ID   KMO_XANOM               Reviewed;         455 AA.
AC   Q2P316;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Kynurenine 3-monooxygenase {ECO:0000255|HAMAP-Rule:MF_01971};
DE            EC=1.14.13.9 {ECO:0000255|HAMAP-Rule:MF_01971};
DE   AltName: Full=Kynurenine 3-hydroxylase {ECO:0000255|HAMAP-Rule:MF_01971};
GN   Name=kmo {ECO:0000255|HAMAP-Rule:MF_01971}; OrderedLocusNames=XOO2306;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(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_01971}.
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_01971};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01971};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_01971}.
CC   -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01971}.
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DR   EMBL; AP008229; BAE69061.1; -; Genomic_DNA.
DR   RefSeq; WP_011408607.1; NC_007705.1.
DR   AlphaFoldDB; Q2P316; -.
DR   SMR; Q2P316; -.
DR   KEGG; xom:XOO2306; -.
DR   HOGENOM; CLU_023210_0_1_6; -.
DR   OMA; REFMFIA; -.
DR   UniPathway; UPA00253; UER00328.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004502; F:kynurenine 3-monooxygenase activity; IEA:UniProtKB-UniRule.
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   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; Monooxygenase; NADP; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis.
FT   CHAIN           1..455
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361951"
SQ   SEQUENCE   455 AA;  50983 MW;  CC8AE451A359FC4B CRC64;
     MSPVSPRSLT LIGAGLAGCL LAILLSRRGW QITVYERRGD PRIKGYECGR SINLALAERG
     RHALRQAGAE ELVMAKAVMM RGRMVHPLVG EPQLQRYGRD DSEVIWSIHR AALNVALLDL
     AEQAGARVHF YRRLHTVDFD AGYARFIDDR DDQPHEIHFQ SLIGSDGAGS ALRAAMQRKS
     PLGERTEFLD HSYKELEIPP LPGGGFRIEG NALHIWPRGR YMFIALPNDG GTFTVTLFLP
     NAGEPSFATT RNGDEAFALF ARDFPDALPL IPQLKQHWEE HPPGLLGTLT LDRWHLDGRA
     LLIGDAAHAM VPFHGQGMNC AFEDCVALAD QLDAHDDLAS AFAAFEAARR DDAGAIQQMA
     LENYLEMRDR VDDPEFLLQR QLEQQLQARW PTRFVPHYTM VTFLRTRYSI ALARSEIQRE
     ILVEATRGHS DLSRLDWAAL ETIVHARLEP LDGAH