| IED ID | IndEnz0001000458 |
| Enzyme Type ID | amylase000458 |
| Protein Name |
Cyclomaltodextrin glucanotransferase EC 2.4.1.19 Cyclodextrin-glycosyltransferase CGTase |
| Gene Name | cgt |
| Organism | Brevibacillus brevis (Bacillus brevis) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Paenibacillaceae Brevibacillus Brevibacillus brevis (Bacillus brevis) |
| Enzyme Sequence | MITPSFIISSFLSLPTVVEASVTNKVNYSKDVIYQIVTDRFSDGNPANNPSGAIFSQNCSDLHKYCGGDWQGIINKMNDGYLTDLGITALWISQPVENVYALHPSGYTSYHGYWARDYKKTNPYFGNFSDFDRLVSTAHNKGIKIIMDFTPNHSSLALETNPNYVENGALYNNGALLGNYSNDRNKLFHHNGGTDFSSYEDSIYRNLYDLADYDLNNKVVDQYLKESIKLWLIKIDGIRVDAVKHMSEGWQTSLMSDIYTYKPVFTFGEWFLGTGEVDPQNHHFANESGMSLLDFQFGQTIRSVLKDRTSNWYDFNEMIKSTEKDYDEVIDQVTFIDNHDMSRFSMVVFNFQTDIALAVLLTSRGVPTIYYGTEQYLTGGNDPDNRKPMKTFDRSTNSYKITSKLASLRQRNSALGYGNTTERWINSDVYIYERKFGNSIVLTAVNSSNRNQTISNLNTSLPQGNYTDELQQLLDGNTITVNANGSANSPQLQANSVAVWQVTKESTSPLIGHVGPMIGKTGNTVTVSGEGFGDKKGSVLFGSTSAEIVSWSNTEIQVKVPNVTAGHYNLSVVNATNTKSPAYEKFEVLSGNQVSVRFAVNNATTNSGTNVYIVGNVSELGNWDPNKAIGPMFNQVMYKYPTWYYDISVPAGKNLEYKYIKKDHNGNVTWQSGNNRTYTSPATGTDTVISNW |
| Enzyme Length | 692 |
| Uniprot Accession Number | O30565 |
| Absorption | |
| Active Site | ACT_SITE 241; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 269; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 153; /note=Substrate; /evidence=ECO:0000250; BINDING 239; /note=Substrate; /evidence=ECO:0000250; BINDING 339; /note=Substrate; /evidence=ECO:0000250; BINDING 382; /note=Substrate; /evidence=ECO:0000250; BINDING 386; /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 (10); 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..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 77,405 |
| Kinetics | |
| Metal Binding | METAL 43; /note=Calcium 1; /evidence=ECO:0000250; METAL 45; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 48; /note=Calcium 1; /evidence=ECO:0000250; METAL 49; /note=Calcium 1; /evidence=ECO:0000250; METAL 67; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 69; /note=Calcium 1; /evidence=ECO:0000250; METAL 152; /note=Calcium 2; /evidence=ECO:0000250; METAL 203; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 212; /note=Calcium 2; /evidence=ECO:0000250; METAL 245; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 2.4.1.19; |