DB code: T00062

RLCP classification 1.30.36000.3 : Hydrolysis
CATH domain 3.20.20.80 : TIM Barrel Catalytic domain
3.90.400.10 : Oligo-1,6-glucosidase; domain 2
2.60.40.1180 : Immunoglobulin-like
E.C. 3.2.1.10
CSA 1uok
M-CSA 1uok
MACiE M0285

CATH domain Related DB codes (homologues)
2.60.40.1180 : Immunoglobulin-like M00113 T00307 D00165 D00176 D00664 D00665 D00863 D00864 M00112 M00193 M00314 T00057 T00067
3.20.20.80 : TIM Barrel S00202 S00210 S00748 S00906 S00907 S00911 S00912 S00915 M00134 M00160 D00479 S00204 S00205 S00206 S00207 S00203 S00208 S00209 S00211 S00213 S00214 M00113 T00307 D00165 D00166 D00169 D00176 D00501 D00502 D00503 D00844 D00861 D00864 M00026 M00112 M00193 M00346 T00057 T00063 T00066 T00067

Uniprot Enzyme Name
UniprotKB Protein name Synonyms CAZy Pfam
P21332 Oligo-1,6-glucosidase
EC 3.2.1.10
Dextrin 6-alpha-D-glucanohydrolase
Oligosaccharide alpha-1,6-glucosidase
Sucrase-isomaltase
Isomaltase
GH13 (Glycoside Hydrolase Family 13)
PF00128 (Alpha-amylase)
[Graphical View]

KEGG enzyme name
oligo-1,6-glucosidase
limit dextrinase (erroneous)
isomaltase
sucrase-isomaltase
exo-oligo-1,6-glucosidase
dextrin 6alpha-glucanohydrolase
alpha-limit dextrinase
dextrin 6-glucanohydrolase
oligosaccharide alpha-1,6-glucohydrolase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P21332 O16G_BACCE Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose. Cytoplasm.

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

Compound table
Substrates Products Intermediates
KEGG-id C00252 C00001 C00031
E.C.
Compound Isomaltose H2O D-Glucose
Type polysaccharide H2O carbohydrate
ChEBI 28189
15377
4167
PubChem 439193
22247451
962
5793
1uokA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1uokA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1uokA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P21332 & literature [4], [9]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1uokA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 199;GLU 255;ASP 329
1uokA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1uokA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
p.678-679
[7]
p.145-146
[8]
Fig. 2, p.4

References
[1]
Resource
Comments
Medline ID
PubMed ID 1915879
Journal FEBS Lett
Year 1991
Volume 290
Pages 221-3
Authors Watanabe K, Kitamura K, Hata Y, Katsube Y, Suzuki Y
Title Overproduction, purification and crystallization of Bacillus cereus oligo-1,6-glucosidase.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 1761534
Journal J Biol Chem
Year 1991
Volume 266
Pages 24287-94
Authors Watanabe K, Chishiro K, Kitamura K, Suzuki Y
Title Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 1555585
Journal Eur J Biochem
Year 1992
Volume 205
Pages 249-56
Authors Suzuki Y, Yonezawa K, Hattori M, Takii Y
Title Assignment of Bacillus thermoamyloliquefaciens KP1071 alpha-glucosidase I to an exo-alpha-1,4-glucosidase, and its striking similarity to bacillary oligo-1,6-glucosidases in N-terminal sequence and in structural parameters calculated from the amino acid composition.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID 93380886
PubMed ID 8370659
Journal J Biochem (Tokyo)
Year 1993
Volume 113
Pages 646-9
Authors Kizaki H, Hata Y, Watanabe K, Katsube Y, Suzuki Y
Title Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 A resolution X-ray analysis.
Related PDB
Related UniProtKB P21332
[5]
Resource
Comments
Medline ID
PubMed ID 8001545
Journal Eur J Biochem
Year 1994
Volume 226
Pages 277-83
Authors Watanabe K, Masuda T, Ohashi H, Mihara H, Suzuki Y
Title Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8787404
Journal Appl Environ Microbiol
Year 1996
Volume 62
Pages 2066-73
Authors Watanabe K, Kitamura K, Suzuki Y
Title Analysis of the critical sites for protein thermostabilization by proline substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC 7050 and the evolutionary consideration of proline residues.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID 97336211
PubMed ID 9193006
Journal J Mol Biol
Year 1997
Volume 269
Pages 142-53
Authors Watanabe K, Hata Y, Kizaki H, Katsube Y, Suzuki Y
Title The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: structural characterization of proline-substitution sites for protein thermostabilization.
Related PDB 1uok
Related UniProtKB P21332
[8]
Resource
Comments
Medline ID
PubMed ID 11257505
Journal Biochim Biophys Acta
Year 2001
Volume 1546
Pages 1-20
Authors MacGregor EA, Janecek S, Svensson B
Title Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 11676021
Journal Biosci Biotechnol Biochem
Year 2001
Volume 65
Pages 2058-64
Authors Watanabe K, Miyake K, Suzuki Y
Title Identification of catalytic and substrate-binding site residues in Bacillus cereus ATCC7064 oligo-1,6-glucosidase.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to glycosyl hydrolase family-13.
This enzyme must adopt a similar mechanism to that of alpha-amylase (D00165 in the EzCatDB).

Created Updated
2005-04-14 2009-02-26