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Protein

Kynureninase

Gene

Kynu

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.UniRule annotation1 Publication

Catalytic activityi

L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation1 Publication
L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation1 Publication

Cofactori

Enzyme regulationi

Inhibited by o-methylbenzoylalanine (OMBA).1 Publication

Kineticsi

  1. KM=440 µM for L-kynurenine1 Publication
  2. KM=32 µM for DL-3-hydroxykynurenine1 Publication

    pH dependencei

    Optimum pH is about 9.0 with L-kynurenine as substrate, and about 8.5 with DL-3-hydroxykynurenine as substrate.1 Publication

    Pathway:iL-kynurenine degradation

    This protein is involved in step 1 of the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Kynureninase (Kynu)
    This subpathway is part of the pathway L-kynurenine degradation, which is itself part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine, the pathway L-kynurenine degradation and in Amino-acid degradation.

    Pathway:iNAD(+) biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Kynurenine 3-monooxygenase (Kmo)
    2. Kynureninase (Kynu)
    3. 3-hydroxyanthranilate 3,4-dioxygenase (Haao)
    This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei137 – 1371Pyridoxal phosphate; via amide nitrogenUniRule annotation
    Binding sitei138 – 1381Pyridoxal phosphateUniRule annotation
    Binding sitei221 – 2211Pyridoxal 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

    • kynureninase activity Source: RGD
    • pyridoxal phosphate binding Source: RGD

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15007.
    ReactomeiREACT_350374. Tryptophan catabolism.
    SABIO-RKP70712.
    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:Kynu
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494 Componenti: Chromosome 3

    Organism-specific databases

    RGDi71061. Kynu.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: RGD
    • mitochondrion Source: Ensembl
    • nucleoplasm Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 464464KynureninasePRO_0000218659Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineUniRule annotation1 Publication
    Modified residuei276 – 2761N6-(pyridoxal phosphate)lysineUniRule annotation

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP70712.

    Expressioni

    Tissue specificityi

    High levels in liver and kidney. Also detected in heart, retina, ovary. Lung, testis and brain.1 Publication

    Inductioni

    Inhibited by thiol reagents and heavy metal ions.

    Gene expression databases

    GenevisibleiP70712. RN.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000050947.

    Structurei

    3D structure databases

    ProteinModelPortaliP70712.
    SMRiP70712. Positions 6-460.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    eggNOGiCOG3844.
    GeneTreeiENSGT00390000008033.
    HOGENOMiHOG000242438.
    HOVERGENiHBG001170.
    InParanoidiP70712.
    KOiK01556.
    OMAiGWYGGDK.
    OrthoDBiEOG7D2FDV.
    PhylomeDBiP70712.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_01970. Kynureninase.
    InterProiIPR000192. Aminotrans_V_dom.
    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.

    P70712-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEPSPLELPV DAVRRIATEL NCDPTDERVA LRLDEEDKLK RFKDCFYIPK
    60 70 80 90 100
    MRDLPSIDLS LVNEDDNAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIGAY
    110 120 130 140 150
    GHEVGKRPWI IGDESIVSLM KDIVGAHEKE IALMNALTVN LHLLLLSFFK
    160 170 180 190 200
    PTPKRHKILL EAKAFPSDHY AIESQIQLHG LDVEKSMRMI KPREGEETLR
    210 220 230 240 250
    MEDILEVIEK EGDSIAVVLF SGLHFYTGQL FNIPAITQAG HAKGCFVGFD
    260 270 280 290 300
    LAHAVGNVEL HLHDWDVDFA CWCSYKYLNS GAGGLAGAFI HEKHAHTIKP
    310 320 330 340 350
    ALVGWFGHEL STRFNMDNKL QLIPGVNGFR ISNPPILLVC SLHASLEIFQ
    360 370 380 390 400
    QATMTALRRK SILLTGYLEY LLKHYHGGND TENKRPVVNI ITPSRAEERG
    410 420 430 440 450
    CQLTLTFSIS KKGVFKELEK RGVVCDKREP EGIRVAPVPL YNSFHDVYKF
    460
    IRLLTAILDS TERN
    Length:464
    Mass (Da):52,470
    Last modified:November 9, 2004 - v2
    Checksum:i1490A74EFF7287AC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181T → A in AAC53206 (PubMed:9180257).Curated
    Sequence conflicti26 – 261D → N AA sequence (PubMed:7578221).Curated
    Sequence conflicti118 – 1181S → T in AAC53206 (PubMed:9180257).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U68168 mRNA. Translation: AAC53206.1.
    BC078762 mRNA. Translation: AAH78762.1.
    PIRiPS0370.
    S59898.
    T48675.
    RefSeqiNP_446354.1. NM_053902.2.
    UniGeneiRn.10575.

    Genome annotation databases

    EnsembliENSRNOT00000043533; ENSRNOP00000050947; ENSRNOG00000029993.
    GeneIDi116682.
    KEGGirno:116682.
    UCSCiRGD:71061. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U68168 mRNA. Translation: AAC53206.1.
    BC078762 mRNA. Translation: AAH78762.1.
    PIRiPS0370.
    S59898.
    T48675.
    RefSeqiNP_446354.1. NM_053902.2.
    UniGeneiRn.10575.

    3D structure databases

    ProteinModelPortaliP70712.
    SMRiP70712. Positions 6-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000050947.

    Chemistry

    BindingDBiP70712.
    ChEMBLiCHEMBL2969.

    Proteomic databases

    PRIDEiP70712.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000043533; ENSRNOP00000050947; ENSRNOG00000029993.
    GeneIDi116682.
    KEGGirno:116682.
    UCSCiRGD:71061. rat.

    Organism-specific databases

    CTDi8942.
    RGDi71061. Kynu.

    Phylogenomic databases

    eggNOGiCOG3844.
    GeneTreeiENSGT00390000008033.
    HOGENOMiHOG000242438.
    HOVERGENiHBG001170.
    InParanoidiP70712.
    KOiK01556.
    OMAiGWYGGDK.
    OrthoDBiEOG7D2FDV.
    PhylomeDBiP70712.

    Enzyme and pathway databases

    UniPathwayiUPA00253; UER00329.
    UPA00334; UER00455.
    BioCyciMetaCyc:MONOMER-15007.
    ReactomeiREACT_350374. Tryptophan catabolism.
    SABIO-RKP70712.

    Miscellaneous databases

    NextBioi619528.
    PROiP70712.

    Gene expression databases

    GenevisibleiP70712. RN.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_01970. Kynureninase.
    InterProiIPR000192. Aminotrans_V_dom.
    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT MET-1.
      Strain: Wistar.
      Tissue: Liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
      Tissue: Liver.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-117, PARTIAL PROTEIN SEQUENCE.
      Tissue: Kidney and Liver.
    5. Matsui Lee I.S., Okuno E., Kido R.
      Submitted (JUN-1992) to the PIR data bank
      Cited for: PROTEIN SEQUENCE OF 83-116 AND 273-319.
      Tissue: Liver.

    Entry informationi

    Entry nameiKYNU_RAT
    AccessioniPrimary (citable) accession number: P70712
    Secondary accession number(s): Q68G25, Q7M0D0, Q9QW90
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 9, 2004
    Last modified: June 24, 2015
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.