DB code: S00048

CATH domain 1.50.10.10 : Glycosyltransferase Catalytic domain
E.C. 3.2.1.3
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
1.50.10.10 : Glycosyltransferase S00531 S00845 D00167 D00500 M00192 T00245 T00246

Uniprot Enzyme Name
UniprotKB Protein name Synonyms CAZy Pfam
P08017 Glucoamylase GLU1
EC 3.2.1.3
Glucan 1,4-alpha-glucosidase
1,4-alpha-D-glucan glucohydrolase
GH15 (Glycoside Hydrolase Family 15)
PF00723 (Glyco_hydro_15)
[Graphical View]

KEGG enzyme name
glucan 1,4-alpha-glucosidase
glucoamylase
amyloglucosidase
gamma-amylase
lysosomal alpha-glucosidase
acid maltase
exo-1,4-alpha-glucosidase
glucose amylase
gamma-1,4-glucan glucohydrolase
acid maltase
1,4-alpha-D-glucan glucohydrolase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P08017 AMYG_SACFI Hydrolysis of terminal (1->4)-linked alpha-D- glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.

KEGG Pathways
Map code Pathways E.C.
MAP00500 Starch and sucrose metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00718 C00001 C00718 C00221
E.C.
Compound Amylose H2O Amylose beta-D-Glucose
Type polysaccharide H2O polysaccharide carbohydrate
ChEBI 15377
 15377
 		15903
 15903
PubChem 22247451
 962
 22247451
 962
 		64689
 64689
1ayxA Unbound Unbound Analogue:TRS

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ayxA TYR 63;GLU 210;GLU 456

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[5]
p.862-864
[7]
Fig.5, p.279-280

References
[1]
Resource
Comments
Medline ID
PubMed ID 7937705
Journal Protein Eng
Year 1994
Volume 7
Pages 749-60
Authors Coutinho PM, Reilly PJ
Title Structural similarities in glucoamylase by hydrophobic cluster analysis.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 8177888
Journal Protein Eng
Year 1994
Volume 7
Pages 393-400
Authors Coutinho PM, Reilly PJ
Title Structure-function relationships in the catalytic and starch binding domains of glucoamylase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8713124
Journal Biochem Biophys Res Commun
Year 1996
Volume 224
Pages 790-5
Authors Solovicova A, Gasperik J, Hostinova E
Title High-yield production of Saccharomycopsis fibuligera glucoamylase in Escherichia coli, refolding, and comparison of the nonglycosylated and glycosylated enzyme forms.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 9365988
Journal Proteins
Year 1997
Volume 29
Pages 334-47
Authors Coutinho PM, Reilly PJ
Title Glucoamylase structural, functional, and evolutionary relationships.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
Medline ID 98437615
PubMed ID 9757101
Journal Acta Crystallogr D Biol Crystallogr
Year 1998
Volume 54
Pages 854-66
Authors Sevcik J, Solovicova A, Hostinova E, Gasperik J, Wilson KS, Dauter Z
Title Structure of glucoamylase from Saccharomycopsis fibuligera at 1.7 A resolution.
Related PDB 1ayx
Related UniProtKB P08017
[6]
Resource
Comments
Medline ID
PubMed ID 10491121
Journal Eur J Biochem
Year 1999
Volume 264
Pages 756-64
Authors Solovicova A, Christensen T, Hostinova E, Gasperik J, Sevcik J, Svensson B
Title Structure-function relationships in glucoamylases encoded by variant Saccharomycopsis fibuligera genes.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 11150611
Journal Biochim Biophys Acta
Year 2000
Volume 1543
Pages 275-93
Authors Sauer J, Sigurskjold BW, Christensen U, Frandsen TP, Mirgorodskaya E, Harrison M, Roepstorff P, Svensson B
Title Glucoamylase: structure/function relationships, and protein engineering.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 12623067
Journal Arch Biochem Biophys
Year 2003
Volume 411
Pages 189-95
Authors Hostinova E, Solovicova A, Dvorsky R, Gasperik J
Title Molecular cloning and 3D structure prediction of the first raw-starch-degrading glucoamylase without a separate starch-binding domain.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 15963591
Journal J Biotechnol
Year 2005
Volume 118
Pages 167-76
Authors Latorre-Garcia L, Adam AC, Manzanares P, Polaina J
Title Improving the amylolytic activity of Saccharomyces cerevisiae glucoamylase by the addition of a starch binding domain.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the glycosidase family-15, with an inverting mechanism.
According to the literature [5] & [7], the catalytic mechanism seems to be similar to that of beta-amylase (D00166 in EzCatDB). Glu210 and Glu456 act as a general acid and a general base, respectively.

Created Updated
2004-07-09 2009-03-16