ID   KMO_XANCB               Reviewed;         456 AA.
AC   B0RV00;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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};
GN   OrderedLocusNames=xcc-b100_2708;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM920689; CAP52069.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RV00; -.
DR   SMR; B0RV00; -.
DR   KEGG; xca:xcc-b100_2708; -.
DR   HOGENOM; CLU_023210_0_1_6; -.
DR   OMA; REFMFIA; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000001188; 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..456
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361949"
SQ   SEQUENCE   456 AA;  50991 MW;  C21CBEB6F04344EB CRC64;
     MSAAASPRSL TLIGAGLAGC LLAILLSRRG WQITLYERRG DPRIKGYESG RSINLALAER
     GRHALRQACA EDAVMAKAVM MRGRMIHPVS GEPQLQRYGR DDSEVIWSIH RAALNVTLLD
     LAEQAGARVH FYRRLHTVDF DAGYARFIDD RDDQPHEIHF QALVGSDGAG SALRAAMQRK
     APVGEHIAFL DHSYKELEIP PRADGGFRIE RNALHIWPRG RYMCIALPND GGTFTVTLFL
     PNEGMPSFAT TRSGDEALAL FARDFPDALP LIPQLKEHWE EHPPGLLGTL TRERWHLDGR
     AVLLGDAAHA MVPFHGQGMN CAFEDCVALA EQLDAHSDLS EAFAAFEAAR RDDAAAIQQM
     ALENYLEMRD RVGDAQFLLQ RALEQQLQAR WPTRFVPHYT MVTFLRTRYA IALARSEIQR
     EILLEATHGH TDLSRIDWVA LETVVHARLE PLEGAH