ID   KMO_PHANO               Reviewed;         482 AA.
AC   Q0V5K1;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 3.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Kynurenine 3-monooxygenase {ECO:0000255|HAMAP-Rule:MF_03018};
DE            EC=1.14.13.9 {ECO:0000255|HAMAP-Rule:MF_03018};
DE   AltName: Full=Biosynthesis of nicotinic acid protein 4 {ECO:0000255|HAMAP-Rule:MF_03018};
DE   AltName: Full=Kynurenine 3-hydroxylase {ECO:0000255|HAMAP-Rule:MF_03018};
GN   Name=BNA4 {ECO:0000255|HAMAP-Rule:MF_03018}; ORFNames=SNOG_00713;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form
CC       3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic
CC       acid. {ECO:0000255|HAMAP-Rule:MF_03018}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine +
CC         H2O + NADP(+); Xref=Rhea:RHEA:20545, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:57959, ChEBI:CHEBI:58125, ChEBI:CHEBI:58349;
CC         EC=1.14.13.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03018};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03018};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03018}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03018}.
CC   -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03018}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH445325; EAT92208.2; -; Genomic_DNA.
DR   RefSeq; XP_001791390.1; XM_001791338.1.
DR   AlphaFoldDB; Q0V5K1; -.
DR   SMR; Q0V5K1; -.
DR   STRING; 321614.Q0V5K1; -.
DR   PRIDE; Q0V5K1; -.
DR   GeneID; 5968074; -.
DR   KEGG; pno:SNOG_00713; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   InParanoid; Q0V5K1; -.
DR   OrthoDB; 462247at2759; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0004502; F:kynurenine 3-monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IBA:GO_Central.
DR   GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
DR   GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0070189; P:kynurenine metabolic process; IBA:GO_Central.
DR   GO; GO:0019674; P:NAD metabolic process; IBA:GO_Central.
DR   GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_01971; Kynurenine_monooxygenase; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027545; Kynurenine_monooxygenase.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Monooxygenase; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..482
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361931"
SQ   SEQUENCE   482 AA;  54203 MW;  821B2728F8744B02 CRC64;
     MPQKIVVVGA GPVGSLAALY AAVRGHDVEI YELRSDLRNS EHSSNISQSI NLALSERGIN
     SLRKTGLPDL ADAVLAETFP MHGRMIHVRK HGQYVRQAQA YDAHGRNLLA MDRTGLNKTL
     LDHLNSMPNV TFFFHRKLVS VDFRKKLAWF ENRTKTDPAK SDDIEVSFDL MIGADGAHSA
     VRYHLMKFVP MSYQQEYIDK LWCQFHVPPS DKGDFRIPPN YLHIWPQDDA MFIALPNLDK
     SFTSTLFLTR SGFEELVASG KVVEYFDEKF PGVVPELITE DELRKQFNEH DHFPLISIKC
     SPYHFGSTGV IVGDSAHAMV PFYGQGMNAG LEDVRVLFEI LDKYPGDQAK ALSEYSEQRT
     PDAQTINDLA LGNYREMASD VKKPLYLLRK WIEEKLYIYV PSAGWATQYS RVTFSNMRYS
     EVQAAAQRQA KILNGIVGVT TLSLIGSAAL WLGRTGGLQQ AKQNILRSIC LLAQQAQKVT
     KG