ID   KMO_YEAST               Reviewed;         460 AA.
AC   P38169; D6VPQ7;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 194.
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=Biosynthesis of nicotinic acid protein 4 {ECO:0000255|HAMAP-Rule:MF_03018};
DE   AltName: Full=Kynurenine 3-hydroxylase {ECO:0000255|HAMAP-Rule:MF_03018};
GN   Name=BNA4 {ECO:0000255|HAMAP-Rule:MF_03018};
GN   OrderedLocusNames=YBL098W; ORFNames=YBL0828;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7502586; DOI=10.1002/yea.320111112;
RA   Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT   "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT   cerevisiae chromosome II.";
RL   Yeast 11:1103-1112(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=12062417; DOI=10.1016/s0014-5793(02)02585-1;
RA   Panozzo C., Nawara M., Suski C., Kucharczyka R., Skoneczny M., Becam A.-M.,
RA   Rytka J., Herbert C.J.;
RT   "Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae.";
RL   FEBS Lett. 517:97-102(2002).
RN   [6]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA   Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA   Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT   "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT   accumulation of a subclass of preproteins.";
RL   Mol. Biol. Cell 17:1436-1450(2006).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA   Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA   Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [8]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [9]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [10]
RP   FUNCTION.
RX   PubMed=15806102; DOI=10.1038/ng1542;
RA   Giorgini F., Guidetti P., Nguyen Q., Bennett S.C., Muchowski P.J.;
RT   "A genomic screen in yeast implicates kynurenine 3-monooxygenase as a
RT   therapeutic target for Huntington disease.";
RL   Nat. Genet. 37:526-531(2005).
RN   [11] {ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31, ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34, ECO:0007744|PDB:4J36}
RP   X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 1-396 IN COMPLEX WITH FAD AND
RP   INHIBITOR, FUNCTION, AND MUTAGENESIS OF ARG-83.
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   [12] {ECO:0007744|PDB:5X6R}
RP   X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 1-394 IN COMPLEX WITH FAD AND
RP   INHIBITOR, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND MUTAGENESIS OF
RP   322-PHE-TYR-323.
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). Required for synthesis of quinolinic
CC       acid. {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:12062417,
CC       ECO:0000269|PubMed:15806102, ECO:0000269|PubMed:23575632}.
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:29429898};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:29429898};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03018,
CC       ECO:0000269|PubMed:12062417, ECO:0000269|PubMed:29429898}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03018, ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16407407}.
CC   -!- MISCELLANEOUS: Present with 556 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: Deletion of BNA4 suppresses the toxicity of a mutant
CC       HD/HTT fragment.
CC   -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03018}.
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DR   EMBL; X79489; CAA56002.1; -; Genomic_DNA.
DR   EMBL; Z35859; CAA84920.1; -; Genomic_DNA.
DR   EMBL; AY692951; AAT92970.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07027.1; -; Genomic_DNA.
DR   PIR; S45402; S45402.
DR   RefSeq; NP_009454.1; NM_001178338.1.
DR   PDB; 4J2W; X-ray; 2.60 A; A/B=1-396.
DR   PDB; 4J31; X-ray; 2.40 A; A/B=1-396.
DR   PDB; 4J33; X-ray; 1.82 A; A/B=1-394.
DR   PDB; 4J34; X-ray; 2.03 A; A/B=1-394.
DR   PDB; 4J36; X-ray; 2.13 A; A/B=1-394.
DR   PDB; 5X6R; X-ray; 1.91 A; A/B=1-394.
DR   PDBsum; 4J2W; -.
DR   PDBsum; 4J31; -.
DR   PDBsum; 4J33; -.
DR   PDBsum; 4J34; -.
DR   PDBsum; 4J36; -.
DR   PDBsum; 5X6R; -.
DR   AlphaFoldDB; P38169; -.
DR   SMR; P38169; -.
DR   BioGRID; 32607; 115.
DR   DIP; DIP-5165N; -.
DR   IntAct; P38169; 2.
DR   STRING; 4932.YBL098W; -.
DR   BindingDB; P38169; -.
DR   ChEMBL; CHEMBL3627588; -.
DR   iPTMnet; P38169; -.
DR   MaxQB; P38169; -.
DR   PaxDb; 4932-YBL098W; -.
DR   PeptideAtlas; P38169; -.
DR   EnsemblFungi; YBL098W_mRNA; YBL098W; YBL098W.
DR   GeneID; 852179; -.
DR   KEGG; sce:YBL098W; -.
DR   AGR; SGD:S000000194; -.
DR   SGD; S000000194; BNA4.
DR   VEuPathDB; FungiDB:YBL098W; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   GeneTree; ENSGT00390000000747; -.
DR   HOGENOM; CLU_023210_0_1_1; -.
DR   InParanoid; P38169; -.
DR   OMA; REFMFIA; -.
DR   OrthoDB; 2250465at2759; -.
DR   BioCyc; MetaCyc:YBL098W-MONOMER; -.
DR   BioCyc; YEAST:YBL098W-MONOMER; -.
DR   BRENDA; 1.14.13.9; 984.
DR   Reactome; R-SCE-71240; Tryptophan catabolism.
DR   UniPathway; UPA00253; UER00328.
DR   BioGRID-ORCS; 852179; 9 hits in 10 CRISPR screens.
DR   PRO; PR:P38169; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38169; Protein.
DR   GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
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; IGI:SGD.
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; 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.
PE   1: Evidence at protein level;
KW   3D-structure; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Monooxygenase; NADP; Oxidoreductase;
KW   Pyridine nucleotide biosynthesis; Reference proteome.
FT   CHAIN           1..460
FT                   /note="Kynurenine 3-monooxygenase"
FT                   /id="PRO_0000020823"
FT   BINDING         13
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31,
FT                   ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34,
FT                   ECO:0007744|PDB:4J36"
FT   BINDING         32..34
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31,
FT                   ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34,
FT                   ECO:0007744|PDB:4J36"
FT   BINDING         53
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31,
FT                   ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34,
FT                   ECO:0007744|PDB:4J36"
FT   BINDING         83
FT                   /ligand="L-kynurenine"
FT                   /ligand_id="ChEBI:CHEBI:57959"
FT                   /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT   BINDING         97
FT                   /ligand="L-kynurenine"
FT                   /ligand_id="ChEBI:CHEBI:57959"
FT                   /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT   BINDING         109
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31,
FT                   ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34,
FT                   ECO:0007744|PDB:4J36"
FT   BINDING         133
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31,
FT                   ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34,
FT                   ECO:0007744|PDB:4J36"
FT   BINDING         195
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:4J33"
FT   BINDING         314
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31,
FT                   ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34,
FT                   ECO:0007744|PDB:4J36"
FT   BINDING         325..328
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007744|PDB:4J2W, ECO:0007744|PDB:4J31,
FT                   ECO:0007744|PDB:4J33, ECO:0007744|PDB:4J34,
FT                   ECO:0007744|PDB:4J36"
FT   BINDING         373
FT                   /ligand="L-kynurenine"
FT                   /ligand_id="ChEBI:CHEBI:57959"
FT                   /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT   BINDING         408
FT                   /ligand="L-kynurenine"
FT                   /ligand_id="ChEBI:CHEBI:57959"
FT                   /evidence="ECO:0000250|UniProtKB:Q84HF5"
FT   MUTAGEN         83
FT                   /note="R->A: Strongly decreases enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:23575632"
FT   MUTAGEN         83
FT                   /note="R->M: Abolsihes enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:23575632"
FT   MUTAGEN         322..323
FT                   /note="FY->AA: Abolishes NADPH oxidase activity."
FT                   /evidence="ECO:0000269|PubMed:29429898"
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   HELIX           12..23
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          27..34
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          39..41
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          50..55
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   HELIX           56..65
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   HELIX           67..73
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          82..86
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          92..96
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:4J34"
FT   STRAND          104..108
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   HELIX           109..120
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   TURN            121..124
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          126..129
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          131..137
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          143..149
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   TURN            151..153
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          156..166
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   HELIX           173..179
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          185..190
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          194..200
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   TURN            208..210
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          211..213
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          220..225
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          230..235
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          241..247
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   HELIX           249..255
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   HELIX           259..269
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   HELIX           271..273
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   TURN            274..276
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   HELIX           279..288
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          295..300
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          302..304
FT                   /evidence="ECO:0007829|PDB:5X6R"
FT   TURN            305..308
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   STRAND          309..311
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   HELIX           314..317
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   TURN            321..323
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   HELIX           326..343
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   TURN            344..346
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   HELIX           348..377
FT                   /evidence="ECO:0007829|PDB:4J33"
FT   TURN            384..386
FT                   /evidence="ECO:0007829|PDB:4J33"
SQ   SEQUENCE   460 AA;  52429 MW;  5340CC6C9D901D17 CRC64;
     MSESVAIIGA GLVGCLAALA FSKEGYNVTL YDFRQDPRLD TTKNKNLKSI NLAISARGID
     ALKSIDPDAC EHILQDMIPM KGRMIHDLKG RQESQLYGLH GEAINSINRS VLNNSLLDEL
     EKSTTELKFG HKLVKIEWTD DKQICHFAIG EDLKTPHTEK YDFVIGCDGA YSATRSQMQR
     KVEMDFSQEY MNLRYIELYI PPTEEFKPNY GGNFAIAPDH LHIWPRHKFM LIALANSDGS
     FTSTFFGSKD QISDLITSKS RVREFLIENF PDIINIMDLD DAVKRFITYP KESLVCVNCK
     PYDVPGGKAI LLGDAAHAMV PFYGQGMNCG FEDVRILMAL LKKHSGDRSR AFTEYTQTRH
     KDLVSITELA KRNYKEMSHD VTSKRFLLRK KLDALFSIIM KDKWIPLYTM ISFRSDISYS
     RALERAGKQT RILKFLESLT LGMLSIGGYK LFKFLTRERS
//