KMO_HUMAN
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 03-AUG-2022, entry version 173.
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, 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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03018,
CC ECO:0000269|PubMed:10672018, 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 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 GlyGen; O15229; 1 site.
DR iPTMnet; O15229; -.
DR PhosphoSitePlus; O15229; -.
DR BioMuta; KMO; -.
DR jPOST; O15229; -.
DR MassIVE; O15229; -.
DR MaxQB; O15229; -.
DR PaxDb; O15229; -.
DR PeptideAtlas; O15229; -.
DR PRIDE; O15229; -.
DR ProteomicsDB; 48519; -. [O15229-1]
DR ProteomicsDB; 48520; -. [O15229-2]
DR ProteomicsDB; 48521; -. [O15229-3]
DR Antibodypedia; 34702; 200 antibodies from 31 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 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; 462247at2759; -.
DR PhylomeDB; O15229; -.
DR TreeFam; TF312990; -.
DR BioCyc; MetaCyc:HS04082-MON; -.
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; 10 hits in 1067 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 124 other tissues.
DR ExpressionAtlas; O15229; baseline and differential.
DR Genevisible; O15229; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
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; 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:0007568; P:aging; IEA:Ensembl.
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:1901216; P:positive regulation of neuron death; 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; -; 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 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 3-
FT 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 glycosylted. Reduces to 80% kynurenine 3-
FT 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
