ID   KMO_CYTH3               Reviewed;         449 AA.
AC   Q11PP7;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=CHU_3380;
OS   Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC
OS   15051 / NCIMB 9469 / D465).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Cytophaga.
OX   NCBI_TaxID=269798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465;
RX   PubMed=17400776; DOI=10.1128/aem.00225-07;
RA   Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P.,
RA   Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R.,
RA   Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B.,
RA   McBride M.J.;
RT   "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT   hutchinsonii.";
RL   Appl. Environ. Microbiol. 73:3536-3546(2007).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=14700627; DOI=10.1016/j.chembiol.2003.11.011;
RA   Kurnasov O., Goral V., Colabroy K., Gerdes S., Anantha S., Osterman A.,
RA   Begley T.P.;
RT   "NAD biosynthesis: identification of the tryptophan to quinolinate pathway
RT   in bacteria.";
RL   Chem. Biol. 10:1195-1204(2003).
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, ECO:0000269|PubMed:14700627}.
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         ECO:0000269|PubMed:14700627};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01971};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=76 uM for L-kynurenine {ECO:0000269|PubMed:14700627};
CC         KM=89 uM for NADPH {ECO:0000269|PubMed:14700627};
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; CP000383; ABG60616.1; -; Genomic_DNA.
DR   RefSeq; WP_011586724.1; NZ_FPJX01000012.1.
DR   AlphaFoldDB; Q11PP7; -.
DR   SMR; Q11PP7; -.
DR   STRING; 269798.CHU_3380; -.
DR   DNASU; 4187169; -.
DR   EnsemblBacteria; ABG60616; ABG60616; CHU_3380.
DR   KEGG; chu:CHU_3380; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_023210_0_1_10; -.
DR   OMA; REFMFIA; -.
DR   OrthoDB; 504558at2; -.
DR   BRENDA; 1.14.13.9; 7214.
DR   SABIO-RK; Q11PP7; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000001822; 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   1: Evidence at protein level;
KW   FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis; Reference proteome.
FT   CHAIN           1..449
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361935"
SQ   SEQUENCE   449 AA;  50783 MW;  87CAAAAF07A2BE16 CRC64;
     MKEQITICGA GLVGSLLAVY LIERGFSVRV FEKRKDPRKN EADAGRSINL AISHRGIHAL
     KDAQTGLEKE ALKLAVPMYG RAIHDLHGHV SFQAYGEASQ HINSIGRGAL NKLLITTAEN
     LGVHFLFEHT CTDYHAAGEQ WLFSDITGNT VATQSKEIVI GADGAFSIVR SFLSKQQQPQ
     PQIETLEYGY KELEIASAHT ETITNNQALH IWPRERFMLI ALPNEDGSYT ATLFLPLKGE
     ISFEALQSDQ DIQLFFKKYF PDTENLFPDL TEQFYRHPTS KLFTIHSSNW FNAHTLLIGD
     AAHALVPFYG QGMNAGFEDC RILAEIIDGK SKTNWSEIFA EFYNQRKENA DAISDLALQN
     FIEMRDHVAD ASFLLRKKIE KHLHQELEDA FIPQYTMVSF TDISYKEAME TGLLHQKILD
     EIMAIPDIEA AWPTEELKNK VITVTKKYI