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E2RB73

- E2RB73_CANFA

UniProt

E2RB73 - E2RB73_CANFA

Protein

Kynureninase

Gene

KYNU

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Unreviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 32 (01 Oct 2014)
      Sequence version 2 (31 Oct 2012)
      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
    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. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.UniRule annotation

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei137 – 1371Pyridoxal phosphate; via amide nitrogenUniRule annotation
    Binding sitei138 – 1381Pyridoxal phosphateUniRule annotation
    Binding sitei250 – 2501Pyridoxal phosphateUniRule annotation
    Binding sitei253 – 2531Pyridoxal phosphateUniRule annotation
    Binding sitei275 – 2751Pyridoxal phosphateUniRule annotation
    Binding sitei305 – 3051Pyridoxal phosphateUniRule annotation
    Binding sitei333 – 3331Pyridoxal 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. response to interferon-gamma Source: Ensembl
    6. response to vitamin B6 Source: Ensembl
    7. tryptophan catabolic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    HydrolaseUniRule annotation

    Keywords - Biological processi

    Pyridine nucleotide biosynthesisUniRule annotation

    Keywords - Ligandi

    Pyridoxal phosphateUniRule annotation

    Enzyme and pathway databases

    UniPathwayiUPA00253; UER00329.
    UPA00334; UER00455.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
    Alternative name(s):
    L-kynurenine hydrolaseUniRule annotation
    Gene namesi
    Name:KYNUUniRule annotationImported
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)Imported
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Chromosome 19

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. mitochondrion Source: Ensembl
    3. nucleus Source: Ensembl

    Keywords - Cellular componenti

    CytoplasmUniRule annotation

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineUniRule annotation
    Modified residuei276 – 2761N6-(pyridoxal phosphate)lysineUniRule annotation

    Keywords - PTMi

    AcetylationUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni165 – 1684Pyridoxal phosphate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the kynureninase family.UniRule annotation

    Phylogenomic databases

    GeneTreeiENSGT00390000008033.
    KOiK01556.
    OMAiGLMNDIV.
    OrthoDBiEOG7D2FDV.
    TreeFamiTF300707.

    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.

    E2RB73-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEPLPLELPA DTVQRIASEL RCHPTDERVA LRLDEEDKLR HFKEHFHIPK    50
    MQDLPAIDLS LVNKDENAIY FSGNSLGLQP KLVKTYLEEE LDKWAKMGVY 100
    GHEVGKRPWI TGDETILGLM NDIVGANEKE IALMNGLTVN LHLLLLSFFK 150
    PTPERYKILL EAKAFPSDHY VIESQLQLHG LNVEKSMRII KPREGEETLR 200
    TEDILEVIEK EGDSIAVILF GGLHFYTGQL FNIPAITRAG QAKGCFVGFD 250
    LAHAVGNVEL HLHDWGVDFA CWCSYKYLNS GAGGLAGAFV HEKHAYRIKP 300
    ALVGWFGHEL SSRFKMDNKL QLSPGVSGFR ISNPPILLVC SLQASLEIFK 350
    QATMKALRRK SILLTGYLEY LIKHYYNKDT ADTKKPFVNI ITPSCIEERG 400
    CQLTLTFSVP MKYVFQELEK RGVVCDKREP NGIRVAPVPL YNSFHDVYKF 450
    INLLTSTLDS AETK 464
    Length:464
    Mass (Da):52,514
    Last modified:October 31, 2012 - v2
    Checksum:i48064619A1E32286
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAEX03011933 Genomic DNA. No translation available.
    RefSeqiXP_005632015.1. XM_005631958.1.
    XP_005632016.1. XM_005631959.1.
    XP_541027.3. XM_541027.4.

    Genome annotation databases

    EnsembliENSCAFT00000008804; ENSCAFP00000008166; ENSCAFG00000005466.
    GeneIDi483907.
    KEGGicfa:483907.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAEX03011933 Genomic DNA. No translation available.
    RefSeqi XP_005632015.1. XM_005631958.1.
    XP_005632016.1. XM_005631959.1.
    XP_541027.3. XM_541027.4.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSCAFT00000008804 ; ENSCAFP00000008166 ; ENSCAFG00000005466 .
    GeneIDi 483907.
    KEGGi cfa:483907.

    Organism-specific databases

    CTDi 8942.

    Phylogenomic databases

    GeneTreei ENSGT00390000008033.
    KOi K01556.
    OMAi GLMNDIV.
    OrthoDBi EOG7D2FDV.
    TreeFami TF300707.

    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 sequence, comparative analysis and haplotype structure of the domestic dog."
      Broad Sequencing Platform
      Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R.
      , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.
      Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: BoxerImported.
    2. Ensembl
      Submitted (JUL-2011) to UniProtKB
      Cited for: IDENTIFICATION.
      Strain: BoxerImported.

    Entry informationi

    Entry nameiE2RB73_CANFA
    AccessioniPrimary (citable) accession number: E2RB73
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 30, 2010
    Last sequence update: October 31, 2012
    Last modified: October 1, 2014
    This is version 32 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Caution

    The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3