Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9CXF0

- KYNU_MOUSE

UniProt

Q9CXF0 - KYNU_MOUSE

Protein

Kynureninase

Gene

Kynu

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 3 (16 Dec 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

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

    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:
    KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
    Alternative name(s):
    L-kynurenine hydrolaseUniRule annotation
    Gene namesi
    Name:Kynu
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1918039. Kynu.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 464464KynureninasePRO_0000218658Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9CXF0.
    PaxDbiQ9CXF0.
    PRIDEiQ9CXF0.

    PTM databases

    PhosphoSiteiQ9CXF0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9CXF0.
    BgeeiQ9CXF0.
    CleanExiMM_KYNU.
    GenevestigatoriQ9CXF0.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CXF0.
    SMRiQ9CXF0. 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.
    HOVERGENiHBG001170.
    InParanoidiQ9CXF0.
    KOiK01556.
    OMAiGWYGGDK.

    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.

    Q9CXF0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEPSPLELPV DAVRRIAAEL NCDPTDERVA LRLDEEDKLS HFRNCFYIPK    50
    MRDLPSIDLS LVSEDDDAIY FLGNSLGLQP KMVRTYLEEE LDKWAKMGAY 100
    GHDVGKRPWI VGDESIVSLM KDIVGAHEKE IALMNALTIN LHLLLLSFFK 150
    PTPKRHKILL EAKAFPSDHY AIESQIQLHG LDVEKSMRMV KPREGEETLR 200
    MEDILEVIEE EGDSIAVILF SGLHFYTGQL FNIPAITKAG HAKGCFVGFD 250
    LAHAVGNVEL RLHDWGVDFA CWCSYKYLNS GAGGLAGAFV HEKHAHTVKP 300
    ALVGWFGHDL STRFNMDNKL QLIPGANGFR ISNPPILLVC SLHASLEVFQ 350
    QATMTALRRK SILLTGYLEY MLKHYHSKDN TENKGPIVNI ITPSRAEERG 400
    CQLTLTFSIP KKSVFKELEK RGVVCDKREP DGIRVAPVPL YNSFHDVYKF 450
    IRLLTSILDS SERS 464
    Length:464
    Mass (Da):52,325
    Last modified:December 16, 2008 - v3
    Checksum:iFF51BE81F935E79E
    GO

    Sequence cautioni

    The sequence BAB29386.2 differs from that shown. Reason: Erroneous initiation.
    The sequence BAC34035.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014484 mRNA. Translation: BAB29386.2. Different initiation.
    AK050024 mRNA. Translation: BAC34035.1. Different initiation.
    RefSeqiNP_001276522.1. NM_001289593.1.
    NP_001276523.1. NM_001289594.1.
    NP_081828.1. NM_027552.2.
    XP_006498388.1. XM_006498325.1.
    UniGeneiMm.105278.

    Genome annotation databases

    GeneIDi70789.
    KEGGimmu:70789.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014484 mRNA. Translation: BAB29386.2 . Different initiation.
    AK050024 mRNA. Translation: BAC34035.1 . Different initiation.
    RefSeqi NP_001276522.1. NM_001289593.1.
    NP_001276523.1. NM_001289594.1.
    NP_081828.1. NM_027552.2.
    XP_006498388.1. XM_006498325.1.
    UniGenei Mm.105278.

    3D structure databases

    ProteinModelPortali Q9CXF0.
    SMRi Q9CXF0. Positions 6-460.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9CXF0.

    Proteomic databases

    MaxQBi Q9CXF0.
    PaxDbi Q9CXF0.
    PRIDEi Q9CXF0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 70789.
    KEGGi mmu:70789.

    Organism-specific databases

    CTDi 8942.
    MGIi MGI:1918039. Kynu.

    Phylogenomic databases

    eggNOGi COG3844.
    HOVERGENi HBG001170.
    InParanoidi Q9CXF0.
    KOi K01556.
    OMAi GWYGGDK.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00329 .
    UPA00334 ; UER00455 .

    Miscellaneous databases

    ChiTaRSi KYNU. mouse.
    NextBioi 332254.
    PROi Q9CXF0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9CXF0.
    Bgeei Q9CXF0.
    CleanExi MM_KYNU.
    Genevestigatori Q9CXF0.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Liver.

    Entry informationi

    Entry nameiKYNU_MOUSE
    AccessioniPrimary (citable) accession number: Q9CXF0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 9, 2004
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 101 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3