9ASCO:E2E1R9

Species (Taxon ID)	Bispora sp. MEY-1. (554688)
Gene Name(s)	AgalB (ECO:0000313 with EMBL:ADN30030.1)
Protein Name(s)	Alpha-galactosidase (ECO:0000256 with RuleBase:RU361168) Melibiase (ECO:0000256 with RuleBase:RU361168)
External Links
UniProt	E2E1R9
EMBL	GU351880
mycoCLAP	MEL27B_BISSP
GO	GO:0052692 GO:0005975
Gene3D	2.60.40.1180 3.20.20.70
InterPro	IPR013785 IPR013780 IPR002241 IPR000111 IPR017853
Pfam	PF02065
PRINTS	PR00740
SUPFAM	SSF51445

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013785	F		Seeded From UniProt	complete
enables	GO:0004553	hydrolase activity, hydrolyzing O-glycosyl compounds	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002241	F		Seeded From UniProt	complete
involved_in	GO:0005975	carbohydrate metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002241	P		Seeded From UniProt	complete
enables	GO:0004557	alpha-galactosidase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.2.1.22	F		Seeded From UniProt	complete
enables	GO:0052692	raffinose alpha-galactosidase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.2.1.22	F		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0326	P		Seeded From UniProt	complete
enables	GO:0016798	hydrolase activity, acting on glycosyl bonds	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0326	F		Seeded From UniProt	complete
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References

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