1J0Z

Beta-amylase from Bacillus cereus var. mycoides in complex with maltose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0005976	biological_process	polysaccharide metabolic process
A	0016161	molecular_function	beta-amylase activity
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0046872	molecular_function	metal ion binding
A	2001070	molecular_function	starch binding
B	0000272	biological_process	polysaccharide catabolic process
B	0005976	biological_process	polysaccharide metabolic process
B	0016161	molecular_function	beta-amylase activity
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0046872	molecular_function	metal ion binding
B	2001070	molecular_function	starch binding
C	0000272	biological_process	polysaccharide catabolic process
C	0005976	biological_process	polysaccharide metabolic process
C	0016161	molecular_function	beta-amylase activity
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0046872	molecular_function	metal ion binding
C	2001070	molecular_function	starch binding
D	0000272	biological_process	polysaccharide catabolic process
D	0005976	biological_process	polysaccharide metabolic process
D	0016161	molecular_function	beta-amylase activity
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0046872	molecular_function	metal ion binding
D	2001070	molecular_function	starch binding

Functional Information from PROSITE/UniProt

site_id	PS00506
Number of Residues	9
Details	BETA_AMYLASE_1 Beta-amylase active site 1. HqCGGNVGD

Chain	Residue	Details
A	HIS89-ASP97

---

site_id	PS00679
Number of Residues	11
Details	BETA_AMYLASE_2 Beta-amylase active site 2. GpAGELRYPSY

Chain	Residue	Details
A	GLY168-TYR178

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	408
Details	Domain: {"description":"CBM20","evidences":[{"source":"PROSITE-ProRule","id":"PRU00594","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10050","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10353816","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12761294","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"10353816","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12761294","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10353816","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12761294","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10353816","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP97
A	GLU172

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1bya

Chain	Residue	Details
B	ASP97
B	GLU172

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1bya

Chain	Residue	Details
C	ASP97
C	GLU172

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1bya

Chain	Residue	Details
D	ASP97
D	GLU172

---