KMO_PSEFL
ID KMO_PSEFL Reviewed; 461 AA.
AC Q84HF5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Kynurenine 3-monooxygenase {ECO:0000255|HAMAP-Rule:MF_01971};
DE Short=PfKMO;
DE EC=1.14.13.9 {ECO:0000255|HAMAP-Rule:MF_01971};
DE AltName: Full=Kynurenine 3-hydroxylase {ECO:0000255|HAMAP-Rule:MF_01971};
GN Name=kmo {ECO:0000255|HAMAP-Rule:MF_01971}; Synonyms=qbsG;
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROBABLE FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 17400;
RX PubMed=15066027; DOI=10.1111/j.1365-2958.2004.03999.x;
RA Matthijs S., Baysse C., Koedam N., Tehrani K.A., Verheyden L.,
RA Budzikiewicz H., Schaefer M., Hoorelbeke B., Meyer J.-M., De Greve H.,
RA Cornelis P.;
RT "The Pseudomonas siderophore quinolobactin is synthesized from xanthurenic
RT acid, an intermediate of the kynurenine pathway.";
RL Mol. Microbiol. 52:371-384(2004).
RN [2]
RP CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=17400;
RX PubMed=16973376; DOI=10.1016/j.pep.2006.07.024;
RA Crozier K.R., Moran G.R.;
RT "Heterologous expression and purification of kynurenine-3-monooxygenase
RT from Pseudomonas fluorescens strain 17400.";
RL Protein Expr. Purif. 51:324-333(2007).
RN [3] {ECO:0007744|PDB:5FN0}
RP X-RAY CRYSTALLOGRAPHY (3.19 ANGSTROMS) IN COMPLEX WITH FAD AND INHIBITOR.
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 [4] {ECO:0007744|PDB:5N7T}
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS)IN COMPLEX WITH FAD AND INHIBITOR.
RX PubMed=28336141; DOI=10.1016/j.bmcl.2017.02.078;
RA Liddle J., Beaufils B., Binnie M., Bouillot A., Denis A.A., Hann M.M.,
RA Haslam C.P., Holmes D.S., Hutchinson J.P., Kranz M., McBride A.,
RA Mirguet O., Mole D.J., Mowat C.G., Pal S., Rowland P., Trottet L.,
RA Uings I.J., Walker A.L., Webster S.P.;
RT "The discovery of potent and selective kynurenine 3-monooxygenase
RT inhibitors for the treatment of acute pancreatitis.";
RL Bioorg. Med. Chem. Lett. 27:2023-2028(2017).
RN [5] {ECO:0007744|PDB:5MZC, ECO:0007744|PDB:5MZI, ECO:0007744|PDB:5MZK}
RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH FAD AND INHIBITOR.
RX PubMed=28398044; DOI=10.1021/acs.jmedchem.7b00055;
RA Walker A.L., Ancellin N., Beaufils B., Bergeal M., Binnie M., Bouillot A.,
RA Clapham D., Denis A., Haslam C.P., Holmes D.S., Hutchinson J.P., Liddle J.,
RA McBride A., Mirguet O., Mowat C.G., Rowland P., Tiberghien N., Trottet L.,
RA Uings I., Webster S.P., Zheng X., Mole D.J.;
RT "Development of a Series of Kynurenine 3-Monooxygenase Inhibitors Leading
RT to a Clinical Candidate for the Treatment of Acute Pancreatitis.";
RL J. Med. Chem. 60:3383-3404(2017).
RN [6] {ECO:0007744|PDB:5NA5, ECO:0007744|PDB:5NAB, ECO:0007744|PDB:5NAE, ECO:0007744|PDB:5NAG, ECO:0007744|PDB:5NAH, ECO:0007744|PDB:5NAK}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH FAD AND INHIBITORS,
RP COFACTOR, CATALYTIC ACTIVITY, 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 [7] {ECO:0007744|PDB:5X6P, ECO:0007744|PDB:5X6Q}
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH FAD AND INHIBITOR,
RP CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF 319-PHE-HIS-320 AND
RP HIS-320.
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).
RN [8] {ECO:0007744|PDB:5Y66, ECO:0007744|PDB:5Y77, ECO:0007744|PDB:5Y7A}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-461 IN COMPLEX WITH FAD;
RP L-KYNURENINE AND INHIBITOR, FUNCTION, MUTAGENESIS OF ARG-84; TYR-98;
RP ASN-369; GLU-372; MET-373 AND TYR-404, AND COFACTOR.
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).
CC -!- FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form
CC 3-hydroxy-L-kynurenine (L-3OHKyn). Probably required for the synthesis
CC of quinolinic acid and the siderophore quinolobactin.
CC {ECO:0000269|PubMed:28604669, ECO:0000269|PubMed:29208702}.
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_01971,
CC ECO:0000269|PubMed:16973376, ECO:0000269|PubMed:28604669,
CC ECO:0000269|PubMed:29429898};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01971,
CC ECO:0000269|PubMed:16973376, ECO:0000269|PubMed:28604669,
CC ECO:0000269|PubMed:29429898};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.8 uM for L-kynurenine (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:16973376};
CC KM=7 uM for L-kynurenine {ECO:0000269|PubMed:28604669};
CC KM=8.5 uM for NADPH (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:16973376};
CC KM=34.2 uM for oxygen (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:16973376};
CC Note=kcat is 2.3 sec(-1) for L-kynurenine.
CC {ECO:0000269|PubMed:28604669};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:16973376};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC L-kynurenine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_01971,
CC ECO:0000269|PubMed:15066027}.
CC -!- PATHWAY: Siderophore biosynthesis; quinolobactin biosynthesis.
CC {ECO:0000269|PubMed:15066027}.
CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01971}.
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DR EMBL; AY271621; AAL65289.1; -; Genomic_DNA.
DR RefSeq; WP_029293793.1; NZ_JENC01000007.1.
DR PDB; 5FN0; X-ray; 3.19 A; A/B/C/D=1-460.
DR PDB; 5MZC; X-ray; 1.82 A; A/B=1-461.
DR PDB; 5MZI; X-ray; 1.71 A; A/B=1-461.
DR PDB; 5MZK; X-ray; 1.82 A; A/B=1-461.
DR PDB; 5N7T; X-ray; 1.81 A; A/B=1-461.
DR PDB; 5NA5; X-ray; 1.94 A; A/B=1-461.
DR PDB; 5NAB; X-ray; 1.63 A; A/B=1-461.
DR PDB; 5NAE; X-ray; 1.76 A; A/B=1-461.
DR PDB; 5NAG; X-ray; 1.68 A; A/B=1-461.
DR PDB; 5NAH; X-ray; 1.75 A; A/B=1-461.
DR PDB; 5NAK; X-ray; 1.50 A; A/B=1-461.
DR PDB; 5X6P; X-ray; 1.78 A; A/B=1-461.
DR PDB; 5X6Q; X-ray; 1.90 A; A=1-461.
DR PDB; 5Y66; X-ray; 2.34 A; A=2-461.
DR PDB; 5Y77; X-ray; 1.60 A; A/B=2-461.
DR PDB; 5Y7A; X-ray; 1.85 A; A=2-461.
DR PDB; 6FOX; X-ray; 1.90 A; A/B=2-460.
DR PDB; 6FOY; X-ray; 1.65 A; A/B=2-460.
DR PDB; 6FOZ; X-ray; 2.15 A; A/B=2-461.
DR PDB; 6FP0; X-ray; 2.03 A; A/B=2-460.
DR PDB; 6FP1; X-ray; 1.97 A; A/B=2-460.
DR PDB; 6FPH; X-ray; 2.00 A; A/B=2-461.
DR PDBsum; 5FN0; -.
DR PDBsum; 5MZC; -.
DR PDBsum; 5MZI; -.
DR PDBsum; 5MZK; -.
DR PDBsum; 5N7T; -.
DR PDBsum; 5NA5; -.
DR PDBsum; 5NAB; -.
DR PDBsum; 5NAE; -.
DR PDBsum; 5NAG; -.
DR PDBsum; 5NAH; -.
DR PDBsum; 5NAK; -.
DR PDBsum; 5X6P; -.
DR PDBsum; 5X6Q; -.
DR PDBsum; 5Y66; -.
DR PDBsum; 5Y77; -.
DR PDBsum; 5Y7A; -.
DR PDBsum; 6FOX; -.
DR PDBsum; 6FOY; -.
DR PDBsum; 6FOZ; -.
DR PDBsum; 6FP0; -.
DR PDBsum; 6FP1; -.
DR PDBsum; 6FPH; -.
DR AlphaFoldDB; Q84HF5; -.
DR SMR; Q84HF5; -.
DR BindingDB; Q84HF5; -.
DR ChEMBL; CHEMBL4105840; -.
DR BRENDA; 1.14.13.9; 5121.
DR UniPathway; UPA00253; UER00328.
DR UniPathway; UPA00981; -.
DR GO; GO:0071949; F:FAD 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:0070189; P:kynurenine metabolic process; IDA:UniProtKB.
DR GO; GO:0019674; P:NAD metabolic process; IDA: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 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase;
KW Pyridine nucleotide biosynthesis.
FT CHAIN 1..461
FT /note="Kynurenine 3-monooxygenase"
FT /id="PRO_0000361942"
FT BINDING 17..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28336141,
FT ECO:0000269|PubMed:28398044, ECO:0000269|PubMed:28604669,
FT ECO:0000269|PubMed:29208702, ECO:0000269|PubMed:29429898,
FT ECO:0007744|PDB:5FN0, ECO:0007744|PDB:5MZC,
FT ECO:0007744|PDB:5MZI, ECO:0007744|PDB:5MZK,
FT ECO:0007744|PDB:5N7T, ECO:0007744|PDB:5NA5,
FT ECO:0007744|PDB:5NAB, ECO:0007744|PDB:5NAE,
FT ECO:0007744|PDB:5NAG, ECO:0007744|PDB:5NAH,
FT ECO:0007744|PDB:5NAK, ECO:0007744|PDB:5X6P,
FT ECO:0007744|PDB:5X6Q, ECO:0007744|PDB:5Y66,
FT ECO:0007744|PDB:5Y77, ECO:0007744|PDB:5Y7A"
FT BINDING 37..39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28336141,
FT ECO:0000269|PubMed:28398044, ECO:0000269|PubMed:28604669,
FT ECO:0000269|PubMed:29208702, ECO:0000269|PubMed:29429898,
FT ECO:0007744|PDB:5FN0, ECO:0007744|PDB:5MZC,
FT ECO:0007744|PDB:5MZI, ECO:0007744|PDB:5MZK,
FT ECO:0007744|PDB:5N7T, ECO:0007744|PDB:5NA5,
FT ECO:0007744|PDB:5NAB, ECO:0007744|PDB:5NAE,
FT ECO:0007744|PDB:5NAG, ECO:0007744|PDB:5NAH,
FT ECO:0007744|PDB:5NAK, ECO:0007744|PDB:5X6P,
FT ECO:0007744|PDB:5X6Q, ECO:0007744|PDB:5Y66,
FT ECO:0007744|PDB:5Y77, ECO:0007744|PDB:5Y7A"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28336141,
FT ECO:0000269|PubMed:28398044, ECO:0000269|PubMed:28604669,
FT ECO:0000269|PubMed:29208702, ECO:0000269|PubMed:29429898,
FT ECO:0007744|PDB:5FN0, ECO:0007744|PDB:5MZC,
FT ECO:0007744|PDB:5MZI, ECO:0007744|PDB:5MZK,
FT ECO:0007744|PDB:5N7T, ECO:0007744|PDB:5NA5,
FT ECO:0007744|PDB:5NAB, ECO:0007744|PDB:5NAE,
FT ECO:0007744|PDB:5NAG, ECO:0007744|PDB:5NAH,
FT ECO:0007744|PDB:5NAK, ECO:0007744|PDB:5X6P,
FT ECO:0007744|PDB:5X6Q, ECO:0007744|PDB:5Y66,
FT ECO:0007744|PDB:5Y77, ECO:0007744|PDB:5Y7A"
FT BINDING 84
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000269|PubMed:29208702,
FT ECO:0007744|PDB:5Y66, ECO:0007744|PDB:5Y77"
FT BINDING 98
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000269|PubMed:29208702,
FT ECO:0007744|PDB:5Y77"
FT BINDING 111
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28336141,
FT ECO:0000269|PubMed:28398044, ECO:0000269|PubMed:28604669,
FT ECO:0000269|PubMed:29208702, ECO:0000269|PubMed:29429898,
FT ECO:0007744|PDB:5FN0, ECO:0007744|PDB:5MZC,
FT ECO:0007744|PDB:5MZI, ECO:0007744|PDB:5MZK,
FT ECO:0007744|PDB:5N7T, ECO:0007744|PDB:5NA5,
FT ECO:0007744|PDB:5NAB, ECO:0007744|PDB:5NAE,
FT ECO:0007744|PDB:5NAG, ECO:0007744|PDB:5NAH,
FT ECO:0007744|PDB:5NAK, ECO:0007744|PDB:5X6P,
FT ECO:0007744|PDB:5X6Q, ECO:0007744|PDB:5Y66,
FT ECO:0007744|PDB:5Y77, ECO:0007744|PDB:5Y7A"
FT BINDING 135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28336141,
FT ECO:0000269|PubMed:28398044, ECO:0000269|PubMed:28604669,
FT ECO:0000269|PubMed:29208702, ECO:0000269|PubMed:29429898,
FT ECO:0007744|PDB:5FN0, ECO:0007744|PDB:5MZC,
FT ECO:0007744|PDB:5MZI, ECO:0007744|PDB:5MZK,
FT ECO:0007744|PDB:5N7T, ECO:0007744|PDB:5NA5,
FT ECO:0007744|PDB:5NAB, ECO:0007744|PDB:5NAE,
FT ECO:0007744|PDB:5NAG, ECO:0007744|PDB:5NAH,
FT ECO:0007744|PDB:5NAK, ECO:0007744|PDB:5X6P,
FT ECO:0007744|PDB:5X6Q, ECO:0007744|PDB:5Y66,
FT ECO:0007744|PDB:5Y77, ECO:0007744|PDB:5Y7A"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28336141,
FT ECO:0000269|PubMed:28398044, ECO:0000269|PubMed:28604669,
FT ECO:0000269|PubMed:29208702, ECO:0000269|PubMed:29429898,
FT ECO:0007744|PDB:5FN0, ECO:0007744|PDB:5MZC,
FT ECO:0007744|PDB:5MZI, ECO:0007744|PDB:5MZK,
FT ECO:0007744|PDB:5N7T, ECO:0007744|PDB:5NA5,
FT ECO:0007744|PDB:5NAB, ECO:0007744|PDB:5NAE,
FT ECO:0007744|PDB:5NAG, ECO:0007744|PDB:5NAH,
FT ECO:0007744|PDB:5NAK, ECO:0007744|PDB:5X6P,
FT ECO:0007744|PDB:5X6Q, ECO:0007744|PDB:5Y66,
FT ECO:0007744|PDB:5Y77, ECO:0007744|PDB:5Y7A"
FT BINDING 324..325
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28336141,
FT ECO:0000269|PubMed:28398044, ECO:0000269|PubMed:28604669,
FT ECO:0000269|PubMed:29208702, ECO:0000269|PubMed:29429898,
FT ECO:0007744|PDB:5FN0, ECO:0007744|PDB:5MZC,
FT ECO:0007744|PDB:5MZI, ECO:0007744|PDB:5MZK,
FT ECO:0007744|PDB:5N7T, ECO:0007744|PDB:5NA5,
FT ECO:0007744|PDB:5NAB, ECO:0007744|PDB:5NAE,
FT ECO:0007744|PDB:5NAG, ECO:0007744|PDB:5NAH,
FT ECO:0007744|PDB:5NAK, ECO:0007744|PDB:5X6P,
FT ECO:0007744|PDB:5X6Q, ECO:0007744|PDB:5Y66,
FT ECO:0007744|PDB:5Y77, ECO:0007744|PDB:5Y7A"
FT BINDING 369
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000269|PubMed:29208702,
FT ECO:0007744|PDB:5Y66, ECO:0007744|PDB:5Y77,
FT ECO:0007744|PDB:5Y7A"
FT BINDING 404
FT /ligand="L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:57959"
FT /evidence="ECO:0000269|PubMed:29208702,
FT ECO:0007744|PDB:5Y66, ECO:0007744|PDB:5Y77,
FT ECO:0007744|PDB:5Y7A"
FT MUTAGEN 84
FT /note="R->A: Abolishes kynurenine 3-monooxygenase
FT activity."
FT /evidence="ECO:0000269|PubMed:29208702"
FT MUTAGEN 98
FT /note="Y->A,F: Abolishes kynurenine 3-monooxygenase
FT activity."
FT /evidence="ECO:0000269|PubMed:29208702"
FT MUTAGEN 319..320
FT /note="FH->AA: Abolishes NADPH oxidase activity."
FT /evidence="ECO:0000269|PubMed:29429898"
FT MUTAGEN 320
FT /note="H->A: Slightly decreases NADPH oxidase activity."
FT /evidence="ECO:0000269|PubMed:29429898"
FT MUTAGEN 369
FT /note="N->A: Decreases kynurenine 3-monooxygenase
FT activity."
FT /evidence="ECO:0000269|PubMed:29208702"
FT MUTAGEN 369
FT /note="N->D: Abolishes kynurenine 3-monooxygenase
FT activity."
FT /evidence="ECO:0000269|PubMed:29208702"
FT MUTAGEN 372
FT /note="E->A,Q: Strongly decreases kynurenine 3-
FT monooxygenase activity."
FT /evidence="ECO:0000269|PubMed:29208702"
FT MUTAGEN 373
FT /note="M->A: Abolishes kynurenine 3-monooxygenase
FT activity."
FT /evidence="ECO:0000269|PubMed:29208702"
FT MUTAGEN 373
FT /note="M->L: Decreases kynurenine 3-monooxygenase
FT activity."
FT /evidence="ECO:0000269|PubMed:29208702"
FT MUTAGEN 404
FT /note="Y->A: Abolishes kynurenine 3-monooxygenase
FT activity."
FT /evidence="ECO:0000269|PubMed:29208702"
FT MUTAGEN 404
FT /note="Y->F: Decreases kynurenine 3-monooxygenase
FT activity."
FT /evidence="ECO:0000269|PubMed:29208702"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5NAK"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:5FN0"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5X6P"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:5NAK"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:5Y7A"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:5NAK"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 233..242
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:5X6P"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 259..269
FT /evidence="ECO:0007829|PDB:5NAK"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 280..286
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:5Y7A"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 323..340
FT /evidence="ECO:0007829|PDB:5NAK"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 344..374
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 380..395
FT /evidence="ECO:0007829|PDB:5NAK"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 403..409
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 414..432
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:5NAK"
FT HELIX 443..453
FT /evidence="ECO:0007829|PDB:5NAK"
SQ SEQUENCE 461 AA; 50712 MW; 6515A55FFE8987F4 CRC64;
MTATDNARQV TIIGAGLAGT LVARLLARNG WQVNLFERRP DPRIETGARG RSINLALAER
GAHALRLAGL EREVLAEAVM MRGRMVHVPG TPPNLQPYGR DDSEVIWSIN RDRLNRILLD
GAEAAGASIH FNLGLDSVDF ARQRLTLSNV SGERLEKRFH LLIGADGCNS AVRQAMASVV
DLGEHLETQP HGYKELQITP EASAQFNLEP NALHIWPHGD YMCIALPNLD RSFTVTLFLH
HQSPAAQPAS PCFAQLVDGH AARRFFQRQF PDLSPMLDSL EQDFEHHPTG KLATLRLTTW
HVGGQAVLLG DAAHPMVPFH GQGMNCALED AVALAEHLQS AADNASALAA FTAQRQPDAL
AIQAMALENY VEMSSKVASP TYLLERELGQ IMAQRQPTRF IPRYSMVTFS RLPYAQAMAR
GQIQEQLLKF AVANHSDLTS INLDAVEHEV TRCLPPLSHL C
