ID   KMO_CRYNB               Reviewed;         506 AA.
AC   P0CO49; Q55W30; Q5KK63;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 48.
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}; OrderedLocusNames=CNBC3070;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(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; AAEY01000013; EAL22169.1; -; Genomic_DNA.
DR   RefSeq; XP_776816.1; XM_771723.1.
DR   AlphaFoldDB; P0CO49; -.
DR   SMR; P0CO49; -.
DR   EnsemblFungi; EAL22169; EAL22169; CNBC3070.
DR   GeneID; 4934972; -.
DR   KEGG; cnb:CNBC3070; -.
DR   VEuPathDB; FungiDB:CNBC3070; -.
DR   HOGENOM; CLU_023210_0_1_1; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000001435; Chromosome 3.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071949; F:FAD binding; IEA:EnsemblFungi.
DR   GO; GO:0004502; F:kynurenine 3-monooxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR   GO; GO:0019674; P:NAD metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
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.
FT   CHAIN           1..506
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000410129"
FT   REGION          153..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   506 AA;  56479 MW;  521E763797746ADB CRC64;
     MSQSRARKVL IVGAGPVGAL TALSLHRRGW EVEVWETRDD PRGQDAAPSN LRSINLAISS
     RGLEALRSVD PSIAENFLEE AIPMKGRMIH HTDGKQESQL YDPIGGQSIN SISRPILNQR
     LVQSLPEAVK LRFNTKLKHI DFKNRVAYAS HKQETSLLPG EESEKDKKQN TEDEDGTAFD
     LVIGCDGSWS KVRTAMMRAE RIDFSQSFIP HAYIELHMPS DPASPGGYAM DKNHLHIWPR
     HAFMLIGLPN KDGSFTLTLF IPFSSLELLD TRESAAAFFR EHFPSAVDIV GEKVLLDDFE
     KNPRGNLVTI NCTPSAWSSH AILLGDASHS MVPFYGQGLN CGLEDVRVLS SILERHHISP
     TTTLALGETD PELELALKAY SDERQGDLKA ICELALQNYT EMRSHVLSPL HHLRRQVDKV
     FTTLFRSAPQ ATLSLMEPFP TKKVRGWTSL YEMVTFRPDV GYSEALRKER WQKDVVGYAG
     WIGGVVGVGA AGVFAATMAK KWLERR