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 02-SEP-2026, entry version 116. 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 Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / OS Af293) (Neosartorya fumigata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Fumigati. OX NCBI_TaxID=330879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293; 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=L-kynurenine + NADPH + O2 + H(+) = 3-hydroxy-L-kynurenine + CC NADP(+) + H2O; 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; Evidence={ECO:0000255|HAMAP- CC 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; AAHF01000006; EAL88589.1; -; Genomic_DNA. DR RefSeq; XP_750627.1; XM_745534.2. DR AlphaFoldDB; Q4WN75; -. DR SMR; Q4WN75; -. DR FunCoup; Q4WN75; 753. DR STRING; 330879.Q4WN75; -. DR EnsemblFungi; Afu6g07340-T; Afu6g07340-T-p1; Afu6g07340. 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; 10053569at2759; -. 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:0004502; F:kynurenine 3-monooxygenase activity; IBA:GO_Central. DR GO; GO:0034354; P:'de novo' NAD+ biosynthetic process from L-tryptophan; IEA:UniProtKB-UniRule. DR GO; GO:0006569; P:L-tryptophan catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 3.50.50.60:FF:000129; Kynurenine 3-monooxygenase; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 PANTHER; PTHR46028; KYNURENINE 3-MONOOXYGENASE; 1. DR PANTHER; PTHR46028:SF2; KYNURENINE 3-MONOOXYGENASE; 1. DR Pfam; PF01494; FAD_binding_3; 1. DR PRINTS; PR00420; RNGMNOXGNASE. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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 //