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P38169

- KMO_YEAST

UniProt

P38169 - KMO_YEAST

Protein

Kynurenine 3-monooxygenase

Gene

BNA4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.2 PublicationsUniRule annotation

    Catalytic activityi

    L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O.UniRule annotation

    Cofactori

    FAD.

    Pathwayi

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: UniProtKB-HAMAP
    2. kynurenine 3-monooxygenase activity Source: SGD

    GO - Biological processi

    1. 'de novo' NAD biosynthetic process from tryptophan Source: SGD
    2. anthranilate metabolic process Source: UniProtKB-HAMAP
    3. quinolinate biosynthetic process Source: UniProtKB-HAMAP
    4. tryptophan catabolic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-8166.
    YEAST:YBL098W-MONOMER.
    UniPathwayiUPA00253; UER00328.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kynurenine 3-monooxygenaseUniRule annotation (EC:1.14.13.9UniRule annotation)
    Alternative name(s):
    Biosynthesis of nicotinic acid protein 4UniRule annotation
    Kynurenine 3-hydroxylaseUniRule annotation
    Gene namesi
    Name:BNA4UniRule annotation
    Ordered Locus Names:YBL098W
    ORF Names:YBL0828
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBL098w.
    SGDiS000000194. BNA4.

    Subcellular locationi

    Mitochondrion outer membrane 3 PublicationsUniRule annotation

    GO - Cellular componenti

    1. mitochondrial outer membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 460460Kynurenine 3-monooxygenasePRO_0000020823Add
    BLAST

    Proteomic databases

    MaxQBiP38169.
    PaxDbiP38169.
    PeptideAtlasiP38169.

    Expressioni

    Gene expression databases

    GenevestigatoriP38169.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SSA2P105921EBI-21350,EBI-8603

    Protein-protein interaction databases

    BioGridi32607. 48 interactions.
    DIPiDIP-5165N.
    IntActiP38169. 1 interaction.
    MINTiMINT-557938.
    STRINGi4932.YBL098W.

    Structurei

    Secondary structure

    1
    460
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Helixi12 – 2312
    Beta strandi27 – 348
    Beta strandi39 – 413
    Beta strandi50 – 556
    Helixi56 – 6510
    Helixi67 – 737
    Turni74 – 763
    Beta strandi82 – 865
    Beta strandi92 – 965
    Beta strandi99 – 1013
    Beta strandi104 – 1085
    Helixi109 – 12012
    Turni121 – 1244
    Beta strandi126 – 1294
    Beta strandi131 – 1377
    Beta strandi143 – 1497
    Turni150 – 1534
    Beta strandi156 – 16611
    Helixi173 – 1797
    Beta strandi185 – 1906
    Beta strandi194 – 2007
    Turni208 – 2103
    Beta strandi211 – 2133
    Beta strandi220 – 2256
    Beta strandi230 – 2356
    Beta strandi241 – 2477
    Helixi249 – 2557
    Helixi259 – 26911
    Helixi271 – 2733
    Turni274 – 2763
    Helixi279 – 28810
    Beta strandi295 – 3006
    Beta strandi302 – 3043
    Turni305 – 3084
    Beta strandi309 – 3113
    Helixi314 – 3174
    Turni321 – 3233
    Helixi326 – 34318
    Turni344 – 3463
    Helixi348 – 37730
    Turni384 – 3863

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4J2WX-ray2.60A/B1-396[»]
    4J31X-ray2.40A/B1-396[»]
    4J33X-ray1.82A/B1-394[»]
    4J34X-ray2.03A/B1-394[»]
    4J36X-ray2.13A/B1-394[»]
    ProteinModelPortaliP38169.
    SMRiP38169. Positions 1-389.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aromatic-ring hydroxylase family. KMO subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0654.
    GeneTreeiENSGT00390000000747.
    HOGENOMiHOG000251788.
    KOiK00486.
    OMAiQPMISVK.
    OrthoDBiEOG7QVMC6.

    Family and domain databases

    HAMAPiMF_01971. Kynurenine_monooxygenase.
    InterProiIPR027545. Kynurenine_monooxygenase.
    IPR002938. mOase_FAD-bd.
    IPR003042. Rng_hydrolase-like.
    [Graphical view]
    PfamiPF01494. FAD_binding_3. 1 hit.
    [Graphical view]
    PRINTSiPR00420. RNGMNOXGNASE.

    Sequencei

    Sequence statusi: Complete.

    P38169-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSESVAIIGA GLVGCLAALA FSKEGYNVTL YDFRQDPRLD TTKNKNLKSI    50
    NLAISARGID ALKSIDPDAC EHILQDMIPM KGRMIHDLKG RQESQLYGLH 100
    GEAINSINRS VLNNSLLDEL EKSTTELKFG HKLVKIEWTD DKQICHFAIG 150
    EDLKTPHTEK YDFVIGCDGA YSATRSQMQR KVEMDFSQEY MNLRYIELYI 200
    PPTEEFKPNY GGNFAIAPDH LHIWPRHKFM LIALANSDGS FTSTFFGSKD 250
    QISDLITSKS RVREFLIENF PDIINIMDLD DAVKRFITYP KESLVCVNCK 300
    PYDVPGGKAI LLGDAAHAMV PFYGQGMNCG FEDVRILMAL LKKHSGDRSR 350
    AFTEYTQTRH KDLVSITELA KRNYKEMSHD VTSKRFLLRK KLDALFSIIM 400
    KDKWIPLYTM ISFRSDISYS RALERAGKQT RILKFLESLT LGMLSIGGYK 450
    LFKFLTRERS 460
    Length:460
    Mass (Da):52,429
    Last modified:October 1, 1994 - v1
    Checksum:i5340CC6C9D901D17
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79489 Genomic DNA. Translation: CAA56002.1.
    Z35859 Genomic DNA. Translation: CAA84920.1.
    AY692951 Genomic DNA. Translation: AAT92970.1.
    BK006936 Genomic DNA. Translation: DAA07027.1.
    PIRiS45402.
    RefSeqiNP_009454.1. NM_001178338.1.

    Genome annotation databases

    EnsemblFungiiYBL098W; YBL098W; YBL098W.
    GeneIDi852179.
    KEGGisce:YBL098W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79489 Genomic DNA. Translation: CAA56002.1 .
    Z35859 Genomic DNA. Translation: CAA84920.1 .
    AY692951 Genomic DNA. Translation: AAT92970.1 .
    BK006936 Genomic DNA. Translation: DAA07027.1 .
    PIRi S45402.
    RefSeqi NP_009454.1. NM_001178338.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4J2W X-ray 2.60 A/B 1-396 [» ]
    4J31 X-ray 2.40 A/B 1-396 [» ]
    4J33 X-ray 1.82 A/B 1-394 [» ]
    4J34 X-ray 2.03 A/B 1-394 [» ]
    4J36 X-ray 2.13 A/B 1-394 [» ]
    ProteinModelPortali P38169.
    SMRi P38169. Positions 1-389.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32607. 48 interactions.
    DIPi DIP-5165N.
    IntActi P38169. 1 interaction.
    MINTi MINT-557938.
    STRINGi 4932.YBL098W.

    Proteomic databases

    MaxQBi P38169.
    PaxDbi P38169.
    PeptideAtlasi P38169.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBL098W ; YBL098W ; YBL098W .
    GeneIDi 852179.
    KEGGi sce:YBL098W.

    Organism-specific databases

    CYGDi YBL098w.
    SGDi S000000194. BNA4.

    Phylogenomic databases

    eggNOGi COG0654.
    GeneTreei ENSGT00390000000747.
    HOGENOMi HOG000251788.
    KOi K00486.
    OMAi QPMISVK.
    OrthoDBi EOG7QVMC6.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00328 .
    BioCyci MetaCyc:MONOMER-8166.
    YEAST:YBL098W-MONOMER.

    Miscellaneous databases

    NextBioi 970640.
    PROi P38169.

    Gene expression databases

    Genevestigatori P38169.

    Family and domain databases

    HAMAPi MF_01971. Kynurenine_monooxygenase.
    InterProi IPR027545. Kynurenine_monooxygenase.
    IPR002938. mOase_FAD-bd.
    IPR003042. Rng_hydrolase-like.
    [Graphical view ]
    Pfami PF01494. FAD_binding_3. 1 hit.
    [Graphical view ]
    PRINTSi PR00420. RNGMNOXGNASE.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II."
      Obermaier B., Gassenhuber J., Piravandi E., Domdey H.
      Yeast 11:1103-1112(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "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.
    6. "Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins."
      Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N., Schoenfisch B., Guiard B., Pfanner N., Meisinger C.
      Mol. Biol. Cell 17:1436-1450(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease."
      Giorgini F., Guidetti P., Nguyen Q., Bennett S.C., Muchowski P.J.
      Nat. Genet. 37:526-531(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiKMO_YEAST
    AccessioniPrimary (citable) accession number: P38169
    Secondary accession number(s): D6VPQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 129 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 556 molecules/cell in log phase SD medium.1 Publication
    Deletion of BNA4 suppresses the toxicity of a mutant HD/HTT fragment.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3