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P38169 (KMO_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kynurenine 3-monooxygenase

EC=1.14.13.9
Alternative name(s):
Biosynthesis of nicotinic acid protein 4
Kynurenine 3-hydroxylase
Gene names
Name:BNA4
Ordered Locus Names:YBL098W
ORF Names:YBL0828
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
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.5 Ref.10

Catalytic activity

L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O. HAMAP-Rule MF_03018

Cofactor

FAD.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3. Ref.5

Subcellular location

Mitochondrion outer membrane Ref.6 Ref.7 Ref.8.

Miscellaneous

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

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 HAMAP-Rule MF_03018
PRO_0000020823

Secondary structure

........................................................................... 460
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38169 [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] [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. 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[8]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]"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] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79489 Genomic DNA. Translation: CAA56002.1.
Z35859 Genomic DNA. Translation: CAA84920.1.
AY692951 Genomic DNA. Translation: AAT92970.1.
BK006936 Genomic DNA. Translation: DAA07027.1.
PIRS45402.
RefSeqNP_009454.1. NM_001178338.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP38169.
SMRP38169. Positions 1-389.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32607. 48 interactions.
DIPDIP-5165N.
IntActP38169. 1 interaction.
MINTMINT-557938.
STRING4932.YBL098W.

Proteomic databases

PaxDbP38169.
PeptideAtlasP38169.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBL098W; YBL098W; YBL098W.
GeneID852179.
KEGGsce:YBL098W.

Organism-specific databases

CYGDYBL098w.
SGDS000000194. BNA4.

Phylogenomic databases

eggNOGCOG0654.
GeneTreeENSGT00390000000747.
HOGENOMHOG000251788.
KOK00486.
OMAQPMISVK.
OrthoDBEOG7QVMC6.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-8166.
YEAST:YBL098W-MONOMER.
UniPathwayUPA00253; UER00328.

Gene expression databases

GenevestigatorP38169.

Family and domain databases

HAMAPMF_01971. Kynurenine_monooxygenase.
InterProIPR027545. Kynurenine_monooxygenase.
IPR002938. mOase_FAD-bd.
IPR003042. Rng_hydrolase-like.
[Graphical view]
PfamPF01494. FAD_binding_3. 1 hit.
[Graphical view]
PRINTSPR00420. RNGMNOXGNASE.
ProtoNetSearch...

Other

NextBio970640.
PROP38169.

Entry information

Entry nameKMO_YEAST
AccessionPrimary (citable) accession number: P38169
Secondary accession number(s): D6VPQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: March 19, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways