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; |