##gff-version 3
P56221	UniProtKB	Chain	1	172	.	.	.	ID=PRO_0000097639;Note=Scytalone dehydratase	
P56221	UniProtKB	Active site	85	85	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7866745;Dbxref=PMID:7866745	
P56221	UniProtKB	Active site	110	110	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7866745;Dbxref=PMID:7866745	
P56221	UniProtKB	Binding site	30	30	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9922139;Dbxref=PMID:9922139	
P56221	UniProtKB	Binding site	50	50	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:9665698;Dbxref=PMID:9665698	
P56221	UniProtKB	Binding site	53	53	.	.	.	Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10382670;Dbxref=PMID:10382670	
P56221	UniProtKB	Binding site	131	131	.	.	.	Ontology_term=ECO:0000305,ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:10382670,ECO:0000305|PubMed:7866745,ECO:0000305|PubMed:9922139;Dbxref=PMID:10382670,PMID:7866745,PMID:9922139	
P56221	UniProtKB	Mutagenesis	30	30	.	.	.	Note=Results in a 9-fold decrease of activity with scytalone as the substrate and increases binding of salicylamide inhibitors. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10320327,ECO:0000269|PubMed:10636235;Dbxref=PMID:10320327,PMID:10636235	
P56221	UniProtKB	Mutagenesis	31	31	.	.	.	Note=Reduces catalysis 5000-fold and substrate affinity about 4-fold with scytalone as the substrate. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10320327;Dbxref=PMID:10320327	
P56221	UniProtKB	Mutagenesis	50	50	.	.	.	Note=Results in a 500-fold decrease of activity with scytalone as the substrate and increases binding of salicylamide inhibitors. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10320327,ECO:0000269|PubMed:10636235;Dbxref=PMID:10320327,PMID:10636235	
P56221	UniProtKB	Mutagenesis	53	53	.	.	.	Note=Leads to significantly higher relative substrate specificities (DDBO/vermelone). F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11790103;Dbxref=PMID:11790103	
P56221	UniProtKB	Mutagenesis	53	53	.	.	.	Note=Affects the binding of inhibitors and has significantly higher relative substrate specificities (DDBO/vermelone). F->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10913266,ECO:0000269|PubMed:11790103;Dbxref=PMID:10913266,PMID:11790103	
P56221	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Affects the binding of inhibitors. M->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10913266;Dbxref=PMID:10913266	
P56221	UniProtKB	Mutagenesis	75	75	.	.	.	Note=Affects the binding of inhibitors and reduces more than 200-fold inhibition by carpropamid. V->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10913266,ECO:0000269|PubMed:15056895;Dbxref=PMID:10913266,PMID:15056895	
P56221	UniProtKB	Mutagenesis	75	75	.	.	.	Note=Strongly reduces inhibition by carpropamid. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15382507;Dbxref=PMID:15382507	
P56221	UniProtKB	Mutagenesis	85	85	.	.	.	Note=Greatly decreases catalytic efficiency and decreases binding to salicylamide inhibitors. H->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10320327,ECO:0000269|PubMed:10636235;Dbxref=PMID:10320327,PMID:10636235	
P56221	UniProtKB	Mutagenesis	110	110	.	.	.	Note=Causes a 250-fold decrease of activity and a 6-fold increase in Km with scytalone as the substrate%2C decreases binding of salicylamide inhibitors%2C and has significantly higher relative substrate specificities (DDBO/vermelone). H->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10320327,ECO:0000269|PubMed:10636235,ECO:0000269|PubMed:11790103;Dbxref=PMID:10320327,PMID:10636235,PMID:11790103	
P56221	UniProtKB	Mutagenesis	129	129	.	.	.	Note=Results in a 80-fold decrease of activity and a 7-fold increase in Km with scytalone as the substrate. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10320327;Dbxref=PMID:10320327	
P56221	UniProtKB	Mutagenesis	129	129	.	.	.	Note=Results in a 120-fold decrease of activity and a 23-fold increase in Km with scytalone as the substrate. S->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10320327;Dbxref=PMID:10320327	
P56221	UniProtKB	Mutagenesis	131	131	.	.	.	Note=Decreases turnover by nearly 90-fold and increases Km 8-fold with scytalone as the substrate%2C decreases strongly binding of salicylamide inhibitors%2C and has significantly higher relative substrate specificities (DDBO/vermelone). N->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10320327,ECO:0000269|PubMed:10636235,ECO:0000269|PubMed:11790103;Dbxref=PMID:10320327,PMID:10636235,PMID:11790103	
P56221	UniProtKB	Mutagenesis	158	158	.	.	.	Note=Affects the binding of inhibitors. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10913266;Dbxref=PMID:10913266	
P56221	UniProtKB	Mutagenesis	162	162	.	.	.	Note=Affects the binding of inhibitors. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10913266;Dbxref=PMID:10913266	
P56221	UniProtKB	Helix	13	32	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1IDP	
P56221	UniProtKB	Helix	35	39	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1IDP	
P56221	UniProtKB	Beta strand	42	49	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1IDP	
P56221	UniProtKB	Helix	51	54	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1IDP	
P56221	UniProtKB	Beta strand	57	62	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1IDP	
P56221	UniProtKB	Helix	63	71	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1IDP	
P56221	UniProtKB	Turn	73	76	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1IDP	
P56221	UniProtKB	Beta strand	81	83	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1IDP	
P56221	UniProtKB	Beta strand	86	96	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1IDP	
P56221	UniProtKB	Beta strand	99	115	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1IDP	
P56221	UniProtKB	Beta strand	121	138	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1IDP	
P56221	UniProtKB	Beta strand	141	155	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1IDP	
P56221	UniProtKB	Helix	158	161	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3STD	
P56221	UniProtKB	Helix	163	169	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3STD