P38169 (KMO_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11
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. HAMAP-Rule MF_03018 Deletion of BNA4 suppresses the toxicity of a mutant HD/HTT fragment. HAMAP-Rule MF_03018
Sequence similarities	Belongs to the aromatic-ring hydroxylase family. KMO subfamily.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	de novo NAD biosynthetic process from tryptophan Inferred from genetic interaction Ref.5. Source: SGD
Cellular_component	mitochondrial outer membrane Inferred from direct assay Ref.6. Source: SGD
Molecular_function	kynurenine 3-monooxygenase activity Inferred from mutant phenotype Ref.11. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SSA2	P10592	1	EBI-21350,EBI-8603

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 460	460	Kynurenine 3-monooxygenase HAMAP-Rule MF_03018		PRO_0000020823
Amino acid modifications
	Modified residue	4	1	Phosphoserine Ref.10
	Modified residue	22	1	Phosphoserine Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P38169 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 5340CC6C9D901D17	FASTA	460	52,429
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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], MASS SPECTROMETRY. 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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-22, MASS SPECTROMETRY. Strain: YAL6B.
[11]	"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.
PIR	S45402.
RefSeq	NP_009454.1. NM_001178338.1.
3D structure databases
ProteinModelPortal	P38169.
SMR	P38169. Positions 1-379.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5165N.
IntAct	P38169. 1 interaction.
MINT	MINT-557938.
STRING	4932.YBL098W.
Proteomic databases
PaxDb	P38169.
PeptideAtlas	P38169.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBL098W; YBL098W; YBL098W.
GeneID	852179.
KEGG	sce:YBL098W.
Organism-specific databases
CYGD	YBL098w.
SGD	S000000194. BNA4.
Phylogenomic databases
eggNOG	COG0654.
GeneTree	ENSGT00390000000747.
HOGENOM	HOG000251788.
KO	K00486.
OMA	YFPDAIP.
OrthoDB	EOG4QG0P2.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-8166.
UniPathway	UPA00253; UER00328.
Gene expression databases
Genevestigator	P38169.
GermOnline	YBL098W. Saccharomyces cerevisiae.
Family and domain databases
HAMAP	MF_01971. Kynurenine_monooxygenase.
InterPro	IPR002938. mOase_FAD-bd. IPR003042. Rng_hydrolase-like. [Graphical view]
Pfam	PF01494. FAD_binding_3. 1 hit. [Graphical view]
PRINTS	PR00420. RNGMNOXGNASE.
ProtoNet	Search...
Other
NextBio	970640.

Entry information

Entry name

KMO_YEAST

Accession

Primary (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:	April 3, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program