IED ID | IndEnz0001000060 |
Enzyme Type ID | amylase000060 |
Protein Name |
Oligo-1,6-glucosidase IMA1 EC 3.2.1.10 Alpha-glucosidase Isomaltase 1 |
Gene Name | IMA1 YGR287C |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Enzyme Sequence | MTISSAHPETEPKWWKEATFYQIYPASFKDSNDDGWGDMKGIASKLEYIKELGADAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCSSEHEWFKESRSSKTNPKRDWFFWRPPKGYDAEGKPIPPNNWKSYFGGSAWTFDEKTQEFYLRLFCSTQPDLNWENEDCRKAIYESAVGYWLDHGVDGFRIDVGSLYSKVVGLPDAPVVDKNSTWQSSDPYTLNGPRIHEFHQEMNQFIRNRVKDGREIMTVGEMQHASDETKRLYTSASRHELSELFNFSHTDVGTSPLFRYNLVPFELKDWKIALAELFRYINGTDCWSTIYLENHDQPRSITRFGDDSPKNRVISGKLLSVLLSALTGTLYVYQGQELGQINFKNWPVEKYEDVEIRNNYNAIKEEHGENSEEMKKFLEAIALISRDHARTPMQWSREEPNAGFSGPSAKPWFYLNDSFREGINVEDEIKDPNSVLNFWKEALKFRKAHKDITVYGYDFEFIDLDNKKLFSFTKKYNNKTLFAALNFSSDATDFKIPNDDSSFKLEFGNYPKKEVDASSRTLKPWEGRIYISE |
Enzyme Length | 589 |
Uniprot Accession Number | P53051 |
Absorption | |
Active Site | ACT_SITE 215; /note=Nucleophile; ACT_SITE 277; /note=Proton donor |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.; EC=3.2.1.10; |
DNA Binding | |
EC Number | 3.2.1.10 |
Enzyme Function | FUNCTION: Major isomaltase (alpha-1,6-glucosidase) required for isomaltose utilization. Preferentially hydrolyzes isomaltose, palatinose, and methyl-alpha-glucoside, with little activity towards isomaltotriose or longer oligosaccharides. Does not hydrolyze maltose. {ECO:0000269|PubMed:15291818, ECO:0000269|PubMed:20562106}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (23); Chain (1); Helix (29); Initiator methionine (1); Mutagenesis (4); Sequence conflict (1); Site (1); Turn (7) |
Keywords | 3D-structure;Direct protein sequencing;Glycosidase;Hydrolase;Maltose metabolism;Mitochondrion;Reference proteome |
Interact With | P39940 |
Induction | INDUCTION: Expression is increased in response to the addition of maltose, isomaltose, and alpha-methylglucopyranoside. {ECO:0000269|PubMed:20562106}. |
Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14576278}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (5) |
Cross Reference PDB | 3A47; 3A4A; 3AJ7; 3AXH; 3AXI; |
Mapped Pubmed ID | 10466139; 16606443; 16702403; 16823961; 17665192; 20443596; 20471265; 20518737; 20886742; 21216897; 21535483; 21925939; 21998701; 22416705; 22448915; 23239941; 24453942; 24465730; 24649402; |
Motif | |
Gene Encoded By | |
Mass | 68,592 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.2.1.10; |