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Protein

Kynurenine 3-monooxygenase

Gene

BNA4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

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

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

FAD, 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

GO - Cellular componenti

Complete GO annotation...

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.
PRIDEiP38169.

PTM databases

iPTMnetiP38169.

Interactioni

Protein-protein interaction databases

BioGridi32607. 48 interactors.
DIPiDIP-5165N.
IntActiP38169. 1 interactor.
MINTiMINT-557938.

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[»]
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.
OMAiHIWPRHN.
OrthoDBiEOG092C0D3Y.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
HAMAPiMF_01971. Kynurenine_monooxygenase. 1 hit.
InterProiIPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR027545. Kynurenine_monooxygenase.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
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.

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.
PIRiS45402.
RefSeqiNP_009454.1. NM_001178338.1.

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[»]
ProteinModelPortaliP38169.
SMRiP38169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32607. 48 interactors.
DIPiDIP-5165N.
IntActiP38169. 1 interactor.
MINTiMINT-557938.

Chemistry databases

ChEMBLiCHEMBL3627588.

PTM databases

iPTMnetiP38169.

Proteomic databases

MaxQBiP38169.
PRIDEiP38169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL098W; YBL098W; YBL098W.
GeneIDi852179.
KEGGisce:YBL098W.

Organism-specific databases

EuPathDBiFungiDB:YBL098W.
SGDiS000000194. BNA4.

Phylogenomic databases

GeneTreeiENSGT00390000000747.
HOGENOMiHOG000251788.
InParanoidiP38169.
KOiK00486.
OMAiHIWPRHN.
OrthoDBiEOG092C0D3Y.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00328.
BioCyciMetaCyc:YBL098W-MONOMER.
YEAST:YBL098W-MONOMER.
BRENDAi1.14.13.9. 984.
ReactomeiR-SCE-71240. Tryptophan catabolism.

Miscellaneous databases

PROiP38169.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
HAMAPiMF_01971. Kynurenine_monooxygenase. 1 hit.
InterProiIPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR027545. Kynurenine_monooxygenase.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiKMO_YEAST
AccessioniPrimary (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: November 30, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.