ID   KMO_LEGPL               Reviewed;         449 AA.
AC   Q5WY16;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, 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=lpl0923;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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; CR628337; CAH15157.1; -; Genomic_DNA.
DR   RefSeq; WP_011215067.1; NC_006369.1.
DR   AlphaFoldDB; Q5WY16; -.
DR   SMR; Q5WY16; -.
DR   PRIDE; Q5WY16; -.
DR   EnsemblBacteria; CAH15157; CAH15157; lpl0923.
DR   KEGG; lpf:lpl0923; -.
DR   LegioList; lpl0923; -.
DR   HOGENOM; CLU_023210_0_1_6; -.
DR   OMA; REFMFIA; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000002517; 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..449
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361940"
SQ   SEQUENCE   449 AA;  51334 MW;  BFF51B7443F9E38B CRC64;
     MKHITIIGAG LAGTLCGLYL ARRGYEVELF ESRPDIRNSP TDYGRSINLA LSCRGITALK
     AMNLLSEVNK IMVPMRARAI HEANGEIHYQ PFGRHIDEYI NAISRSDLNA LLLNKAKLCP
     NIKLHFNMKL HSLDIHNKKI KFENKNGDFV EASYHRLIGA DGAPSHVRDM LKNEGIVSAS
     RDFLSHGYKE LSISKKHTKG MAREHLHLWP RDSFMLLGNP NPDDSITGSL FLANEGKDSF
     AELNNEEKLH LFFKTQFPDA YAAMPNLVQE FFGNPTGHLS TIQCSPWYYK DECLLIGDAA
     HGIIPFFGQG MNSAFEDCRI LDELLDEYQD DWSRVNSVFY EHRKVNTDAI AKMSMDNYHE
     IHSDIRNPKF ILQKQIEREL MLRYPEHYVS MHVLVMFTNT PYAKAMAIGE LQSGLLEQIC
     FPITDIKELN WQEVEKLLSL YDKKLAKII