ID   KMO_XANOP               Reviewed;         455 AA.
AC   B2SIT6;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   25-MAY-2022, entry version 67.
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=PXO_00760;
OS   Xanthomonas oryzae pv. oryzae (strain PXO99A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=360094;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PXO99A;
RX   PubMed=18452608; DOI=10.1186/1471-2164-9-204;
RA   Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D.,
RA   Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R.,
RA   Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A.,
RA   Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R.,
RA   Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S.,
RA   Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E.,
RA   White F.F., Bogdanove A.J.;
RT   "Genome sequence and rapid evolution of the rice pathogen Xanthomonas
RT   oryzae pv. oryzae PXO99A.";
RL   BMC Genomics 9:204-204(2008).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACD58731.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000967; ACD58731.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; B2SIT6; -.
DR   SMR; B2SIT6; -.
DR   STRING; 360094.PXO_00760; -.
DR   EnsemblBacteria; ACD58731; ACD58731; PXO_00760.
DR   KEGG; xop:PXO_00760; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_023210_0_1_6; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000001740; 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..455
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361952"
SQ   SEQUENCE   455 AA;  51014 MW;  5FA4778CE64A75ED CRC64;
     MNPVSPRSLT MIGAGLAGCL LAILLSRRGW QITVYERRGD PRIKGYECGR SINLALAERG
     RHALRQAGAE EVVMAKAVMM 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