SCYD_MAGO7
ID SCYD_MAGO7 Reviewed; 172 AA.
AC P56221; A4QTI6; G4N445;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia 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; 318829.MGG_05059T0; -.
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; RKCIAPT; -.
DR OrthoDB; 1377897at2759; -.
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 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; SSF54427; 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: Reduces strongly 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
