

    BioCyci NMEN122586:GHGG-1672-MONOMER.

    Family and domain databases

    Gene3Di 2.60.40.420. 2 hits.
    InterProi IPR011707. Cu-oxidase_3.
    IPR008972. Cupredoxin.
    IPR001287. NO2-reductase_Cu.
    [Graphical view ]
    Pfami PF07732. Cu-oxidase_3. 1 hit.
    [Graphical view ]
    PRINTSi PR00695. CUNO2RDTASE.
    SUPFAMi SSF49503. SSF49503. 2 hits.
    TIGRFAMsi TIGR02376. Cu_nitrite_red. 1 hit.
    PROSITEi PS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MC58.
    2. "Nitric oxide metabolism in Neisseria meningitidis."
      Anjum M.F., Stevanin T.M., Read R.C., Moir J.W.B.
      J. Bacteriol. 184:2987-2993(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: MC58.

    Entry informationi

    Entry nameiANIA_NEIMB
    AccessioniPrimary (citable) accession number: Q9JYE1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 83 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3