##gff-version 3
Q8U2I1	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17419725;Dbxref=PMID:17419725	
Q8U2I1	UniProtKB	Chain	2	265	.	.	.	ID=PRO_0000415086;Note=6-oxopurine nucleoside phosphorylase	
Q8U2I1	UniProtKB	Binding site	10	10	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01963	
Q8U2I1	UniProtKB	Binding site	49	50	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01963	
Q8U2I1	UniProtKB	Binding site	82	83	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01963	
Q8U2I1	UniProtKB	Binding site	187	187	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01963	
Q8U2I1	UniProtKB	Binding site	188	188	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01963	
Q8U2I1	UniProtKB	Binding site	211	213	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01963	
Q8U2I1	UniProtKB	Site	169	169	.	.	.	Note=Important for substrate specificity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01963	
Q8U2I1	UniProtKB	Site	223	223	.	.	.	Note=Important for substrate specificity;Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_01963	
Q8U2I1	UniProtKB	Disulfide bond	136	202	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17419725;Dbxref=PMID:17419725	
Q8U2I1	UniProtKB	Disulfide bond	162	190	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17419725;Dbxref=PMID:17419725	
Q8U2I1	UniProtKB	Disulfide bond	254	256	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17419725;Dbxref=PMID:17419725	
Q8U2I1	UniProtKB	Mutagenesis	169	169	.	.	.	Note=Decreases catalytic activity for insosine and allows the enzyme to phosphorolytically cleave MTA with a catalytic efficiency about 4-fold higher than for inosine%3B when associated with D-211%2C D-213 and A-223. E->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21683167;Dbxref=PMID:21683167	
Q8U2I1	UniProtKB	Mutagenesis	211	211	.	.	.	Note=Decreases catalytic activity for insosine and allows the enzyme to phosphorolytically cleave MTA with a catalytic efficiency about 4-fold higher than for inosine%3B when associated with S-169%2C D-213 and A-223. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21683167;Dbxref=PMID:21683167	
Q8U2I1	UniProtKB	Mutagenesis	213	213	.	.	.	Note=Decreases catalytic activity for insosine and allows the enzyme to phosphorolytically cleave MTA with a catalytic efficiency about 4-fold higher than for inosine%3B when associated with S-169%2C D-211 and A-223. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21683167;Dbxref=PMID:21683167	
Q8U2I1	UniProtKB	Mutagenesis	223	223	.	.	.	Note=Decreases catalytic activity for insosine and allows the enzyme to phosphorolytically cleave MTA with a catalytic efficiency about 4-fold higher than for inosine%3B when associated with S-169%2C D-211 and D-213. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21683167;Dbxref=PMID:21683167	
Q8U2I1	UniProtKB	Mutagenesis	254	254	.	.	.	Note=Fully active%2C but reduces thermodynamic and kinetic stability of the enzyme%3B when associated with S-256. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17419725;Dbxref=PMID:17419725	
Q8U2I1	UniProtKB	Mutagenesis	256	256	.	.	.	Note=Fully active%2C but reduces thermodynamic and kinetic stability of the enzyme%3B when associated with S-254. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17419725;Dbxref=PMID:17419725