ID   KMO_FLAPJ               Reviewed;         447 AA.
AC   A6H1P4;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=FP2212;
OS   Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS   JIP02/86).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=402612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX   PubMed=17592475; DOI=10.1038/nbt1313;
RA   Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA   Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA   Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT   "Complete genome sequence of the fish pathogen Flavobacterium
RT   psychrophilum.";
RL   Nat. Biotechnol. 25:763-769(2007).
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; AM398681; CAL44268.1; -; Genomic_DNA.
DR   RefSeq; WP_011964302.1; NC_009613.3.
DR   RefSeq; YP_001297069.1; NC_009613.3.
DR   AlphaFoldDB; A6H1P4; -.
DR   SMR; A6H1P4; -.
DR   STRING; 402612.FP2212; -.
DR   EnsemblBacteria; CAL44268; CAL44268; FP2212.
DR   GeneID; 66553315; -.
DR   KEGG; fps:FP2212; -.
DR   PATRIC; fig|402612.5.peg.2259; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_023210_0_1_10; -.
DR   OMA; REFMFIA; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000006394; 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; Reference proteome.
FT   CHAIN           1..447
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361937"
SQ   SEQUENCE   447 AA;  51302 MW;  6792DA4BDCB6185A CRC64;
     MQKSQKIAIV GSGLVGSLLA IYLKKEGHTV HVYDRSPDIR TIQFSGRSIN LAMSNRGWNA
     LDGAGVGDKV RHIAIAMEKR AIHIGNQLNF QHYGLQGECI YSISRGVLNR KMIDLAEEAG
     AEFFFEQKIW DVNLTDATLQ MGETERGEWT NVSYDMVFGA DGAFSRIRHR MQRQSMFNYS
     QDFLNTGYKE LHIPANPDGS YKLDKHSLHI WPRGKYMLIA LPNLDGSFTC TLFMPFEGEN
     SFASLDNRQK VEAFFAENLP DTVDVIPDLA EDFFKNPTST LVTMKCFPWT YSDKVALIGD
     AAHAIVPFYG QGMNAGFEDI TILYQMMQEY GNDWKTIFSE YEKSRKPDAD AIAELSYRNF
     MEMSTKTANE KFLLQKKIER WFASKYPEKW IPLYDRVTFS TRPYSEALAI GDFQETIMQE
     ILKIENIETN WETEEIEHKI IQLLNSK