3EQA

Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004339	molecular_function	glucan 1,4-alpha-glucosidase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0005976	biological_process	polysaccharide metabolic process

Functional Information from PROSITE/UniProt

site_id	PS00820
Number of Residues	11
Details	GLUCOAMYLASE Glucoamylase active site region signature. TGy.DlWEEvnG

Chain	Residue	Details
A	THR197-GLY207

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10051","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10051","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Glycosylation: {"description":"O-linked (Man) serine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1983","firstPage":"529","lastPage":"544","volume":"48","journal":"Carlsberg Res. Commun.","title":"The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger.","authors":["Svensson B.","Larsen K.","Svendsen I.","Boel E."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (Man) threonine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1983","firstPage":"529","lastPage":"544","volume":"48","journal":"Carlsberg Res. Commun.","title":"The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger.","authors":["Svensson B.","Larsen K.","Svendsen I.","Boel E."]}}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1agm