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A2QJI5

- KYNU2_ASPNC

UniProt

A2QJI5 - KYNU2_ASPNC

Protein

Kynureninase 2

Gene

bna5-2

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.UniRule annotation

    Catalytic activityi

    L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation
    L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation

    Cofactori

    Pyridoxal phosphate.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei134 – 1341Pyridoxal phosphate; via amide nitrogenUniRule annotation
    Binding sitei135 – 1351Pyridoxal phosphateUniRule annotation
    Binding sitei247 – 2471Pyridoxal phosphateUniRule annotation
    Binding sitei250 – 2501Pyridoxal phosphateUniRule annotation
    Binding sitei272 – 2721Pyridoxal phosphateUniRule annotation
    Binding sitei312 – 3121Pyridoxal phosphateUniRule annotation
    Binding sitei340 – 3401Pyridoxal phosphateUniRule annotation

    GO - Molecular functioni

    1. kynureninase activity Source: UniProtKB-HAMAP
    2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
    2. anthranilate metabolic process Source: UniProtKB-HAMAP
    3. L-kynurenine catabolic process Source: UniProtKB-UniPathway
    4. quinolinate biosynthetic process Source: UniProtKB-HAMAP
    5. tryptophan catabolic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    UniPathwayiUPA00253; UER00329.
    UPA00334; UER00455.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kynureninase 2UniRule annotation (EC:3.7.1.3UniRule annotation)
    Alternative name(s):
    Biosynthesis of nicotinic acid protein 5-2UniRule annotation
    L-kynurenine hydrolase 2UniRule annotation
    Gene namesi
    Name:bna5-2
    ORF Names:An04g07200
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 6L

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 463463Kynureninase 2PRO_0000356968Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei273 – 2731N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00004336.

    Structurei

    3D structure databases

    ProteinModelPortaliA2QJI5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni162 – 1654Pyridoxal phosphate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the kynureninase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG3844.
    HOGENOMiHOG000242438.
    KOiK01556.
    OrthoDBiEOG7V1G0J.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_01970. Kynureninase.
    InterProiIPR000192. Aminotrans_V/Cys_dSase.
    IPR010111. Kynureninase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR14084. PTHR14084. 1 hit.
    PfamiPF00266. Aminotran_5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038800. KYNU. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR01814. kynureninase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A2QJI5-1 [UniParc]FASTAAdd to Basket

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    MSKSNGVSLA FPAEAATKEY AASLDSSDRL AAFREKFIVP SKANIASKKL    50
    AKPGLSPESC IYFCGNSLGI QPKATAKYLE AQLDTWSSIG VGGHFTDLEG 100
    SPLKQWQLLS EQAADSMSKI VGAKPEEVAA MGTLTTNLHL LLASFYKPTQ 150
    TKHKILMDWK AFPSDHYAIE SHIAWHDLDP KESMVLIGPD EGEYEISTQK 200
    IFSYIDKHAD EAAMILLPGI QYYTGQLFDI QKITKYAHSR NMVVGWDLAH 250
    AFANVELKLH DWNVDFAAWC TYKYGNAGPG AMGGLFVHEQ HGEVDYSAGE 300
    DAPKFRHRLT GWYGGDRSVR FKMDNKFKPI PGAGGFQISN PSAIDLACLC 350
    AALSVFDETS MADLRRKSLK LTAYLEFLLL RDYEEESRPF SIITPKDPEA 400
    RGAQLSLLLK PGLLQNVAQK LQEAGIVCDK REPGVVRVAP VPLYNSFSEV 450
    WTFVKIFKDA LQQ 463
    Length:463
    Mass (Da):51,300
    Last modified:March 6, 2007 - v1
    Checksum:i69BFF4F248B8AB07
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270081 Genomic DNA. Translation: CAK44720.1.
    RefSeqiXP_001402081.1. XM_001402044.2.

    Genome annotation databases

    EnsemblFungiiCADANGAT00004431; CADANGAP00004336; CADANGAG00004431.
    GeneIDi4991124.
    KEGGiang:ANI_1_1148184.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270081 Genomic DNA. Translation: CAK44720.1 .
    RefSeqi XP_001402081.1. XM_001402044.2.

    3D structure databases

    ProteinModelPortali A2QJI5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00004336.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00004431 ; CADANGAP00004336 ; CADANGAG00004431 .
    GeneIDi 4991124.
    KEGGi ang:ANI_1_1148184.

    Phylogenomic databases

    eggNOGi COG3844.
    HOGENOMi HOG000242438.
    KOi K01556.
    OrthoDBi EOG7V1G0J.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00329 .
    UPA00334 ; UER00455 .

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPi MF_01970. Kynureninase.
    InterProi IPR000192. Aminotrans_V/Cys_dSase.
    IPR010111. Kynureninase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    PANTHERi PTHR14084. PTHR14084. 1 hit.
    Pfami PF00266. Aminotran_5. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038800. KYNU. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR01814. kynureninase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
      Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
      , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
      Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CBS 513.88 / FGSC A1513.

    Entry informationi

    Entry nameiKYNU2_ASPNC
    AccessioniPrimary (citable) accession number: A2QJI5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 16, 2008
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 51 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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