ID   KMO_DROWI               Reviewed;         455 AA.
AC   P0CU30; B4MPK3;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   25-MAY-2022, entry version 24.
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=cn {ECO:0000255|HAMAP-Rule:MF_03018}; ORFNames=GK21583;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(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_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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDW74042.1; Type=Erroneous gene model prediction; Note=The predicted gene GK21583 has been split into 2 genes: GK21583 and GK27737.; Evidence={ECO:0000305};
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; CH963849; EDW74042.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_015034226.1; XM_015178740.1.
DR   AlphaFoldDB; P0CU30; -.
DR   SMR; P0CU30; -.
DR   EnsemblMetazoa; FBtr0416149; FBpp0374346; FBgn0223575.
DR   GeneID; 6639967; -.
DR   KEGG; dwi:6639967; -.
DR   OrthoDB; 462247at2759; -.
DR   UniPathway; UPA00253; UER00328.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-UniRule.
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; Membrane; Mitochondrion; Monooxygenase; NADP;
KW   Oxidoreductase; Pyridine nucleotide biosynthesis; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..455
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000437790"
FT   TRANSMEM        393..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT   TRANSMEM        429..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
SQ   SEQUENCE   455 AA;  52329 MW;  27A3FD8607E56473 CRC64;
     MSVILTETNG SDERRKVAIV GAGLVGSLAA LYFARMGNQV DLYEYRDDVR KSELVQGRSI
     NLALSQRGRK ALSQLGLGLE EQVLSTAIPM KGRMLHNIQG KTSVVIYDPC FKQCLYSVGR
     KQLNELLLNA CDKFPNIKCH FDHKLTKANV KEGQLEFKRS HSVEGVKAKA DLIVGCDGAF
     SALRQNLIKL PGFNYTQEYI ETGYLELCIP AKKNEFQMPP NYLHIWPRDN FMMIALPNQD
     KSFTVTLSMP FDIFASIKNP EELIQFFTQY YPDALPLIGK EQLIKDFFKT KPQHLLSIKC
     RPYHYENKAL LLGDAAHAMV PYYGQGMNAG MEDVTLLNSL LQQLPLEEAL AQYTEQRWQD
     AFAICDLAMY NYVEMRDLTK RWSFRCRKML DTWLFRLFPT IWVPLYNSVS FTSMPYSKCI
     ANRKWQDQLL WRTFLGFIVV GLGVTGSAIY WQRFR