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P38169

- KMO_YEAST

UniProt

P38169 - KMO_YEAST

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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

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

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
Complete GO annotation...

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.
ReactomeiREACT_230831. Tryptophan catabolism.
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-KW
Complete GO annotation...

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. 49 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 – 85Combined sources
Helixi12 – 2312Combined sources
Beta strandi27 – 348Combined sources
Beta strandi39 – 413Combined sources
Beta strandi50 – 556Combined sources
Helixi56 – 6510Combined sources
Helixi67 – 737Combined sources
Turni74 – 763Combined sources
Beta strandi82 – 865Combined sources
Beta strandi92 – 965Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi104 – 1085Combined sources
Helixi109 – 12012Combined sources
Turni121 – 1244Combined sources
Beta strandi126 – 1294Combined sources
Beta strandi131 – 1377Combined sources
Beta strandi143 – 1497Combined sources
Turni150 – 1534Combined sources
Beta strandi156 – 16611Combined sources
Helixi173 – 1797Combined sources
Beta strandi185 – 1906Combined sources
Beta strandi194 – 2007Combined sources
Turni208 – 2103Combined sources
Beta strandi211 – 2133Combined sources
Beta strandi220 – 2256Combined sources
Beta strandi230 – 2356Combined sources
Beta strandi241 – 2477Combined sources
Helixi249 – 2557Combined sources
Helixi259 – 26911Combined sources
Helixi271 – 2733Combined sources
Turni274 – 2763Combined sources
Helixi279 – 28810Combined sources
Beta strandi295 – 3006Combined sources
Beta strandi302 – 3043Combined sources
Turni305 – 3084Combined sources
Beta strandi309 – 3113Combined sources
Helixi314 – 3174Combined sources
Turni321 – 3233Combined sources
Helixi326 – 34318Combined sources
Turni344 – 3463Combined sources
Helixi348 – 37730Combined sources
Turni384 – 3863Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP38169.
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

        10         20         30         40         50
MSESVAIIGA GLVGCLAALA FSKEGYNVTL YDFRQDPRLD TTKNKNLKSI
60 70 80 90 100
NLAISARGID ALKSIDPDAC EHILQDMIPM KGRMIHDLKG RQESQLYGLH
110 120 130 140 150
GEAINSINRS VLNNSLLDEL EKSTTELKFG HKLVKIEWTD DKQICHFAIG
160 170 180 190 200
EDLKTPHTEK YDFVIGCDGA YSATRSQMQR KVEMDFSQEY MNLRYIELYI
210 220 230 240 250
PPTEEFKPNY GGNFAIAPDH LHIWPRHKFM LIALANSDGS FTSTFFGSKD
260 270 280 290 300
QISDLITSKS RVREFLIENF PDIINIMDLD DAVKRFITYP KESLVCVNCK
310 320 330 340 350
PYDVPGGKAI LLGDAAHAMV PFYGQGMNCG FEDVRILMAL LKKHSGDRSR
360 370 380 390 400
AFTEYTQTRH KDLVSITELA KRNYKEMSHD VTSKRFLLRK KLDALFSIIM
410 420 430 440 450
KDKWIPLYTM ISFRSDISYS RALERAGKQT RILKFLESLT LGMLSIGGYK
460
LFKFLTRERS
Length:460
Mass (Da):52,429
Last modified:October 1, 1994 - v1
Checksum:i5340CC6C9D901D17
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 49 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.
InParanoidi P38169.
KOi K00486.
OMAi QPMISVK.
OrthoDBi EOG7QVMC6.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00328 .
BioCyci MetaCyc:MONOMER-8166.
YEAST:YBL098W-MONOMER.
Reactomei REACT_230831. Tryptophan catabolism.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 131 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