ID   SCYD_PYRO7              Reviewed;         172 AA.
AC   P56221; A4QTI6; G4N445;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   24-JAN-2024, entry version 133.
DE   RecName: Full=Scytalone dehydratase {ECO:0000303|PubMed:9571787};
DE            Short=SD {ECO:0000303|PubMed:9539706};
DE            Short=SDH {ECO:0000303|PubMed:9571787};
DE            EC=4.2.1.94 {ECO:0000269|PubMed:10320327, ECO:0000269|PubMed:10386945, ECO:0000269|PubMed:9466791, ECO:0000269|PubMed:9466792, ECO:0000269|PubMed:9539706, ECO:0000269|PubMed:9571787};
GN   Name=SDH1; ORFNames=MGG_05059;
OS   Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Magnaporthe oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9571787; DOI=10.1271/bbb.62.564;
RA   Motoyama T., Imanishi K., Yamaguchi I.;
RT   "cDNA cloning, expression, and mutagenesis of scytalone dehydratase needed
RT   for pathogenicity of the rice blast fungus, Pyricularia oryzae.";
RL   Biosci. Biotechnol. Biochem. 62:564-566(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 95-106, AND INDUCTION.
RX   PubMed=15378734; DOI=10.1002/pmic.200400969;
RA   Kim S.T., Yu S., Kim S.G., Kim H.J., Kang S.Y., Hwang D.H., Jang Y.S.,
RA   Kang K.Y.;
RT   "Proteome analysis of rice blast fungus (Magnaporthe grisea) proteome
RT   during appressorium formation.";
RL   Proteomics 4:3579-3587(2004).
RN   [4]
RP   CRYSTALLIZATION.
RX   PubMed=8355286; DOI=10.1006/jmbi.1993.1449;
RA   Lundqvist T., Weber P.C., Hodge C.N., Braswell E.H., Rice J., Pierce J.;
RT   "Preliminary crystallographic studies on scytalone dehydratase from
RT   Magnaporthe grisea.";
RL   J. Mol. Biol. 232:999-1002(1993).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9466791; DOI=10.1006/abio.1997.2489;
RA   Thompson J.E., Basarab G.S., Pierce J., Hodge C.N., Jordan D.B.;
RT   "2,3-Dihydro-2,5-dihydroxy-4H-benzopyran-4-one: a nonphysiological
RT   substrate for fungal melanin biosynthetic enzymes.";
RL   Anal. Biochem. 256:1-6(1998).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9466792; DOI=10.1006/abio.1997.2490;
RA   Thompson J.E., Jordan D.B.;
RT   "Partition analysis of an enzyme acting concurrently upon two substrates in
RT   a continuous multiwavelength assay.";
RL   Anal. Biochem. 256:7-13(1998).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX   PubMed=9539706; DOI=10.1073/pnas.95.8.4158;
RA   Zheng Y.J., Bruice T.C.;
RT   "Role of a critical water in scytalone dehydratase-catalyzed reaction.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:4158-4163(1998).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP   AND MUTAGENESIS OF TYR-30; ASP-31; TYR-50; HIS-85; HIS-110; SER-129 AND
RP   ASN-131.
RX   PubMed=10320327; DOI=10.1021/bi982952b;
RA   Basarab G.S., Steffens J.J., Wawrzak Z., Schwartz R.S., Lundqvist T.,
RA   Jordan D.B.;
RT   "Catalytic mechanism of scytalone dehydratase: site-directed mutagenesis,
RT   kinetic isotope effects, and alternate substrates.";
RL   Biochemistry 38:6012-6024(1999).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=10386945; DOI=10.1016/s0960-894x(99)00246-2;
RA   Jordan D.B., Lessen T.A., Wawrzak Z., Bisaha J.J., Gehret T.C.,
RA   Hansen S.L., Schwartz R.S., Basarab G.S.;
RT   "Design of scytalone dehydratase inhibitors as rice blast fungicides: (N-
RT   phenoxypropyl)-carboxamides.";
RL   Bioorg. Med. Chem. Lett. 9:1607-1612(1999).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=10386946; DOI=10.1016/s0960-894x(99)00247-4;
RA   Basarab G.S., Jordan D.B., Gehret T.C., Schwartz R.S., Wawrzak Z.;
RT   "Design of scytalone dehydratase inhibitors as rice blast fungicides:
RT   derivatives of norephedrine.";
RL   Bioorg. Med. Chem. Lett. 9:1613-1618(1999).
RN   [11]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10694394; DOI=10.1021/bi991839y;
RA   Jordan D.B., Zheng Y.J., Lockett B.A., Basarab G.S.;
RT   "Stereochemistry of the enolization of scytalone by scytalone
RT   dehydratase.";
RL   Biochemistry 39:2276-2282(2000).
RN   [12]
RP   FUNCTION, CATALYTIC ACTIVITY, INHIBITOR-BINDING, AND MUTAGENESIS OF PHE-53;
RP   MET-69; VAL-75; PHE-158 AND PHE-162.
RX   PubMed=10913266; DOI=10.1021/bi000467m;
RA   Jordan D.B., Basarab G.S., Steffens J.J., Schwartz R.S., Doughty J.G.;
RT   "Tight binding inhibitors of scytalone dehydratase: effects of site-
RT   directed mutations.";
RL   Biochemistry 39:8593-8602(2000).
RN   [13]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-30; TYR-50; HIS-85;
RP   HIS-110 AND ASN-131.
RX   PubMed=10636235; DOI=10.1016/s0960-894x(99)00586-7;
RA   Jordan D.B., Basarab G.S.;
RT   "Binding dynamics of two water molecules constrained within the scytalone
RT   dehydratase binding pocket.";
RL   Bioorg. Med. Chem. Lett. 10:23-26(2000).
RN   [14]
RP   ACTIVITY REGULATION.
RX   PubMed=10882002; DOI=10.1016/s0968-0896(00)00034-1;
RA   Jennings L.D., Rayner D.R., Jordan D.B., Okonya J.F., Basarab G.S.,
RA   Amorose D.K., Anaclerio B.M., Lee J.K., Schwartz R.S., Whitmore K.A.;
RT   "Cyclobutane carboxamide inhibitors of fungal melanin: biosynthesis and
RT   their evaluation as fungicides.";
RL   Bioorg. Med. Chem. 8:897-907(2000).
RN   [15]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   MUTAGENESIS OF PHE-53; HIS-110 AND ASN-131.
RX   PubMed=11790103; DOI=10.1021/bi015848u;
RA   Zheng Y.J., Basarab G.S., Jordan D.B.;
RT   "Roles of substrate distortion and intramolecular hydrogen bonding in
RT   enzymatic catalysis by scytalone dehydratase.";
RL   Biochemistry 41:820-826(2002).
RN   [16]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=12413868; DOI=10.1016/s0968-0896(02)00272-9;
RA   Basarab G.S., Jordan D.B., Gehret T.C., Schwartz R.S.;
RT   "Design of inhibitors of scytalone dehydratase: probing interactions with
RT   an asparagine carboxamide.";
RL   Bioorg. Med. Chem. 10:4143-4154(2002).
RN   [17]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP   VAL-75.
RX   PubMed=15056895; DOI=10.1271/bbb.68.615;
RA   Yamada N., Motoyama T., Nakasako M., Kagabu S., Kudo T., Yamaguchi I.;
RT   "Enzymatic characterization of scytalone dehydratase Val75Met variant found
RT   in melanin biosynthesis dehydratase inhibitor (MBI-D) resistant strains of
RT   the rice blast fungus.";
RL   Biosci. Biotechnol. Biochem. 68:615-621(2004).
RN   [18]
RP   ACTIVITY REGULATION, AND MUTAGENESIS OF VAL-75.
RX   PubMed=15382507; DOI=10.1002/ps.896;
RA   Takagaki M., Kaku K., Watanabe S., Kawai K., Shimizu T., Sawada H.,
RA   Kumakura K., Nagayama K.;
RT   "Mechanism of resistance to carpropamid in Magnaporthe grisea.";
RL   Pest Manag. Sci. 60:921-926(2004).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH INHIBITOR, SUBUNIT,
RP   AND ACTIVE SITE.
RX   PubMed=7866745; DOI=10.1016/s0969-2126(94)00095-6;
RA   Lundqvist T., Rice J., Hodge C.N., Basarab G.S., Pierce J., Lindqvist Y.;
RT   "Crystal structure of scytalone dehydratase -- a disease determinant of the
RT   rice pathogen, Magnaporthe grisea.";
RL   Structure 2:937-944(1994).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH INHIBITOR
RP   CARPROPAMID.
RX   PubMed=9665698; DOI=10.1021/bi980321b;
RA   Nakasako M., Motoyama T., Kurahashi Y., Yamaguchi I.;
RT   "Cryogenic X-ray crystal structure analysis for the complex of scytalone
RT   dehydratase of a rice blast fungus and its tight-binding inhibitor,
RT   carpropamid: the structural basis of tight-binding inhibition.";
RL   Biochemistry 37:9931-9939(1998).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 10-172 IN COMPLEX WITH INHIBITOR.
RX   PubMed=9922139; DOI=10.1021/bi981848r;
RA   Chen J.M., Xu S.L., Wawrzak Z., Basarab G.S., Jordan D.B.;
RT   "Structure-based design of potent inhibitors of scytalone dehydratase:
RT   displacement of a water molecule from the active site.";
RL   Biochemistry 37:17735-17744(1998).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 10-172 IN COMPLEX WITH INHIBITOR.
RX   PubMed=10382670;
RX   DOI=10.1002/(sici)1097-0134(19990601)35:4<425::aid-prot6>3.0.co;2-1;
RA   Wawrzak Z., Sandalova T., Steffens J.J., Basarab G.S., Lundqvist T.,
RA   Lindqvist Y., Jordan D.B.;
RT   "High-resolution structures of scytalone dehydratase-inhibitor complexes
RT   crystallized at physiological pH.";
RL   Proteins 35:425-439(1999).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
RX   PubMed=11752795; DOI=10.1107/s0907444901017371;
RA   Motoyama T., Nakasako M., Yamaguchi I.;
RT   "Crystallization of scytalone dehydratase F162A mutant in the unligated
RT   state and a preliminary X-ray diffraction study at 37 K.";
RL   Acta Crystallogr. D 58:148-150(2002).
CC   -!- FUNCTION: Scytalone dehydratase; part of the gene cluster that mediates
CC       the biosynthesis of dihydroxynaphthalene melanin, a bluish-green
CC       pigment and a structural component of the conidial wall
CC       (PubMed:9571787). Within the pathway, catalyzes the dehydration of
CC       scytalone as well as of vermelone (PubMed:9571787, PubMed:9466791,
CC       PubMed:9466792, PubMed:9539706, PubMed:10320327, PubMed:10386945,
CC       PubMed:10386946, PubMed:10694394, PubMed:10913266, PubMed:10636235,
CC       PubMed:11790103, PubMed:12413868, PubMed:15056895). Is also able to
CC       dehydrate the alternate substrate 2,3-dihydro-2,5-dihydroxy-4H-
CC       benzopyran-4-one (DDBO) to 5-hydroxy-4H-1-benzopyran-4-one (HBO)
CC       (PubMed:9466791, PubMed:9466792, PubMed:10320327, PubMed:10386945,
CC       PubMed:11790103). {ECO:0000269|PubMed:10320327,
CC       ECO:0000269|PubMed:10386945, ECO:0000269|PubMed:10386946,
CC       ECO:0000269|PubMed:10636235, ECO:0000269|PubMed:10694394,
CC       ECO:0000269|PubMed:10913266, ECO:0000269|PubMed:11790103,
CC       ECO:0000269|PubMed:12413868, ECO:0000269|PubMed:15056895,
CC       ECO:0000269|PubMed:9466791, ECO:0000269|PubMed:9466792,
CC       ECO:0000269|PubMed:9539706, ECO:0000269|PubMed:9571787}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=scytalone = 1,3,8-trihydroxynaphthalene + H2O;
CC         Xref=Rhea:RHEA:24396, ChEBI:CHEBI:15377, ChEBI:CHEBI:16945,
CC         ChEBI:CHEBI:18393; EC=4.2.1.94;
CC         Evidence={ECO:0000269|PubMed:10320327, ECO:0000269|PubMed:10386945,
CC         ECO:0000269|PubMed:10386946, ECO:0000269|PubMed:10636235,
CC         ECO:0000269|PubMed:10694394, ECO:0000269|PubMed:10913266,
CC         ECO:0000269|PubMed:11790103, ECO:0000269|PubMed:12413868,
CC         ECO:0000269|PubMed:15056895, ECO:0000269|PubMed:9466791,
CC         ECO:0000269|PubMed:9466792, ECO:0000269|PubMed:9539706,
CC         ECO:0000269|PubMed:9571787};
CC   -!- ACTIVITY REGULATION: (N-phenoxypropyl)-carboxamides such as carpropamid
CC       and derivatives of norephedrine act as inhibitors of scytalone
CC       dehydratase activity. {ECO:0000269|PubMed:10386945,
CC       ECO:0000269|PubMed:10386946, ECO:0000269|PubMed:10882002,
CC       ECO:0000269|PubMed:12413868, ECO:0000269|PubMed:15056895,
CC       ECO:0000269|PubMed:15382507}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=15 uM for 2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one (DDBO)
CC         {ECO:0000269|PubMed:10320327, ECO:0000269|PubMed:9466791};
CC         KM=33 uM for scytalone {ECO:0000269|PubMed:10320327};
CC         KM=31 uM for vermelone {ECO:0000269|PubMed:10320327,
CC         ECO:0000269|PubMed:11790103};
CC   -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC       {ECO:0000269|PubMed:9571787}.
CC   -!- SUBUNIT: Homotrimer (PubMed:7866745). Each subunit contains an active
CC       site, located in the central part of the hydrophobic core of the
CC       monomer, which functions independently (PubMed:7866745).
CC       {ECO:0000269|PubMed:7866745}.
CC   -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:O14434}.
CC   -!- INDUCTION: Expression is induced in the stationary phase, when melanin
CC       synthesis occurs (PubMed:9571787). Expression is specifically induced
CC       during appressorium formation (PubMed:15378734).
CC       {ECO:0000269|PubMed:15378734, ECO:0000269|PubMed:9571787}.
CC   -!- SIMILARITY: Belongs to the scytalone dehydratase family. {ECO:0000305}.
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DR   EMBL; AB004741; BAA34046.1; -; mRNA.
DR   EMBL; CM001233; EHA52765.1; -; Genomic_DNA.
DR   RefSeq; XP_003712572.1; XM_003712524.1.
DR   PDB; 1IDP; X-ray; 1.45 A; A/B/C=1-172.
DR   PDB; 1STD; X-ray; 2.90 A; A=1-172.
DR   PDB; 2STD; X-ray; 2.10 A; A=1-172.
DR   PDB; 3STD; X-ray; 1.65 A; A/B/C=10-172.
DR   PDB; 4STD; X-ray; 2.15 A; A/B/C=10-172.
DR   PDB; 5STD; X-ray; 1.95 A; A/B/C=10-172.
DR   PDB; 6STD; X-ray; 1.80 A; A/B/C=10-172.
DR   PDB; 7STD; X-ray; 1.80 A; A/B/C=10-172.
DR   PDBsum; 1IDP; -.
DR   PDBsum; 1STD; -.
DR   PDBsum; 2STD; -.
DR   PDBsum; 3STD; -.
DR   PDBsum; 4STD; -.
DR   PDBsum; 5STD; -.
DR   PDBsum; 6STD; -.
DR   PDBsum; 7STD; -.
DR   AlphaFoldDB; P56221; -.
DR   SMR; P56221; -.
DR   STRING; 242507.P56221; -.
DR   BindingDB; P56221; -.
DR   ChEMBL; CHEMBL2578; -.
DR   EnsemblFungi; MGG_05059T0; MGG_05059T0; MGG_05059.
DR   GeneID; 2675492; -.
DR   KEGG; mgr:MGG_05059; -.
DR   VEuPathDB; FungiDB:MGG_05059; -.
DR   eggNOG; ENOG502SNND; Eukaryota.
DR   HOGENOM; CLU_101889_0_0_1; -.
DR   InParanoid; P56221; -.
DR   OMA; SACYEWA; -.
DR   OrthoDB; 2783020at2759; -.
DR   BRENDA; 4.2.1.94; 3152.
DR   UniPathway; UPA00785; -.
DR   EvolutionaryTrace; P56221; -.
DR   PRO; PR:P56221; -.
DR   Proteomes; UP000009058; Chromosome 3.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030411; F:scytalone dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00531; NTF2_like; 1.
DR   Gene3D; 3.10.450.50; -; 1.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR004235; Scytalone_dehydratase.
DR   Pfam; PF02982; Scytalone_dh; 1.
DR   PIRSF; PIRSF024851; SCD1; 1.
DR   SUPFAM; SSF54427; NTF2-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Direct protein sequencing; Endosome; Lyase;
KW   Melanin biosynthesis; Metal-binding; Reference proteome.
FT   CHAIN           1..172
FT                   /note="Scytalone dehydratase"
FT                   /id="PRO_0000097639"
FT   ACT_SITE        85
FT                   /evidence="ECO:0000305|PubMed:7866745"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000305|PubMed:7866745"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:9922139"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:9665698"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:10382670"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:10382670,
FT                   ECO:0000305|PubMed:7866745, ECO:0000305|PubMed:9922139"
FT   MUTAGEN         30
FT                   /note="Y->F: Results in a 9-fold decrease of activity with
FT                   scytalone as the substrate and increases binding of
FT                   salicylamide inhibitors."
FT                   /evidence="ECO:0000269|PubMed:10320327,
FT                   ECO:0000269|PubMed:10636235"
FT   MUTAGEN         31
FT                   /note="D->N: Reduces catalysis 5000-fold and substrate
FT                   affinity about 4-fold with scytalone as the substrate."
FT                   /evidence="ECO:0000269|PubMed:10320327"
FT   MUTAGEN         50
FT                   /note="Y->F: Results in a 500-fold decrease of activity
FT                   with scytalone as the substrate and increases binding of
FT                   salicylamide inhibitors."
FT                   /evidence="ECO:0000269|PubMed:10320327,
FT                   ECO:0000269|PubMed:10636235"
FT   MUTAGEN         53
FT                   /note="F->A: Leads to significantly higher relative
FT                   substrate specificities (DDBO/vermelone)."
FT                   /evidence="ECO:0000269|PubMed:11790103"
FT   MUTAGEN         53
FT                   /note="F->L: Affects the binding of inhibitors and has
FT                   significantly higher relative substrate specificities
FT                   (DDBO/vermelone)."
FT                   /evidence="ECO:0000269|PubMed:10913266,
FT                   ECO:0000269|PubMed:11790103"
FT   MUTAGEN         69
FT                   /note="M->L: Affects the binding of inhibitors."
FT                   /evidence="ECO:0000269|PubMed:10913266"
FT   MUTAGEN         75
FT                   /note="V->A: Affects the binding of inhibitors and reduces
FT                   more than 200-fold inhibition by carpropamid."
FT                   /evidence="ECO:0000269|PubMed:10913266,
FT                   ECO:0000269|PubMed:15056895"
FT   MUTAGEN         75
FT                   /note="V->M: Strongly reduces inhibition by carpropamid."
FT                   /evidence="ECO:0000269|PubMed:15382507"
FT   MUTAGEN         85
FT                   /note="H->N: Greatly decreases catalytic efficiency and
FT                   decreases binding to salicylamide inhibitors."
FT                   /evidence="ECO:0000269|PubMed:10320327,
FT                   ECO:0000269|PubMed:10636235"
FT   MUTAGEN         110
FT                   /note="H->N: Causes a 250-fold decrease of activity and a
FT                   6-fold increase in Km with scytalone as the substrate,
FT                   decreases binding of salicylamide inhibitors, and has
FT                   significantly higher relative substrate specificities
FT                   (DDBO/vermelone)."
FT                   /evidence="ECO:0000269|PubMed:10320327,
FT                   ECO:0000269|PubMed:10636235, ECO:0000269|PubMed:11790103"
FT   MUTAGEN         129
FT                   /note="S->A: Results in a 80-fold decrease of activity and
FT                   a 7-fold increase in Km with scytalone as the substrate."
FT                   /evidence="ECO:0000269|PubMed:10320327"
FT   MUTAGEN         129
FT                   /note="S->T: Results in a 120-fold decrease of activity and
FT                   a 23-fold increase in Km with scytalone as the substrate."
FT                   /evidence="ECO:0000269|PubMed:10320327"
FT   MUTAGEN         131
FT                   /note="N->A: Decreases turnover by nearly 90-fold and
FT                   increases Km 8-fold with scytalone as the substrate,
FT                   decreases strongly binding of salicylamide inhibitors, and
FT                   has significantly higher relative substrate specificities
FT                   (DDBO/vermelone)."
FT                   /evidence="ECO:0000269|PubMed:10320327,
FT                   ECO:0000269|PubMed:10636235, ECO:0000269|PubMed:11790103"
FT   MUTAGEN         158
FT                   /note="F->L: Affects the binding of inhibitors."
FT                   /evidence="ECO:0000269|PubMed:10913266"
FT   MUTAGEN         162
FT                   /note="F->L: Affects the binding of inhibitors."
FT                   /evidence="ECO:0000269|PubMed:10913266"
FT   HELIX           13..32
FT                   /evidence="ECO:0007829|PDB:1IDP"
FT   HELIX           35..39
FT                   /evidence="ECO:0007829|PDB:1IDP"
FT   STRAND          42..49
FT                   /evidence="ECO:0007829|PDB:1IDP"
FT   HELIX           51..54
FT                   /evidence="ECO:0007829|PDB:1IDP"
FT   STRAND          57..62
FT                   /evidence="ECO:0007829|PDB:1IDP"
FT   HELIX           63..71
FT                   /evidence="ECO:0007829|PDB:1IDP"
FT   TURN            73..76
FT                   /evidence="ECO:0007829|PDB:1IDP"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:1IDP"
FT   STRAND          86..96
FT                   /evidence="ECO:0007829|PDB:1IDP"
FT   STRAND          99..115
FT                   /evidence="ECO:0007829|PDB:1IDP"
FT   STRAND          121..138
FT                   /evidence="ECO:0007829|PDB:1IDP"
FT   STRAND          141..155
FT                   /evidence="ECO:0007829|PDB:1IDP"
FT   HELIX           158..161
FT                   /evidence="ECO:0007829|PDB:3STD"
FT   HELIX           163..169
FT                   /evidence="ECO:0007829|PDB:3STD"
SQ   SEQUENCE   172 AA;  20250 MW;  2FA56296D5EE00DC CRC64;
     MGSQVQKSDE ITFSDYLGLM TCVYEWADSY DSKDWDRLRK VIAPTLRIDY RSFLDKLWEA
     MPAEEFVGMV SSKQVLGDPT LRTQHFIGGT RWEKVSEDEV IGYHQLRVPH QRYKDTTMKE
     VTMKGHAHSA NLHWYKKIDG VWKFAGLKPD IRWGEFDFDR IFEDGRETFG DK
//