Detail Information for IndEnz0001000060
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;