ID   KMO_HUMAN               Reviewed;         486 AA.
AC   O15229; A2A2U8; A2A2U9; A2A2V0; Q5SY07; Q5SY08; Q5SY09;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   27-MAR-2024, entry version 180.
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,
GN   ECO:0000312|HGNC:HGNC:6381};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAA73613.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND VARIANT CYS-452.
RC   TISSUE=Liver {ECO:0000312|EMBL:CAA73613.1};
RX   PubMed=9237672; DOI=10.1016/s0014-5793(97)00627-3;
RA   Alberati-Giani D., Cesura A.M., Broger C., Warren W.D., Rover S.,
RA   Malherbe P.;
RT   "Cloning and functional expression of human kynurenine 3-monooxygenase.";
RL   FEBS Lett. 410:407-412(1997).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAC62615.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANT CYS-452.
RC   TISSUE=Liver {ECO:0000269|PubMed:10672018};
RX   PubMed=10672018; DOI=10.1046/j.1432-1327.2000.01104.x;
RA   Breton J., Avanzi N., Magagnin S., Covini N., Magistrelli G., Cozzi L.,
RA   Isacchi A.;
RT   "Functional characterization and mechanism of action of recombinant human
RT   kynurenine 3-hydroxylase.";
RL   Eur. J. Biochem. 267:1092-1099(2000).
RN   [3] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4] {ECO:0000305}
RP   REVIEW.
RX   PubMed=12402501; DOI=10.1038/nrd870;
RA   Stone T.W., Darlington L.G.;
RT   "Endogenous kynurenines as targets for drug discovery and development.";
RL   Nat. Rev. Drug Discov. 1:609-620(2002).
RN   [5]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=23575632; DOI=10.1038/nature12039;
RA   Amaral M., Levy C., Heyes D.J., Lafite P., Outeiro T.F., Giorgini F.,
RA   Leys D., Scrutton N.S.;
RT   "Structural basis of kynurenine 3-monooxygenase inhibition.";
RL   Nature 496:382-385(2013).
RN   [6]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=26752518; DOI=10.1038/nm.4020;
RA   Mole D.J., Webster S.P., Uings I., Zheng X., Binnie M., Wilson K.,
RA   Hutchinson J.P., Mirguet O., Walker A., Beaufils B., Ancellin N.,
RA   Trottet L., Beneton V., Mowat C.G., Wilkinson M., Rowland P., Haslam C.,
RA   McBride A., Homer N.Z., Baily J.E., Sharp M.G., Garden O.J., Hughes J.,
RA   Howie S.E., Holmes D.S., Liddle J., Iredale J.P.;
RT   "Kynurenine-3-monooxygenase inhibition prevents multiple organ failure in
RT   rodent models of acute pancreatitis.";
RL   Nat. Med. 22:202-209(2016).
RN   [7]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX   PubMed=28604669; DOI=10.1038/ncomms15827;
RA   Hutchinson J.P., Rowland P., Taylor M.R.D., Christodoulou E.M., Haslam C.,
RA   Hobbs C.I., Holmes D.S., Homes P., Liddle J., Mole D.J., Uings I.,
RA   Walker A.L., Webster S.P., Mowat C.G., Chung C.W.;
RT   "Structural and mechanistic basis of differentiated inhibitors of the acute
RT   pancreatitis target kynurenine-3-monooxygenase.";
RL   Nat. Commun. 8:15827-15827(2017).
RN   [8]
RP   FUNCTION, DOMAIN, GLYCOSYLATION AT ASN-465, AND MUTAGENESIS OF ARG-85;
RP   TYR-99; ASN-363; GLU-366; MET-367; TYR-398 AND ASN-465.
RX   PubMed=29208702; DOI=10.1096/fj.201700397rr;
RA   Gao J., Yao L., Xia T., Liao X., Zhu D., Xiang Y.;
RT   "Biochemistry and structural studies of kynurenine 3-monooxygenase reveal
RT   allosteric inhibition by Ro 61-8048.";
RL   FASEB J. 32:2036-2045(2018).
RN   [9] {ECO:0007744|PDB:5X68}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-374 IN COMPLEX WITH FAD,
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, GLYCOSYLATION AT ASN-465, AND
RP   MUTAGENESIS OF 312-PHE-PHE-313; PHE-312 AND PHE-313.
RX   PubMed=29429898; DOI=10.1016/j.chembiol.2018.01.008;
RA   Kim H.T., Na B.K., Chung J., Kim S., Kwon S.K., Cha H., Son J., Cho J.M.,
RA   Hwang K.Y.;
RT   "Structural Basis for Inhibitor-Induced Hydrogen Peroxide Production by
RT   Kynurenine 3-Monooxygenase.";
RL   Cell Chem. Biol. 0:0-0(2018).
CC   -!- FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form
CC       3-hydroxy-L-kynurenine (L-3OHKyn) (PubMed:29429898, PubMed:23575632,
CC       PubMed:26752518, PubMed:28604669, PubMed:29208702). Required for
CC       synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and
CC       potential endogenous inhibitor of NMDA receptor signaling in axonal
CC       targeting, synaptogenesis and apoptosis during brain development.
CC       Quinolinic acid may also affect NMDA receptor signaling in pancreatic
CC       beta cells, osteoblasts, myocardial cells, and the gastrointestinal
CC       tract (Probable). {ECO:0000269|PubMed:23575632,
CC       ECO:0000269|PubMed:26752518, ECO:0000269|PubMed:28604669,
CC       ECO:0000269|PubMed:29208702, ECO:0000269|PubMed:29429898,
CC       ECO:0000305|PubMed:12402501}.
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         ECO:0000269|PubMed:10672018, ECO:0000269|PubMed:29429898,
CC         ECO:0000269|PubMed:9237672};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03018, ECO:0000269|PubMed:10672018,
CC         ECO:0000269|PubMed:29429898};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=24.1 uM for L-kynurenine {ECO:0000269|PubMed:10672018,
CC         ECO:0000269|PubMed:23575632, ECO:0000269|PubMed:9237672};
CC         KM=2 uM for L-kynurenine {ECO:0000269|PubMed:26752518};
CC         KM=78 uM for L-kynurenine {ECO:0000269|PubMed:26752518};
CC         Vmax=8.5 umol/min/mg enzyme {ECO:0000269|PubMed:10672018,
CC         ECO:0000269|PubMed:9237672};
CC         Note=kcat is 0.24 sec(-1) for L-kynurenine.
CC         {ECO:0000269|PubMed:28604669};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:10672018,
CC         ECO:0000269|PubMed:9237672};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03018}.
CC   -!- INTERACTION:
CC       O15229-2; P42858: HTT; NbExp=3; IntAct=EBI-21870540, EBI-466029;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03018, ECO:0000269|PubMed:9237672}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:9237672}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|PubMed:10672018, ECO:0000269|PubMed:9237672};
CC         IsoId=O15229-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:16710414};
CC         IsoId=O15229-2; Sequence=VSP_051973;
CC       Name=3 {ECO:0000269|PubMed:16710414};
CC         IsoId=O15229-3; Sequence=VSP_051972;
CC   -!- TISSUE SPECIFICITY: Highest levels in placenta and liver. Detectable in
CC       kidney. {ECO:0000269|PubMed:9237672}.
CC   -!- DOMAIN: Transmembrane domains are required for enzymatic activity.
CC       {ECO:0000269|PubMed:29208702, ECO:0000269|PubMed:29429898}.
CC   -!- MISCELLANEOUS: Increased in neuroinflammatory conditions. Inhibitors
CC       are investigated as potential neuroprotective drugs since they lead to
CC       an increased level of kynurenic acid, a neuroprotective NMDA receptor
CC       agonist. {ECO:0000269|PubMed:9237672}.
CC   -!- MISCELLANEOUS: [Isoform 3]: Gene model based on mouse cDNA data.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03018}.
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DR   EMBL; Y13153; CAA73613.1; -; mRNA.
DR   EMBL; AF056032; AAC62615.1; -; mRNA.
DR   EMBL; AL133390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; FO393423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS1618.1; -. [O15229-1]
DR   CCDS; CCDS91182.1; -. [O15229-2]
DR   RefSeq; NP_003670.2; NM_003679.4. [O15229-1]
DR   PDB; 5X68; X-ray; 2.10 A; A/B=1-374.
DR   PDBsum; 5X68; -.
DR   AlphaFoldDB; O15229; -.
DR   SMR; O15229; -.
DR   BioGRID; 114133; 8.
DR   IntAct; O15229; 4.
DR   MINT; O15229; -.
DR   STRING; 9606.ENSP00000355517; -.
DR   BindingDB; O15229; -.
DR   ChEMBL; CHEMBL2145; -.
DR   GuidetoPHARMACOLOGY; 2886; -.
DR   GlyCosmos; O15229; 1 site, No reported glycans.
DR   GlyGen; O15229; 1 site.
DR   iPTMnet; O15229; -.
DR   PhosphoSitePlus; O15229; -.
DR   BioMuta; KMO; -.
DR   jPOST; O15229; -.
DR   MassIVE; O15229; -.
DR   MaxQB; O15229; -.
DR   PaxDb; 9606-ENSP00000355517; -.
DR   PeptideAtlas; O15229; -.
DR   ProteomicsDB; 48519; -. [O15229-1]
DR   ProteomicsDB; 48520; -. [O15229-2]
DR   ProteomicsDB; 48521; -. [O15229-3]
DR   Antibodypedia; 34702; 231 antibodies from 32 providers.
DR   DNASU; 8564; -.
DR   Ensembl; ENST00000366557.8; ENSP00000355515.4; ENSG00000117009.12. [O15229-3]
DR   Ensembl; ENST00000366558.7; ENSP00000355516.3; ENSG00000117009.12. [O15229-2]
DR   Ensembl; ENST00000366559.9; ENSP00000355517.4; ENSG00000117009.12. [O15229-1]
DR   GeneID; 8564; -.
DR   KEGG; hsa:8564; -.
DR   MANE-Select; ENST00000366559.9; ENSP00000355517.4; NM_003679.5; NP_003670.2.
DR   UCSC; uc001hyy.4; human. [O15229-1]
DR   AGR; HGNC:6381; -.
DR   CTD; 8564; -.
DR   DisGeNET; 8564; -.
DR   GeneCards; KMO; -.
DR   HGNC; HGNC:6381; KMO.
DR   HPA; ENSG00000117009; Group enriched (kidney, liver).
DR   MIM; 603538; gene.
DR   neXtProt; NX_O15229; -.
DR   OpenTargets; ENSG00000117009; -.
DR   PharmGKB; PA30172; -.
DR   VEuPathDB; HostDB:ENSG00000117009; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   GeneTree; ENSGT00390000000747; -.
DR   HOGENOM; CLU_023210_0_0_1; -.
DR   InParanoid; O15229; -.
DR   OMA; REFMFIA; -.
DR   OrthoDB; 2250465at2759; -.
DR   PhylomeDB; O15229; -.
DR   TreeFam; TF312990; -.
DR   BioCyc; MetaCyc:HS04082-MONOMER; -.
DR   BRENDA; 1.14.13.9; 2681.
DR   PathwayCommons; O15229; -.
DR   Reactome; R-HSA-71240; Tryptophan catabolism.
DR   SABIO-RK; O15229; -.
DR   SignaLink; O15229; -.
DR   UniPathway; UPA00253; UER00328.
DR   BioGRID-ORCS; 8564; 11 hits in 1148 CRISPR screens.
DR   ChiTaRS; KMO; human.
DR   GeneWiki; KMO_(gene); -.
DR   GenomeRNAi; 8564; -.
DR   Pharos; O15229; Tchem.
DR   PRO; PR:O15229; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O15229; Protein.
DR   Bgee; ENSG00000117009; Expressed in right lobe of liver and 125 other cell types or tissues.
DR   ExpressionAtlas; O15229; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR   GO; GO:0004502; F:kynurenine 3-monooxygenase activity; IDA:UniProtKB.
DR   GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IDA:UniProtKB.
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:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0034276; P:kynurenic acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0070189; P:kynurenine metabolic process; IDA:UniProtKB.
DR   GO; GO:0097052; P:L-kynurenine metabolic process; IEA:Ensembl.
DR   GO; GO:0019674; P:NAD metabolic process; IDA:UniProtKB.
DR   GO; GO:1903296; P:positive regulation of glutamate secretion, neurotransmission; IEA:Ensembl.
DR   GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009651; P:response to salt stress; IDA:UniProtKB.
DR   GO; GO:0006569; P:tryptophan catabolic process; TAS:Reactome.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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   PANTHER; PTHR46028; KYNURENINE 3-MONOOXYGENASE; 1.
DR   PANTHER; PTHR46028:SF2; KYNURENINE 3-MONOOXYGENASE; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   Genevisible; O15229; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; FAD; Flavoprotein; Glycoprotein;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Monooxygenase; NADP;
KW   Oxidoreductase; Pyridine nucleotide biosynthesis; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..486
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000229742"
FT   TRANSMEM        385..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03018"
FT   BINDING         19
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:29429898,
FT                   ECO:0007744|PDB:5X68"
FT   BINDING         37..40
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:29429898,
FT                   ECO:0007744|PDB:5X68"
FT   BINDING         57
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:29429898,
FT                   ECO:0007744|PDB:5X68"
FT   BINDING         85
FT                   /ligand="L-kynurenine"
FT                   /ligand_id="ChEBI:CHEBI:57959"
FT                   /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT   BINDING         99
FT                   /ligand="L-kynurenine"
FT                   /ligand_id="ChEBI:CHEBI:57959"
FT                   /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT   BINDING         111
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:29429898,
FT                   ECO:0007744|PDB:5X68"
FT   BINDING         136
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:29429898,
FT                   ECO:0007744|PDB:5X68"
FT   BINDING         172
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:29429898,
FT                   ECO:0007744|PDB:5X68"
FT   BINDING         304
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:29429898,
FT                   ECO:0007744|PDB:5X68"
FT   BINDING         317..318
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:29429898,
FT                   ECO:0007744|PDB:5X68"
FT   BINDING         363
FT                   /ligand="L-kynurenine"
FT                   /ligand_id="ChEBI:CHEBI:57959"
FT                   /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT   BINDING         398
FT                   /ligand="L-kynurenine"
FT                   /ligand_id="ChEBI:CHEBI:57959"
FT                   /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT   CARBOHYD        465
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:29429898"
FT   VAR_SEQ         367..400
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16710414"
FT                   /id="VSP_051972"
FT   VAR_SEQ         367..379
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16710414"
FT                   /id="VSP_051973"
FT   VARIANT         452
FT                   /note="R -> C (in dbSNP:rs1053230)"
FT                   /evidence="ECO:0000269|PubMed:10672018,
FT                   ECO:0000269|PubMed:9237672"
FT                   /id="VAR_030845"
FT   MUTAGEN         85
FT                   /note="R->A,K: Abolishes kynurenine 3-monooxygenase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:29208702"
FT   MUTAGEN         99
FT                   /note="Y->A: Abolishes kynurenine 3-monooxygenase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:29208702"
FT   MUTAGEN         99
FT                   /note="Y->F: Strongly decreases kynurenine 3-monooxygenase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:29208702"
FT   MUTAGEN         312..313
FT                   /note="FF->AA: Abolishes NADPH oxidase activity."
FT                   /evidence="ECO:0000269|PubMed:29429898"
FT   MUTAGEN         312
FT                   /note="F->A: Decreases to 30% NADPH oxidase activity."
FT                   /evidence="ECO:0000269|PubMed:29429898"
FT   MUTAGEN         313
FT                   /note="F->A: Decreases to 50% NADPH oxidase activity."
FT                   /evidence="ECO:0000269|PubMed:29429898"
FT   MUTAGEN         363
FT                   /note="N->A: Strongly decreases kynurenine 3-monooxygenase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:29208702"
FT   MUTAGEN         363
FT                   /note="N->D: Abolishes kynurenine 3-monooxygenase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:29208702"
FT   MUTAGEN         366
FT                   /note="E->A,Q: Strongly decreases kynurenine
FT                   3-monooxygenase activity."
FT                   /evidence="ECO:0000269|PubMed:29208702"
FT   MUTAGEN         367
FT                   /note="M->A: Strongly decreases kynurenine 3-monooxygenase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:29208702"
FT   MUTAGEN         367
FT                   /note="M->L: Strongly decreases kynurenine 3-monooxygenase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:29208702"
FT   MUTAGEN         398
FT                   /note="Y->A,F: Abolishes kynurenine 3-monooxygenase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:29208702"
FT   MUTAGEN         465
FT                   /note="N->A: Not glycosylated. Reduces to 80% kynurenine
FT                   3-monooxygenase activity."
FT                   /evidence="ECO:0000269|PubMed:29208702"
FT   STRAND          10..14
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   HELIX           18..28
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   TURN            29..31
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          33..37
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   TURN            43..45
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          55..58
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   HELIX           60..68
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   HELIX           72..76
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          94..98
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   HELIX           102..104
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   HELIX           111..123
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          128..131
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   TURN            141..144
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          145..148
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          156..159
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          161..165
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   HELIX           172..177
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          189..199
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          202..205
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          212..217
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          222..227
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          233..240
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   HELIX           241..244
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   HELIX           250..260
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   HELIX           264..268
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   HELIX           270..277
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          283..286
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          288..290
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          293..295
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   TURN            296..298
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          299..301
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   HELIX           303..305
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   TURN            311..313
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   HELIX           316..333
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   TURN            334..336
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   HELIX           338..349
FT                   /evidence="ECO:0007829|PDB:5X68"
FT   STRAND          363..365
FT                   /evidence="ECO:0007829|PDB:5X68"
SQ   SEQUENCE   486 AA;  55810 MW;  164870D52E62A08A CRC64;
     MDSSVIQRKK VAVIGGGLVG SLQACFLAKR NFQIDVYEAR EDTRVATFTR GRSINLALSH
     RGRQALKAVG LEDQIVSQGI PMRARMIHSL SGKKSAIPYG TKSQYILSVS RENLNKDLLT
     AAEKYPNVKM HFNHRLLKCN PEEGMITVLG SDKVPKDVTC DLIVGCDGAY STVRSHLMKK
     PRFDYSQQYI PHGYMELTIP PKNGDYAMEP NYLHIWPRNT FMMIALPNMN KSFTCTLFMP
     FEEFEKLLTS NDVVDFFQKY FPDAIPLIGE KLLVQDFFLL PAQPMISVKC SSFHFKSHCV
     LLGDAAHAIV PFFGQGMNAG FEDCLVFDEL MDKFSNDLSL CLPVFSRLRI PDDHAISDLS
     MYNYIEMRAH VNSSWFIFQK NMERFLHAIM PSTFIPLYTM VTFSRIRYHE AVQRWHWQKK
     VINKGLFFLG SLIAISSTYL LIHYMSPRSF LRLRRPWNWI AHFRNTTCFP AKAVDSLEQI
     SNLISR
//