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Protein

Kynurenine 3-monooxygenase

Gene

BNA4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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.UniRule annotation2 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

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

Cofactori

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation1 Publication
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Kynurenine 3-monooxygenase (BNA4)
  2. Kynureninase (BNA5)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (BNA1)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
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.

GO - Molecular functioni

  • FAD binding Source: InterPro
  • flavin adenine dinucleotide binding Source: GO_Central
  • kynurenine 3-monooxygenase activity Source: SGD
  • NAD(P)H oxidase activity Source: GO_Central

GO - Biological processi

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
Biological processPyridine nucleotide biosynthesis
LigandFAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciMetaCyc:YBL098W-MONOMER
YEAST:YBL098W-MONOMER
BRENDAi1.14.13.9 984
ReactomeiR-SCE-71240 Tryptophan catabolism
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
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL098W
SGDiS000000194 BNA4

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3627588

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000208231 – 460Kynurenine 3-monooxygenaseAdd BLAST460

Proteomic databases

MaxQBiP38169
PaxDbiP38169
PRIDEiP38169

PTM databases

iPTMnetiP38169

Interactioni

Protein-protein interaction databases

BioGridi32607, 95 interactors
DIPiDIP-5165N
IntActiP38169, 4 interactors
STRINGi4932.YBL098W

Chemistry databases

BindingDBiP38169

Structurei

Secondary structure

1460
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Helixi12 – 23Combined sources12
Beta strandi27 – 34Combined sources8
Beta strandi39 – 41Combined sources3
Beta strandi50 – 55Combined sources6
Helixi56 – 65Combined sources10
Helixi67 – 73Combined sources7
Turni74 – 76Combined sources3
Beta strandi82 – 86Combined sources5
Beta strandi92 – 96Combined sources5
Beta strandi99 – 101Combined sources3
Beta strandi104 – 108Combined sources5
Helixi109 – 120Combined sources12
Turni121 – 124Combined sources4
Beta strandi126 – 129Combined sources4
Beta strandi131 – 137Combined sources7
Beta strandi143 – 149Combined sources7
Turni151 – 153Combined sources3
Beta strandi156 – 166Combined sources11
Helixi173 – 179Combined sources7
Beta strandi185 – 190Combined sources6
Beta strandi194 – 200Combined sources7
Turni208 – 210Combined sources3
Beta strandi211 – 213Combined sources3
Beta strandi220 – 225Combined sources6
Beta strandi230 – 235Combined sources6
Beta strandi241 – 247Combined sources7
Helixi249 – 255Combined sources7
Helixi259 – 269Combined sources11
Helixi271 – 273Combined sources3
Turni274 – 276Combined sources3
Helixi279 – 288Combined sources10
Beta strandi295 – 300Combined sources6
Beta strandi302 – 304Combined sources3
Turni305 – 308Combined sources4
Beta strandi309 – 311Combined sources3
Helixi314 – 317Combined sources4
Turni321 – 323Combined sources3
Helixi326 – 343Combined sources18
Turni344 – 346Combined sources3
Helixi348 – 377Combined sources30
Turni384 – 386Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5X6RX-ray1.91A/B1-394[»]
ProteinModelPortaliP38169
SMRiP38169
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00390000000747
HOGENOMiHOG000251788
InParanoidiP38169
KOiK00486
OMAiMPSTFIP
OrthoDBiEOG092C0D3Y

Family and domain databases

Gene3Di3.50.50.60, 1 hit
HAMAPiMF_01971 Kynurenine_monooxygenase, 1 hit
InterProiView protein in InterPro
IPR002938 FAD-bd
IPR036188 FAD/NAD-bd_sf
IPR027545 Kynurenine_monooxygenase
PfamiView protein in Pfam
PF01494 FAD_binding_3, 1 hit
SUPFAMiSSF51905 SSF51905, 2 hits

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:
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
PIRiS45402
RefSeqiNP_009454.1, NM_001178338.1

Genome annotation databases

EnsemblFungiiYBL098W; YBL098W; YBL098W
GeneIDi852179
KEGGisce:YBL098W

Similar proteinsi

Entry informationi

Entry nameiKMO_YEAST
AccessioniPrimary (citable) accession number: P38169
Secondary accession number(s): D6VPQ7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 25, 2018
This is version 163 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health