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Reviewed, UniProtKB/Swiss-Prot P38169 (KMO_YEAST)

Last modified November 3, 2009. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Kynurenine 3-monooxygenase
    EC=1.14.13.9
Alternative name(s):
    Kynurenine 3-hydroxylase
    Biosynthesis of nicotinic acid protein 4
Gene names
Name: BNA4
Ordered Locus Names: YBL098W
ORF Names: YBL0828
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid. Ref.4 Ref.9

Catalytic activity

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

Cofactor

FAD.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3. Ref.4

Subcellular location

Mitochondrion. Ref.5 Ref.6

Miscellaneous

Present with 556 molecules/cell in log phase SD medium. Ref.7

Deletion of BNA4 suppresses the toxicity of a mutant HD/HTT fragment.

Sequence similarities

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SSA2P105921EBI-21350,EBI-8603

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 460460Kynurenine 3-monooxygenase
PRO_0000020823

Amino acid modifications

Modified residue41Phosphoserine Ref.8
Modified residue221Phosphoserine Ref.8

Sequences

Sequence LengthMass (Da)Tools
P38169-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 5340CC6C9D901D17

FASTA46052,429
        10         20         30         40         50         60 
MSESVAIIGA GLVGCLAALA FSKEGYNVTL YDFRQDPRLD TTKNKNLKSI NLAISARGID 

        70         80         90        100        110        120 
ALKSIDPDAC EHILQDMIPM KGRMIHDLKG RQESQLYGLH GEAINSINRS VLNNSLLDEL 

       130        140        150        160        170        180 
EKSTTELKFG HKLVKIEWTD DKQICHFAIG EDLKTPHTEK YDFVIGCDGA YSATRSQMQR 

       190        200        210        220        230        240 
KVEMDFSQEY MNLRYIELYI PPTEEFKPNY GGNFAIAPDH LHIWPRHKFM LIALANSDGS 

       250        260        270        280        290        300 
FTSTFFGSKD QISDLITSKS RVREFLIENF PDIINIMDLD DAVKRFITYP KESLVCVNCK 

       310        320        330        340        350        360 
PYDVPGGKAI LLGDAAHAMV PFYGQGMNCG FEDVRILMAL LKKHSGDRSR AFTEYTQTRH 

       370        380        390        400        410        420 
KDLVSITELA KRNYKEMSHD VTSKRFLLRK KLDALFSIIM KDKWIPLYTM ISFRSDISYS 

       430        440        450        460 
RALERAGKQT RILKFLESLT LGMLSIGGYK LFKFLTRERS 

« Hide

References

« Hide 'large scale' references
[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: 7502586] [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. expand/collapse author list , 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: 7813418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"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: 12062417] [Abstract]
Cited for: FUNCTION, PATHWAY.
[5]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-22, MASS SPECTROMETRY.
[9]"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: 15806102] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

X79489 Genomic DNA. Translation: CAA56002.1.
Z35859 Genomic DNA. Translation: CAA84920.1.
AY692951 Genomic DNA. Translation: AAT92970.1.
PIRS45402.
RefSeqNP_009454.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5165N.
IntActP38169. 2 interactions.
STRINGP38169.

Proteomic databases

PeptideAtlasP38169.

Genome annotation databases

EnsemblYBL098W; YBL098W; YBL098W; Saccharomyces cerevisiae. [Genome view]
GeneID852179.
GenomeReviewsGene locus YBL098W in contig Y13134_GR.
KEGGsce:YBL098W.
NMPDRfig|4932.3.peg.140.

Organism-specific databases

CYGDYBL098w.
SGDS000000194. BNA4.

Phylogenomic databases

HOGENOMP38169.
OMALHAIMPS.

Enzyme and pathway databases

BioCycMetaCyc:MON-8166.
BRENDA1.14.13.9. 250.

Gene expression databases

ArrayExpressP38169.
GenevestigatorP38169.
GermOnlineYBL098W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR003042. Rng_hydrolase-like.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
PRINTSPR00420. RNGMNOXGNASE.
ProtoNetSearch...

Other Resources

NextBio970640.

Entry information

Entry nameKMO_YEAST
AccessionPrimary (citable) accession number: P38169
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 3, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents