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Q18026

- KYNU_CAEEL

UniProt

Q18026 - KYNU_CAEEL

Protein

Kynureninase

Gene

flu-2

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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.1 PublicationUniRule 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 sitei150 – 1501Pyridoxal phosphate; via amide nitrogenUniRule annotation
    Binding sitei151 – 1511Pyridoxal phosphateUniRule annotation
    Binding sitei234 – 2341Pyridoxal phosphateUniRule annotation
    Binding sitei263 – 2631Pyridoxal phosphateUniRule annotation
    Binding sitei266 – 2661Pyridoxal phosphateUniRule annotation
    Binding sitei288 – 2881Pyridoxal phosphateUniRule annotation
    Binding sitei318 – 3181Pyridoxal phosphateUniRule annotation
    Binding sitei346 – 3461Pyridoxal 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:
    KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
    Alternative name(s):
    Abnormal fluorescence under UV illumination
    L-kynurenine hydrolaseUniRule annotation
    Gene namesi
    Name:flu-2
    ORF Names:C15H9.7
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000001940: Chromosome X

    Organism-specific databases

    WormBaseiC15H9.7; CE06835; WBGene00015802; flu-2.

    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 – 478478KynureninasePRO_0000218660Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei289 – 2891N6-(pyridoxal phosphate)lysineUniRule annotation

    Proteomic databases

    PaxDbiQ18026.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    IntActiQ18026. 1 interaction.
    STRINGi6239.C15H9.7.

    Structurei

    3D structure databases

    ProteinModelPortaliQ18026.
    SMRiQ18026. Positions 38-471.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni178 – 1814Pyridoxal phosphate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the kynureninase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG3844.
    GeneTreeiENSGT00390000008033.
    HOGENOMiHOG000242438.
    InParanoidiQ18026.
    KOiK01556.
    OMAiHVAYRSA.
    PhylomeDBiQ18026.

    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.

    Q18026-1 [UniParc]FASTAAdd to Basket

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    MSDAPPQPEN EQECMCTQDK VLQFLNKMAD ESGIKDLTDP ALAEFLSDSD    50
    ALKEIRDLFH YPKAGTLPDA DPSLVDPESD SIYLCGNSLG LMPKATGEVM 100
    KDHLDKWAKM GVFGHMSGEV PWAHCDEYCL EGVGRLVGAK KEEVSVCNSL 150
    TVNIHVLLTS FYKPTETRHK ILLESKAFPS DHYAIESQIR LKGRTVQDSM 200
    VCLEPREGEE TLRTEDILDY IEKNGDEIAI VFFSGIQYYT GQLFDMRAIT 250
    EAGHRKGCFV GFDLAHAFAN VPLHLHWWDV DFACWCSYKY GCTGAGSIGG 300
    LFVHERFLND QRERMLGWWS HKMSSRFVMD NVLDLDEGAA GYRISNPPIH 350
    TVAAMLGSLK VFDQVSLENL RSRSCYLTGY LEYLVKTLFG ENSEQRTTKL 400
    SISIITPEEF HQRGCQLSLK FSSPIDIIYP ELVKRGCAVD KRYPNVIRVA 450
    PVHLYNNYVD IRRFISVLQE VAHIVESE 478
    Length:478
    Mass (Da):54,050
    Last modified:November 1, 1996 - v1
    Checksum:iE889450929EC94BD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FO080555 Genomic DNA. Translation: CCD64633.1.
    AF303267 mRNA. Translation: AAG50225.1.
    PIRiT15516.
    RefSeqiNP_509023.1. NM_076622.4.
    UniGeneiCel.19413.

    Genome annotation databases

    EnsemblMetazoaiC15H9.7; C15H9.7; WBGene00015802.
    GeneIDi180883.
    KEGGicel:CELE_C15H9.7.
    UCSCiC15H9.7. c. elegans.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FO080555 Genomic DNA. Translation: CCD64633.1 .
    AF303267 mRNA. Translation: AAG50225.1 .
    PIRi T15516.
    RefSeqi NP_509023.1. NM_076622.4.
    UniGenei Cel.19413.

    3D structure databases

    ProteinModelPortali Q18026.
    SMRi Q18026. Positions 38-471.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q18026. 1 interaction.
    STRINGi 6239.C15H9.7.

    Proteomic databases

    PaxDbi Q18026.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai C15H9.7 ; C15H9.7 ; WBGene00015802 .
    GeneIDi 180883.
    KEGGi cel:CELE_C15H9.7.
    UCSCi C15H9.7. c. elegans.

    Organism-specific databases

    CTDi 180883.
    WormBasei C15H9.7 ; CE06835 ; WBGene00015802 ; flu-2.

    Phylogenomic databases

    eggNOGi COG3844.
    GeneTreei ENSGT00390000008033.
    HOGENOMi HOG000242438.
    InParanoidi Q18026.
    KOi K01556.
    OMAi HVAYRSA.
    PhylomeDBi Q18026.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00329 .
    UPA00334 ; UER00455 .

    Miscellaneous databases

    NextBioi 911400.
    PROi Q18026.

    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 of the nematode C. elegans: a platform for investigating biology."
      The C. elegans sequencing consortium
      Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Bristol N2.
    2. "The Caenorhabditis elegans transcriptome project, a complementary view of the genome."
      Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y., Thierry-Mieg D., Thierry-Mieg J.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Bristol N2.
    3. "Mutagen sensitivity of kynureninase mutants of the nematode Caenorhabditis elegans."
      Bhat S.G., Babu P.
      Mol. Gen. Genet. 180:635-638(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiKYNU_CAEEL
    AccessioniPrimary (citable) accession number: Q18026
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Caenorhabditis elegans
      Caenorhabditis elegans: entries, gene names and cross-references to WormBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3