ID   KMO_MYXXD               Reviewed;         464 AA.
AC   Q1DDU6;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=MXAN_0916;
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA   Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA   Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA   Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF90126.1; -; Genomic_DNA.
DR   RefSeq; WP_011551037.1; NC_008095.1.
DR   AlphaFoldDB; Q1DDU6; -.
DR   SMR; Q1DDU6; -.
DR   STRING; 246197.MXAN_0916; -.
DR   EnsemblBacteria; ABF90126; ABF90126; MXAN_0916.
DR   GeneID; 41358375; -.
DR   KEGG; mxa:MXAN_0916; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_023210_0_1_7; -.
DR   OMA; REFMFIA; -.
DR   OrthoDB; 504558at2; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000002402; 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..464
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361941"
SQ   SEQUENCE   464 AA;  50920 MW;  F89635B2099C96B9 CRC64;
     MSEARKDTVT VVGAGLVGSL LSIYLARRGH TVELLERRPD MRRETVDGGR SINLAISTRG
     LHALRQVGLE NEALKHAIPM RGRMIHPPQG ELVYQPYGKD DSQHINAMSR GWLNAFLMTA
     AEATGKVRIR FKQRVTDVDF GSGALTVHDD ATGEARQEPG RVVFGTDGSA SAIRQALEKR
     PDFKGTQEQL GHGYKELTIP AGPGGAFQME KHALHIWPRG TFMLIALPDE EGSFTCTLFL
     PWQGPVSFAS LDTPAKLEAF FGAQFPDAKA LIPDLVEAFF SRPTGSMVTV KGAPWHAGGQ
     TLLLGDAAHA IVPFFGQGMN CGFEDCVVLD QLLGQGAGWE QVFTDFERLR KTNADAIADM
     AVENFVEMRD STGDPRFLFR KAVEKVLLNA FPGEFVSRYS LVSFSHVPYR LAYQMGALTD
     GIVSELSEGL PRAEDVDLKR AAELIRSRLT PFMKEHADGF RTEG