ID   KMO_DANRE               Reviewed;         474 AA.
AC   Q1RLY6;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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 {ECO:0000255|HAMAP-Rule:MF_03018}; ORFNames=zgc:136684;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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 outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03018}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       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; BC115227; AAI15228.1; -; mRNA.
DR   AlphaFoldDB; Q1RLY6; -.
DR   SMR; Q1RLY6; -.
DR   STRING; 7955.ENSDARP00000024051; -.
DR   PaxDb; Q1RLY6; -.
DR   ZFIN; ZDB-GENE-030424-4; kmo.
DR   eggNOG; KOG2614; Eukaryota.
DR   InParanoid; Q1RLY6; -.
DR   PhylomeDB; Q1RLY6; -.
DR   Reactome; R-DRE-71240; Tryptophan catabolism.
DR   UniPathway; UPA00253; UER00328.
DR   PRO; PR:Q1RLY6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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:0072015; P:podocyte development; IMP:ZFIN.
DR   GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0001878; P:response to yeast; IDA:ZFIN.
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   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Monooxygenase; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..474
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000361909"
FT   TRANSMEM        393..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT   TRANSMEM        433..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
SQ   SEQUENCE   474 AA;  54247 MW;  4BBC8BA0F664BA61 CRC64;
     METAFSHPPQ SSSSKRKVIA VVGGGLVGSL NACFLAKRGF DVEVYESRED IRQAKVVKGR
     SINLALSHRG RQALKHVGME DKIISKGIPM HARMIHNVNG KRSPIPYGKK GQYILSVDRA
     NLNKELLTAA EAYPNTRLNF NHKLHDWSPK TGTMTFIGSD GQKTETQADL IVGCDGAFSA
     VRKQFLRQSR FNYSQTYIPH GYMELTMPPK DGDFAMEPNY LHIWPRNTFM MIALPNLDRT
     FTCTLFMPFE DFEKIRTGDE LLRFFHKYFP DSVPLIGVEA LKQDFFRLPA QAMVSVKCCP
     YHLFEKCVLM GDAAHAVVPF YGQGMNAGFE DCLVFDEIMD QFNENLVAVL QEYTRVRVPD
     DHAIADLAMY NYIEMRAHVN SKYFIFRKYL DNLLHFFMPK TIVPLYTMVT FTRTRYNDAV
     NRWHWQNKVI TRGLWLCGFV SAAGGTYVLV KNSHKLPSIS AEQLWTRILA LKLF