##gff-version 3
P94522	UniProtKB	Signal peptide	1	32	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15556708;Dbxref=PMID:15556708	
P94522	UniProtKB	Chain	33	323	.	.	.	ID=PRO_0000360437;Note=Extracellular endo-alpha-(1->5)-L-arabinanase 1	
P94522	UniProtKB	Active site	44	44	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15708971;Dbxref=PMID:15708971	
P94522	UniProtKB	Active site	215	215	.	.	.	Note=Proton donor;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15708971;Dbxref=PMID:15708971	
P94522	UniProtKB	Binding site	44	44	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P94522	UniProtKB	Binding site	107	107	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P94522	UniProtKB	Binding site	125	125	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P94522	UniProtKB	Binding site	160	163	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P94522	UniProtKB	Binding site	165	165	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P94522	UniProtKB	Binding site	180	182	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P94522	UniProtKB	Binding site	287	287	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P94522	UniProtKB	Site	163	163	.	.	.	Note=Important for catalytic activity%2C responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15708971;Dbxref=PMID:15708971	
P94522	UniProtKB	Mutagenesis	43	43	.	.	.	Note=Decrease in binding affinity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15708971;Dbxref=PMID:15708971	
P94522	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Loss of arabinanase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15708971;Dbxref=PMID:15708971	
P94522	UniProtKB	Mutagenesis	104	104	.	.	.	Note=Significantly less active (10000-fold) than the wild-type arabinanase against both linear arabinan and arabinooligosaccharides. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15708971;Dbxref=PMID:15708971	
P94522	UniProtKB	Mutagenesis	124	124	.	.	.	Note=Increase in binding affinity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15708971;Dbxref=PMID:15708971	
P94522	UniProtKB	Mutagenesis	163	163	.	.	.	Note=Loss of arabinanase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15708971;Dbxref=PMID:15708971	
P94522	UniProtKB	Mutagenesis	181	181	.	.	.	Note=Significantly less active than the wild-type arabinanase against both linear arabinan (50-fold) and the arabinooligosaccharides (1000-fold). F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15708971;Dbxref=PMID:15708971	
P94522	UniProtKB	Mutagenesis	182	182	.	.	.	Note=Same binding affinity as wild-type. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15708971;Dbxref=PMID:15708971	
P94522	UniProtKB	Mutagenesis	215	215	.	.	.	Note=Loss of arabinanase activity. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15556708,ECO:0000269|PubMed:15708971;Dbxref=PMID:15556708,PMID:15708971	
P94522	UniProtKB	Sequence conflict	172	172	.	.	.	Note=G->D;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P94522	UniProtKB	Beta strand	34	41	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	46	50	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	53	59	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	64	77	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	79	84	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Helix	90	94	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	104	111	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	114	121	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	129	137	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Turn	139	142	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	145	153	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	157	159	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	165	168	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	174	178	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	185	190	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Turn	192	194	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	196	205	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Turn	208	212	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	214	222	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	225	233	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	235	239	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	242	252	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Helix	265	267	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	271	274	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	278	289	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Turn	290	292	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	293	300	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Turn	301	305	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4	
P94522	UniProtKB	Beta strand	307	313	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UV4