ID   KMO_ASPFU               Reviewed;         512 AA.
AC   Q4WN75;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
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; ORFNames=AFUA_6G07340;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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}.
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DR   EMBL; AAHF01000006; EAL88589.1; -; Genomic_DNA.
DR   RefSeq; XP_750627.1; XM_745534.1.
DR   AlphaFoldDB; Q4WN75; -.
DR   SMR; Q4WN75; -.
DR   STRING; 746128.CADAFUBP00007138; -.
DR   EnsemblFungi; EAL88589; EAL88589; AFUA_6G07340.
DR   GeneID; 3508717; -.
DR   KEGG; afm:AFUA_6G07340; -.
DR   VEuPathDB; FungiDB:Afu6g07340; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   HOGENOM; CLU_023210_2_1_1; -.
DR   InParanoid; Q4WN75; -.
DR   OMA; REFMFIA; -.
DR   OrthoDB; 462247at2759; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000002530; Chromosome 6.
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..512
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361918"
SQ   SEQUENCE   512 AA;  58088 MW;  0CACA1B38B85140D CRC64;
     MADTVRKKQK LVVVGAGPVG SLAALYAAAR GDEVEIYELR GDLRDPSTVP LNFTKSINLA
     LSERGITAMK HSNREDLVNN VLRDTIPMHG RMIHGRDRGK LWEAAQAYDV HGRAINAVDR
     STLNNALLDE LECTPNVKLF FNHKLTGADF NARKAWFERR VPGEAPLPNS ANRVPEIEVD
     FDFMIGADGA HSAARYHMMK FARVDYQQEY IDTLWCEFRI PPTEDGDFRI SPNHLHIWPG
     REFMFIALPS ADKSFTCTLF APAAHYKHLG SSPQNLVESF KDHFPGVCPE LISPEDLQEQ
     FTTNPHLPLI SLKCKPHHYN SSIVIVGDAA HAVLPFYGQG LNAGLEDIRV LFECLDKHGS
     YNLDASPDAR REARAKAFQA YTDQRCADTH AINDLSKQNY LEMRWGVKTP LYKLRKSVEE
     ALDRYVPSLG WQTQYSRVSF SNQRYSDVIR SARWQGRILA LGLATTLIST VGVIAYVFWK
     KPRQYSPLSL LRYSWRRLSS IWVTMFRTIA YA