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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

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
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.
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 – 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.
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:
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. 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.

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: October 29, 2014
This is version 130 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