Detail Information for IndEnz0001000182
IED ID IndEnz0001000182
Enzyme Type ID amylase000182
Protein Name Cyclomaltodextrin glucanotransferase
EC 2.4.1.19
Cyclodextrin-glycosyltransferase
CGTase
Gene Name cgt
Organism Geobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Geobacillus Geobacillus stearothermophilus (Bacillus stearothermophilus)
Enzyme Sequence MRRWLSLVLSMSFVFSAIFIVSDTQKVTVEAAGNLNKVNFTSDVVYQIVVDRFVDGNTSNNPSGALFSSGCTNLRKYCGGDWQGIINKINDGYLTDMGVTAIWISQPVENVFSVMNDASGSASYHGYWARDFKKPNPFFGTLSDFQRLVDAAHAKGIKVIIDFAPNHTSPASETNPSYMENGRLYDNGTLLGGYTNDANMYFHHNGGTTFSSLEDGIYRNLFDLADLNHQNPVIDRYLKDAVKMWIDMGIDGIRMDAVKHMPFGWQKSLMDEIDNYRPVFTFGEWFLSENEVDANNHYFANESGMSLLDFRFGQKLRQVLRNNSDNWYGFNQMIQDTASAYDEVLDQVTFIDNHDMDRFMIDGGDPRKVDMALAVLLTSRGVPNIYYGTEQYMTGNGDPNNRKMMSSFNKNTRAYQVIQKLSSLRRNNPALAYGDTEQRWINGDVYVYERQFGKDVVLVAVNRSSSSNYSITGLFTALPAGTYTDQLGGLLDGNTIQVGSNGSVNAFDLGPGEVGVWAYSATESTPIIGHVGPMMGQVGHQVTIDGEGFGTNTGTVKFGTTAANVVSWSNNQIVVAVPNVSPGKYNITVQSSSGQTSAAYDNFEVLTNDQVSVRFVVNNATTNLGQNIYIVGNVYELGNWDTSKAIGPMFNQVVYSYPTWYIDVSVPEGKTIEFKFIKKDSQGNVTWESGSNHVYTTPTNTTGKIIVDWQN
Enzyme Length 711
Uniprot Accession Number P31797
Absorption
Active Site ACT_SITE 256; /note=Nucleophile; ACT_SITE 284; /note=Proton donor
Activity Regulation
Binding Site BINDING 167; /note=Substrate; /evidence=ECO:0000250; BINDING 254; /note=Substrate; /evidence=ECO:0000250; BINDING 354; /note=Substrate; /evidence=ECO:0000250; BINDING 398; /note=Substrate; /evidence=ECO:0000250; BINDING 402; /note=Substrate; /evidence=ECO:0000250
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond.; EC=2.4.1.19;
DNA Binding
EC Number 2.4.1.19
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Beta strand (40); Binding site (5); Chain (1); Disulfide bond (1); Domain (2); Helix (22); Metal binding (10); Region (9); Sequence conflict (1); Signal peptide (1); Site (1); Turn (5)
Keywords 3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Glycosyltransferase;Metal-binding;Secreted;Signal;Transferase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..31; /evidence=ECO:0000269|Ref.2
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1CYG;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 78,923
Kinetics
Metal Binding METAL 55; /note=Calcium 1; METAL 57; /note=Calcium 1; via carbonyl oxygen; METAL 60; /note=Calcium 1; METAL 61; /note=Calcium 1; METAL 79; /note=Calcium 1; via carbonyl oxygen; METAL 81; /note=Calcium 1; METAL 166; /note=Calcium 2; METAL 217; /note=Calcium 2; via carbonyl oxygen; METAL 226; /note=Calcium 2; METAL 260; /note=Calcium 2; via carbonyl oxygen
Rhea ID
Cross Reference Brenda 2.4.1.19;