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P70712

- KYNU_RAT

UniProt

P70712 - KYNU_RAT

Protein

Kynureninase

Gene

Kynu

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (09 Nov 2004)
      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. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.1 PublicationUniRule annotation

    Catalytic activityi

    L-kynurenine + H2O = anthranilate + L-alanine.1 PublicationUniRule annotation
    L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.1 PublicationUniRule annotation

    Cofactori

    Pyridoxal phosphate.

    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

    Pathwayi

    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

    1. kynureninase activity Source: RGD
    2. pyridoxal phosphate binding Source: RGD

    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 to acetyl-CoA Source: RGD
    8. tryptophan catabolic process to kynurenine Source: RGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15007.
    ReactomeiREACT_222206. 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: Chromosome 3

    Organism-specific databases

    RGDi71061. Kynu.

    Subcellular locationi

    GO - Cellular componenti

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

    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-acetylmethionine1 PublicationUniRule annotation
    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

    GenevestigatoriP70712.

    Interactioni

    Subunit structurei

    Homodimer.

    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.
    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/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.

    P70712-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEPSPLELPV DAVRRIATEL NCDPTDERVA LRLDEEDKLK RFKDCFYIPK    50
    MRDLPSIDLS LVNEDDNAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIGAY 100
    GHEVGKRPWI IGDESIVSLM KDIVGAHEKE IALMNALTVN LHLLLLSFFK 150
    PTPKRHKILL EAKAFPSDHY AIESQIQLHG LDVEKSMRMI KPREGEETLR 200
    MEDILEVIEK EGDSIAVVLF SGLHFYTGQL FNIPAITQAG HAKGCFVGFD 250
    LAHAVGNVEL HLHDWDVDFA CWCSYKYLNS GAGGLAGAFI HEKHAHTIKP 300
    ALVGWFGHEL STRFNMDNKL QLIPGVNGFR ISNPPILLVC SLHASLEIFQ 350
    QATMTALRRK SILLTGYLEY LLKHYHGGND TENKRPVVNI ITPSRAEERG 400
    CQLTLTFSIS KKGVFKELEK RGVVCDKREP EGIRVAPVPL YNSFHDVYKF 450
    IRLLTAILDS TERN 464
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U68168 mRNA. Translation: AAC53206.1 .
    BC078762 mRNA. Translation: AAH78762.1 .
    PIRi PS0370.
    S59898.
    T48675.
    RefSeqi NP_446354.1. NM_053902.2.
    UniGenei Rn.10575.

    3D structure databases

    ProteinModelPortali P70712.
    SMRi P70712. Positions 6-460.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P70712.
    ChEMBLi CHEMBL2969.

    Proteomic databases

    PRIDEi P70712.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000043533 ; ENSRNOP00000050947 ; ENSRNOG00000029993 .
    GeneIDi 116682.
    KEGGi rno:116682.
    UCSCi RGD:71061. rat.

    Organism-specific databases

    CTDi 8942.
    RGDi 71061. Kynu.

    Phylogenomic databases

    eggNOGi COG3844.
    GeneTreei ENSGT00390000008033.
    HOGENOMi HOG000242438.
    HOVERGENi HBG001170.
    KOi K01556.
    OMAi GWYGGDK.
    OrthoDBi EOG7D2FDV.
    PhylomeDBi P70712.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00329 .
    UPA00334 ; UER00455 .
    BioCyci MetaCyc:MONOMER-15007.
    Reactomei REACT_222206. Tryptophan catabolism.
    SABIO-RK P70712.

    Miscellaneous databases

    NextBioi 619528.
    PROi P70712.

    Gene expression databases

    Genevestigatori P70712.

    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. 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: October 1, 2014
    This is version 117 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