ID   KMO_SALTO               Reviewed;         453 AA.
AC   A4XD40;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Strop_4419;
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=369723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(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; CP000667; ABP56847.1; -; Genomic_DNA.
DR   RefSeq; WP_012015611.1; NC_009380.1.
DR   AlphaFoldDB; A4XD40; -.
DR   SMR; A4XD40; -.
DR   STRING; 369723.Strop_4419; -.
DR   EnsemblBacteria; ABP56847; ABP56847; Strop_4419.
DR   KEGG; stp:Strop_4419; -.
DR   PATRIC; fig|369723.5.peg.4570; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_023210_0_1_11; -.
DR   OMA; EALHVWP; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000000235; 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..453
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361944"
SQ   SEQUENCE   453 AA;  49803 MW;  53AF035F34109243 CRC64;
     MNRRRERVVV VGAGLAGSLV ALYLARQGHE VDVFERRPDP RSALGRPEGR SINLGLSARG
     MRALDGVGLL ADVLKHSVPM RDRVVHSPDG GIRTQPYGVR EHEILHSVLR EELISLVVTA
     AEAEPGVRFH FDSLLASLDR ETGTVDVAPT AGGETRTVTA DLIVGADGAF STIRQQMQHG
     LRANYAQEFL PWGYKELTIP VDADGQPRVR LEALHVWPGH EAMMIAHPNR DGSLTCTLFM
     AHEGPVSFAA LDTPTAVRDF FRQRFPDAEE LMPDLVREVT EHPVGHLVTV RSDPWRYADR
     VVLIGDAAHA VYPFYGQGMN SAFEDCVVLD ECLTAHPDRA TALAAYEAAR KPHTDVLADL
     STANFEDLRD RVHRLGYSAS AAADRLLARL LPQHWVPLYG MVAHTTIPYA DALARAKRQD
     RILRQAGAGL ALVTVLAATA ALRAGRRRRA NRR