ID   KMO_XANC8               Reviewed;         456 AA.
AC   Q4UT92;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=XC_2682;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8004;
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA   Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA   Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(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; CP000050; AAY49731.1; -; Genomic_DNA.
DR   RefSeq; WP_011036736.1; NC_007086.1.
DR   AlphaFoldDB; Q4UT92; -.
DR   SMR; Q4UT92; -.
DR   EnsemblBacteria; AAY49731; AAY49731; XC_2682.
DR   KEGG; xcb:XC_2682; -.
DR   HOGENOM; CLU_023210_0_1_6; -.
DR   OMA; SVWAIFD; -.
DR   OrthoDB; 504558at2; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000000420; Chromosome.
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..456
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361948"
SQ   SEQUENCE   456 AA;  50945 MW;  265B933209C490EA CRC64;
     MSAAASPRSL TLIGAGLAGC LLAILLSRRG WQITLYERRG DPRIKGYESG RSINLALAER
     GRHALRQAGA EDAVMAKAVM MRGRMIHPVS GEPQLQRYGR DDSEVIWSIH RAALNVTLLD
     LAEQAGARVH FYRRLHTVDF DAGYARFIDD RDDQPHEIHF QALVGSDGAG SALRAAMQRK
     APVGEHIAFL DHSYKELEIP PRADGGFRIE RNALHIWPRG RYMCIALPND GGTFTVTLFL
     PNEGMPSFAT TRSGDEALAL FARDFPDALP LIPQLKEHWE EHPPGLLGTL TRERWHLDGR
     AVLLGDAAHA MVPFHGQGMN CAFEDCVALA EQLDAHSDLS EAFAAFEAAR RDDAAAIQQM
     ALENYLEMRD RVGDAQFLLQ RALEQQLQAR WPTRFVPHYT MVTFLRTRYA IALARSEIQR
     EILLEATHGH TDLSRIDWVA LETVVHARLE PLEGAH