##gff-version 3
P0A955	UniProtKB	Chain	1	213	.	.	.	ID=PRO_0000201037;Note=KHG/KDPG aldolase	
P0A955	UniProtKB	Active site	45	45	.	.	.	Note=Proton acceptor	
P0A955	UniProtKB	Active site	49	49	.	.	.	.	
P0A955	UniProtKB	Active site	133	133	.	.	.	Note=Schiff-base intermediate with substrate	
P0A955	UniProtKB	Binding site	8	9	.	.	.	.	
P0A955	UniProtKB	Binding site	49	49	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16403639;Dbxref=PMID:16403639	
P0A955	UniProtKB	Binding site	73	73	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16403639;Dbxref=PMID:16403639	
P0A955	UniProtKB	Binding site	133	133	.	.	.	Note=Covalent;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16403639;Dbxref=PMID:16403639	
P0A955	UniProtKB	Binding site	161	161	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16403639;Dbxref=PMID:16403639	
P0A955	UniProtKB	Binding site	163	163	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16403639;Dbxref=PMID:16403639	
P0A955	UniProtKB	Binding site	184	184	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16403639;Dbxref=PMID:16403639	
P0A955	UniProtKB	Site	161	161	.	.	.	Note=Plays a major role in determining the stereoselectivity	
P0A955	UniProtKB	Mutagenesis	45	45	.	.	.	Note=50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity. E->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16403639,ECO:0000269|PubMed:17981470;Dbxref=PMID:16403639,PMID:17981470	
P0A955	UniProtKB	Mutagenesis	133	133	.	.	.	Note=Absence of aldolase activity. Shows a markedly altered substrate specificity relative to the wild-type%2C with an enhanced activity against pyridine carboxaldehyde%2C benzaldehyde%2C and alpha-ketobutyrate%3B when associated with k-161. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11342129;Dbxref=PMID:11342129	
P0A955	UniProtKB	Mutagenesis	161	161	.	.	.	Note=Shows activity significantly greater than wild-type. Shows a markedly altered substrate specificity relative to the wild-type%2C with an enhanced activity against pyridine carboxaldehyde%2C benzaldehyde%2C and alpha-ketobutyrate%3B when associated with Q-133. T->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11342129,ECO:0000269|PubMed:17981470;Dbxref=PMID:11342129,PMID:17981470	
P0A955	UniProtKB	Mutagenesis	161	161	.	.	.	Note=Little stereoselectivity%2C accepting KDPG and KDPGal as substrate with roughly equal efficacy. It strongly diminishes the activity against KDPG and slightly increases activity against KDPGal. T->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11342129,ECO:0000269|PubMed:17981470;Dbxref=PMID:11342129,PMID:17981470	
P0A955	UniProtKB	Mutagenesis	168	168	.	.	.	Note=Shows activity significantly greater than wild-type. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11342129;Dbxref=PMID:11342129	
P0A955	UniProtKB	Helix	8	13	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Beta strand	16	21	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Helix	26	28	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Helix	29	38	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Beta strand	43	48	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Helix	53	63	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Beta strand	67	73	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Helix	77	86	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Beta strand	91	95	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Helix	98	106	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Beta strand	107	109	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Beta strand	111	117	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Helix	118	126	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Beta strand	131	134	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Turn	135	141	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Helix	142	150	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Beta strand	157	163	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Turn	166	168	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Helix	169	173	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Beta strand	181	183	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Helix	184	186	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Helix	189	194	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH	
P0A955	UniProtKB	Helix	197	210	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1WBH