ID   KMO_CAEBR               Reviewed;         461 AA.
AC   A8Y432;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Kynurenine 3-monooxygenase {ECO:0000255|HAMAP-Rule:MF_03018};
DE            EC=1.14.13.9 {ECO:0000255|HAMAP-Rule:MF_03018};
DE   AltName: Full=Kynurenine 3-hydroxylase {ECO:0000255|HAMAP-Rule:MF_03018};
GN   Name=kmo-1 {ECO:0000255|HAMAP-Rule:MF_03018}; ORFNames=CBG23368;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(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_03018}.
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_03018};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03018};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03018}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03018}.
CC       Membrane {ECO:0000255|HAMAP-Rule:MF_03018}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03018}.
CC   -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03018}.
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DR   EMBL; HE601533; CAP39652.1; -; Genomic_DNA.
DR   RefSeq; XP_002636657.1; XM_002636611.1.
DR   AlphaFoldDB; A8Y432; -.
DR   SMR; A8Y432; -.
DR   STRING; 6238.CBG23368; -.
DR   PRIDE; A8Y432; -.
DR   EnsemblMetazoa; CBG23368.1; CBG23368.1; WBGene00041735.
DR   GeneID; 8578652; -.
DR   KEGG; cbr:CBG_23368; -.
DR   CTD; 8578652; -.
DR   WormBase; CBG23368; CBP05530; WBGene00041735; Cbr-kmo-1.
DR   eggNOG; KOG2614; Eukaryota.
DR   HOGENOM; CLU_023210_0_1_1; -.
DR   InParanoid; A8Y432; -.
DR   OMA; REFMFIA; -.
DR   OrthoDB; 462247at2759; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000008549; Chromosome V.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0004502; F:kynurenine 3-monooxygenase activity; ISS:UniProtKB.
DR   GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IBA:GO_Central.
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:0070189; P:kynurenine metabolic process; IBA:GO_Central.
DR   GO; GO:0019674; P:NAD metabolic process; ISS:UniProtKB.
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; Membrane; Mitochondrion; Monooxygenase; NADP;
KW   Oxidoreductase; Pyridine nucleotide biosynthesis; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..461
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361910"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT   TRANSMEM        432..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
SQ   SEQUENCE   461 AA;  52555 MW;  719D25F54A5B0B46 CRC64;
     MPSVAIAGAG LVGALNACFF AQKGWDVSVY EFRKDIRTMK HVQGRSINLA LSQRGKSALE
     AVGLKEYIVN QGVPLYARLV HNKDGKTYSR QPYGKPGEHI VSINRRHLNE VMITQAEKSP
     NVKFFFEHKV KSVDYDKKQL VVQCTSQPSR IPTFGTKSPP AEHEEFHVEA DLIIACDGAY
     SAVRRSLMTI PRFDFSQEYI EHGYVELNIM ANNNEFAFEE NVFHLWPRGH FTLIALANRD
     KTFTVTIFAP FTEFEKHMST TEEVLSFFEE NFPDAYLLLG KEHIADTFNR VKPQSLVSIK
     CSPHSFFNNL VLMGDAAHAM VPFYGQGMNC GFEDCLVFSE TLEEQNNDIA SAVQVYSERR
     VNDAHTINDL AMYNYEELKD LVNKNSYKLR KKFDGFMNAI FPKSWIPLYS MVTFTRIPYS
     EVVDRRRKQD RILSNLWKTT STLALIGAAI GIYSNRGRLG L