UniProtKB - P38169 (KMO_YEAST)
Protein
Kynurenine 3-monooxygenase
Gene
BNA4
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.UniRule annotation3 Publications
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.
Catalytic activityi
- H+ + L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + H2O + NADP+UniRule annotation1 PublicationEC:1.14.13.9UniRule annotation1 Publication
Cofactori
FAD1 Publication
: NAD(+) biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation2 PublicationsProteins known to be involved in the 3 steps of the subpathway in this organism are:
- Kynurenine 3-monooxygenase (BNA4)
- Kynureninase (BNA5)
- 3-hydroxyanthranilate 3,4-dioxygenase (BNA1)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 13 | FAD; via amide nitrogenCombined sources | 1 | |
Binding sitei | 53 | FAD; via amide nitrogen and carbonyl oxygenCombined sources | 1 | |
Binding sitei | 83 | L-kynurenineBy similarity | 1 | |
Binding sitei | 97 | L-kynurenineBy similarity | 1 | |
Binding sitei | 109 | FADCombined sources | 1 | |
Binding sitei | 133 | FAD; via amide nitrogen and carbonyl oxygenCombined sources | 1 | |
Binding sitei | 195 | FADCombined sources | 1 | |
Binding sitei | 314 | FADCombined sources | 1 | |
Binding sitei | 373 | L-kynurenineBy similarity | 1 | |
Binding sitei | 408 | L-kynurenineBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 32 – 34 | FADCombined sources | 3 | |
Nucleotide bindingi | 325 – 328 | FADCombined sources | 4 |
GO - Molecular functioni
- FAD binding Source: UniProtKB
- flavin adenine dinucleotide binding Source: UniProtKB
- kynurenine 3-monooxygenase activity Source: UniProtKB
- NAD(P)H oxidase (H(2)O(2)-forming activity Source: UniProtKB
GO - Biological processi
- 'de novo' NAD biosynthetic process from tryptophan Source: SGD
- anthranilate metabolic process Source: UniProtKB-UniRule
- kynurenine metabolic process Source: UniProtKB
- NAD metabolic process Source: UniProtKB
- quinolinate biosynthetic process Source: UniProtKB-UniRule
- tryptophan catabolic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | Monooxygenase, Oxidoreductase |
Biological process | Pyridine nucleotide biosynthesis |
Ligand | FAD, Flavoprotein, NADP |
Enzyme and pathway databases
BioCyci | MetaCyc:YBL098W-MONOMER |
BRENDAi | 1.14.13.9, 984 |
Reactomei | R-SCE-71240, Tryptophan catabolism |
UniPathwayi | UPA00253;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 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
EuPathDBi | FungiDB:YBL098W |
SGDi | S000000194, BNA4 |
Subcellular locationi
Mitochondrion
- Mitochondrion outer membrane UniRule annotation3 Publications
Mitochondrion
- mitochondrial outer membrane Source: SGD
- mitochondrion Source: SGD
Keywords - Cellular componenti
Membrane, Mitochondrion, Mitochondrion outer membranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 83 | R → A: Strongly decreases enzymatic activity. 1 Publication | 1 | |
Mutagenesisi | 83 | R → M: Abolsihes enzymatic activity. 1 Publication | 1 | |
Mutagenesisi | 322 – 323 | FY → AA: Abolishes NADPH oxidase activity. 1 Publication | 2 |
Chemistry databases
ChEMBLi | CHEMBL3627588 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000020823 | 1 – 460 | Kynurenine 3-monooxygenaseAdd BLAST | 460 |
Proteomic databases
MaxQBi | P38169 |
PaxDbi | P38169 |
PRIDEi | P38169 |
PTM databases
iPTMneti | P38169 |
Interactioni
Protein-protein interaction databases
BioGRIDi | 32607, 96 interactors |
DIPi | DIP-5165N |
IntActi | P38169, 2 interactors |
STRINGi | 4932.YBL098W |
Chemistry databases
BindingDBi | P38169 |
Miscellaneous databases
RNActi | P38169, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P38169 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG2614, Eukaryota |
GeneTreei | ENSGT00390000000747 |
HOGENOMi | CLU_023210_0_1_1 |
InParanoidi | P38169 |
OMAi | NLAMSNR |
Family and domain databases
Gene3Di | 3.50.50.60, 1 hit |
HAMAPi | MF_01971, Kynurenine_monooxygenase, 1 hit |
InterProi | View protein in InterPro IPR002938, FAD-bd IPR036188, FAD/NAD-bd_sf IPR027545, Kynurenine_monooxygenase |
Pfami | View protein in Pfam PF01494, FAD_binding_3, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit |
i Sequence
Sequence statusi: Complete.
P38169-1 [UniParc]FASTAAdd to basket
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
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 |
Genome annotation databases
EnsemblFungii | YBL098W_mRNA; YBL098W; YBL098W |
GeneIDi | 852179 |
KEGGi | sce:YBL098W |
Similar proteinsi
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 | PDB 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 | [»] | |
5X6R | X-ray | 1.91 | A/B | 1-394 | [»] | |
SMRi | P38169 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 32607, 96 interactors |
DIPi | DIP-5165N |
IntActi | P38169, 2 interactors |
STRINGi | 4932.YBL098W |
Chemistry databases
BindingDBi | P38169 |
ChEMBLi | CHEMBL3627588 |
PTM databases
iPTMneti | P38169 |
Proteomic databases
MaxQBi | P38169 |
PaxDbi | P38169 |
PRIDEi | P38169 |
Genome annotation databases
EnsemblFungii | YBL098W_mRNA; YBL098W; YBL098W |
GeneIDi | 852179 |
KEGGi | sce:YBL098W |
Organism-specific databases
EuPathDBi | FungiDB:YBL098W |
SGDi | S000000194, BNA4 |
Phylogenomic databases
eggNOGi | KOG2614, Eukaryota |
GeneTreei | ENSGT00390000000747 |
HOGENOMi | CLU_023210_0_1_1 |
InParanoidi | P38169 |
OMAi | NLAMSNR |
Enzyme and pathway databases
UniPathwayi | UPA00253;UER00328 |
BioCyci | MetaCyc:YBL098W-MONOMER |
BRENDAi | 1.14.13.9, 984 |
Reactomei | R-SCE-71240, Tryptophan catabolism |
Miscellaneous databases
PROi | PR:P38169 |
RNActi | P38169, protein |
Family and domain databases
Gene3Di | 3.50.50.60, 1 hit |
HAMAPi | MF_01971, Kynurenine_monooxygenase, 1 hit |
InterProi | View protein in InterPro IPR002938, FAD-bd IPR036188, FAD/NAD-bd_sf IPR027545, Kynurenine_monooxygenase |
Pfami | View protein in Pfam PF01494, FAD_binding_3, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | KMO_YEAST | |
Accessioni | P38169Primary (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: | December 2, 2020 | |
This is version 181 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - 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