ID   KMO_USTMA               Reviewed;         600 AA.
AC   Q4P0N0; A0A0D1CUY6;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   25-MAY-2022, entry version 106.
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=UMAG_06333;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- SEQUENCE CAUTION:
CC       Sequence=KIS70248.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CM003143; KIS70248.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_011388318.1; XM_011390016.1.
DR   AlphaFoldDB; Q4P0N0; -.
DR   SMR; Q4P0N0; -.
DR   STRING; 5270.UM06333P0; -.
DR   EnsemblFungi; KIS70248; KIS70248; UMAG_06333.
DR   GeneID; 23565951; -.
DR   KEGG; uma:UMAG_06333; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   InParanoid; Q4P0N0; -.
DR   OrthoDB; 113640at2759; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000000561; Chromosome 4.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004502; F:kynurenine 3-monooxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase 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:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 2.
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; 2.
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..600
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361933"
FT   REGION          217..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   600 AA;  65460 MW;  52C6ECAF5FFC31A5 CRC64;
     MSETRKDTDR ASAQLPTKCQ LPERVAVIGA GPVGCLAALA FAQRGCKVDI FESRPDPRTH
     EAITRASQRS INLALSTRGI TGLRSVSLAG LGVGTNAPNG MDLADLVLQN SVPMRARMIH
     VVTRQASATQ AAEVKEISQL YSTKGESINS VDRGRLNNIL LEHALMHRNV EVHFEHKLQS
     VDFDHDIKSA AKRAGTPPPA IDASANKWLR GANVTGGDSC ADEPSGCGGR KQATTKSQGS
     EYVAPAGTSA VDRVRLDFDV HSTNQHIRKT SNTHYASFVV GCDGAHSSIR SAMGSLIRMH
     YTHNYIDTGY IELSIPPRTS LGSGSRIRGS GGVDGKRGGH DAFHLDANHL HIWPRHSFML
     IALPNLDGSF TCTLFAPFKM FASELSTKEG IVAVFQQHFP DALALIDEEK LVKCLTTRRA
     SALGSVQCDP YHYKDRAVLI GDAAHAMLPF YGQGLNCGFE DVRVMFDIID QHESLQVALD
     LYTKERHPDL VAILQLAEQN YREMAHSVVS WPYLLRKKLD GLLMSILPSS MWSSLYAMTT
     FSNLPYSRVV KTEKRQQAII GHALVATAVA FVSAAAVGVY STRALWQPVT VRCIARLHNS