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Q05979

- KYNU_YEAST

UniProt

Q05979 - KYNU_YEAST

Protein

Kynureninase

Gene

BNA5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 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 sitei111 – 1111Pyridoxal phosphate; via amide nitrogenUniRule annotation
    Binding sitei112 – 1121Pyridoxal phosphateUniRule annotation
    Binding sitei196 – 1961Pyridoxal phosphateUniRule annotation
    Binding sitei226 – 2261Pyridoxal phosphateUniRule annotation
    Binding sitei229 – 2291Pyridoxal phosphateUniRule annotation
    Binding sitei251 – 2511Pyridoxal phosphateUniRule annotation
    Binding sitei286 – 2861Pyridoxal phosphateUniRule annotation
    Binding sitei314 – 3141Pyridoxal phosphateUniRule annotation

    GO - Molecular functioni

    1. kynureninase activity Source: SGD
    2. protein binding Source: IntAct
    3. pyridoxal phosphate binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. 'de novo' NAD biosynthetic process from tryptophan Source: SGD
    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

    BioCyciMetaCyc:MONOMER-8163.
    YEAST:YLR231C-MONOMER.
    UniPathwayiUPA00253; UER00329.
    UPA00334; UER00455.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
    Alternative name(s):
    Biosynthesis of nicotinic acid protein 5UniRule annotation
    L-kynurenine hydrolaseUniRule annotation
    Gene namesi
    Name:BNA5UniRule annotation
    Ordered Locus Names:YLR231C
    ORF Names:L8083.14
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR231c.
    SGDiS000004221. BNA5.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 453453KynureninasePRO_0000218665Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei252 – 2521N6-(pyridoxal phosphate)lysineUniRule annotation

    Proteomic databases

    MaxQBiQ05979.
    PaxDbiQ05979.
    PeptideAtlasiQ05979.

    Expressioni

    Gene expression databases

    GenevestigatoriQ05979.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RSP5P399402EBI-10016,EBI-16219

    Protein-protein interaction databases

    BioGridi31501. 38 interactions.
    DIPiDIP-6518N.
    IntActiQ05979. 6 interactions.
    MINTiMINT-706654.
    STRINGi4932.YLR231C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05979.
    SMRiQ05979. Positions 4-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni139 – 1424Pyridoxal phosphate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the kynureninase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG3844.
    GeneTreeiENSGT00390000008033.
    HOGENOMiHOG000242438.
    KOiK01556.
    OMAiACESHIN.
    OrthoDBiEOG7V1G0J.

    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.

    Q05979-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKALELDGE YPESLRDEFN IPTFKSMGLS SDDKPVTYLC GNSLGLMPKS    50
    TRNSINAELD AWSDCAVESH FKHPEEARGK VPWVSIDLPI LPLLAPIVGA 100
    QENEVAVMNS LTANLNSLLI TFYKPTEKRF KILFEKGSFP SDYYAFYNQC 150
    KIHGISEPEN VFIQIEPREG ETYIRTQDIL DTIEVNQDEL ALVCLSGVQY 200
    YTGQYFDIGR ITSFAHQFPD ILVGWDLAHA VGNVPLQLHD WGVDFACWCS 250
    YKYLNAGPGG IGGLFVHSKH TKPDPAKESL PRLAGWWGND PAKRFQMLEV 300
    FEPIPGALGF RQSNPSVIDT VALRSSLELF AKFNGINEVR KRSLLLTNYM 350
    TELLEASKYY KHPLRIEKLP CFFTILTPTS TDEEHGAQLS LYFDSDTGKE 400
    DIMPKVFQYL HDHGVIGDAR RPNVIRLAPA PLYNTFSDVY IAVNALNEAM 450
    DKL 453
    Length:453
    Mass (Da):51,032
    Last modified:November 1, 1996 - v1
    Checksum:i95C84CBB4F6FCF9B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U19027 Genomic DNA. Translation: AAB67417.1.
    BK006945 Genomic DNA. Translation: DAA09548.1.
    PIRiS51453.
    RefSeqiNP_013332.1. NM_001182118.1.

    Genome annotation databases

    EnsemblFungiiYLR231C; YLR231C; YLR231C.
    GeneIDi850933.
    KEGGisce:YLR231C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U19027 Genomic DNA. Translation: AAB67417.1 .
    BK006945 Genomic DNA. Translation: DAA09548.1 .
    PIRi S51453.
    RefSeqi NP_013332.1. NM_001182118.1.

    3D structure databases

    ProteinModelPortali Q05979.
    SMRi Q05979. Positions 4-451.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31501. 38 interactions.
    DIPi DIP-6518N.
    IntActi Q05979. 6 interactions.
    MINTi MINT-706654.
    STRINGi 4932.YLR231C.

    Proteomic databases

    MaxQBi Q05979.
    PaxDbi Q05979.
    PeptideAtlasi Q05979.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR231C ; YLR231C ; YLR231C .
    GeneIDi 850933.
    KEGGi sce:YLR231C.

    Organism-specific databases

    CYGDi YLR231c.
    SGDi S000004221. BNA5.

    Phylogenomic databases

    eggNOGi COG3844.
    GeneTreei ENSGT00390000008033.
    HOGENOMi HOG000242438.
    KOi K01556.
    OMAi ACESHIN.
    OrthoDBi EOG7V1G0J.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00329 .
    UPA00334 ; UER00455 .
    BioCyci MetaCyc:MONOMER-8163.
    YEAST:YLR231C-MONOMER.

    Miscellaneous databases

    NextBioi 967372.
    PROi Q05979.

    Gene expression databases

    Genevestigatori Q05979.

    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 nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae."
      Panozzo C., Nawara M., Suski C., Kucharczyka R., Skoneczny M., Becam A.-M., Rytka J., Herbert C.J.
      FEBS Lett. 517:97-102(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PATHWAY.
    4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKYNU_YEAST
    AccessioniPrimary (citable) accession number: Q05979
    Secondary accession number(s): D6VYN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 3060 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3