##gff-version 3
Q58813	UniProtKB	Chain	1	181	.	.	.	ID=PRO_0000162932;Note=L-fuculose phosphate aldolase	
Q58813	UniProtKB	Active site	68	68	.	.	.	Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AB87	
Q58813	UniProtKB	Binding site	24	25	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AB87	
Q58813	UniProtKB	Binding site	39	40	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AB87	
Q58813	UniProtKB	Binding site	66	67	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AB87	
Q58813	UniProtKB	Binding site	68	68	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AB87	
Q58813	UniProtKB	Binding site	87	87	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AB87	
Q58813	UniProtKB	Binding site	89	89	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AB87	
Q58813	UniProtKB	Binding site	147	147	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0AB87	
Q58813	UniProtKB	Mutagenesis	25	25	.	.	.	Note=It shows a 3-fold increase of the affinty for dihydroxyacetone phosphate (DHAP) and a 3-fold decrease of the affinity for DL-glyceraldehyde compared to the wild-type. N->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.2	
Q58813	UniProtKB	Mutagenesis	25	25	.	.	.	Note=It shows a 5-fold decrease of the affinty for dihydroxyacetone phosphate (DHAP)%2C but has the same affinity for DL-glyceraldehyde compared to the wild-type. N->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.2