Detail Information for IndEnz0001000462
IED ID IndEnz0001000462
Enzyme Type ID amylase000462
Protein Name Cyclomaltodextrin glucanotransferase
EC 2.4.1.19
Cyclodextrin-glycosyltransferase
CGTase
Gene Name cgt
Organism Bacillus ohbensis
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus ohbensis
Enzyme Sequence MKNLTVLLKTIPLALLLFILLSLPTAAQADVTNKVNYTRDVIYQIVTDRFSDGDPSNNPTGAIYSQDCSDLHKYCGGDWQGIIDKINDGYLTDLGITAIWISQPVENVYALHPSGYTSYHGYWARDYKRTNPFYGDFSDFDRLMDTAHSNGIKVIMDFTPNHSSPALETDPSYAENGAVYNDGVLIGNYSNDPNNLFHHNGGTDFSSYEDSIYRNLYDLADYDLNNTVMDQYLKESIKLWLDKGIDGIRVDAVKHMSEGWQTSLMSDIYAHEPVFTFGEWFLGSGEVDPQNHHFANESGMSLLDFQFGQTIRDVLMDGSSNWYDFNEMIASTEEDYDEVIDQVTFIDNHDMSRFSFEQSSNRHTDIALAVLLTSRGVPTIYYGTEQYLTGGNDPENRKPMSDFDRTTNSYQIISTLASLRQNNPALGYGNTSERWINSDVYIYERSFGDSVVLTAVNSGDTSYTINNLNTSLPQGQYTDELQQLLDGNEITVNSNGAVDSFQLSANGVSVWQITEEHASPLIGHVGPMMGKHGNTVTITGEGFGDNEGSVLFDSDFSDVLSWSDTKIEVSVPDVTAGHYDISVVNAGDSQSPTYDKFEVLTGDQVSIRFAVNNATTSLGTNLYMVGNVNELGNWDPDQAIGPMFNQVMYQYPTWYYDISVPAEENLEYKFIKKDSSGNVVWESGNNHTYTTPATGTDTVLVDWQ
Enzyme Length 704
Uniprot Accession Number P27036
Absorption
Active Site ACT_SITE 251; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 279; /note=Proton donor; /evidence=ECO:0000250
Activity Regulation
Binding Site BINDING 162; /note=Substrate; /evidence=ECO:0000250; BINDING 249; /note=Substrate; /evidence=ECO:0000250; BINDING 349; /note=Substrate; /evidence=ECO:0000250; BINDING 393; /note=Substrate; /evidence=ECO:0000250; BINDING 397; /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); Binding site (5); Chain (1); Disulfide bond (1); Domain (2); Metal binding (9); Region (3); Signal peptide (1); Site (1)
Keywords Calcium;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..29
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 78,621
Kinetics
Metal Binding METAL 52; /note=Calcium 1; /evidence=ECO:0000250; METAL 57; /note=Calcium 1; /evidence=ECO:0000250; METAL 58; /note=Calcium 1; /evidence=ECO:0000250; METAL 76; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 78; /note=Calcium 1; /evidence=ECO:0000250; METAL 161; /note=Calcium 2; /evidence=ECO:0000250; METAL 212; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 221; /note=Calcium 2; /evidence=ECO:0000250; METAL 255; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda 2.4.1.19;