| IED ID | IndEnz0001000184 |
| Enzyme Type ID | amylase000184 |
| Protein Name |
Cyclomaltodextrin glucanotransferase EC 2.4.1.19 Cyclodextrin-glycosyltransferase CGTase |
| Gene Name | cgt |
| Organism | Bacillus sp. (strain 1011) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus unclassified Bacillus (in: Bacteria) Bacillus sp. (strain 1011) |
| Enzyme Sequence | MKRFMKLTAVWTLWLSLTLGLLSPVHAAPDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFDGSCTNLRLYCGGDWQGIINKINDGYLTGMGITAIWISQPVENIYSVINYSGVNNTAYHGYWARDFKKTNPAYGTMQDFKNLIDTAHAHNIKVIIDFAPNHTSPASSDDPSFAENGRLYDNGNLLGGYTNDTQNLFHHYGGTDFSTIENGIYKNLYDLADLNHNNSSVDVYLKDAIKMWLDLGVDGIRVDAVKHMPFGWQKSFMATINNYKPVFTFGEWFLGVNEISPEYHQFANESGMSLLDFRFAQKARQVFRDNTDNMYGLKAMLEGSEVDYAQVNDQVTFIDNHDMERFHTSNGDRRKLEQALAFTLTSRGVPAIYYGSEQYMSGGNDPDNRARLPSFSTTTTAYQVIQKLAPLRKSNPAIAYGSTHERWINNDVIIYERKFGNNVAVVAINRNMNTPASITGLVTSLRRASYNDVLGGILNGNTLTVGAGGAASNFTLAPGGTAVWQYTTDATTPIIGNVGPMMAKPGVTITIDGRGFGSGKGTVYFGTTAVTGADIVAWEDTQIQVKIPAVPGGIYDIRVANAAGAASNIYDNFEVLTGDQVTVRFVINNATTALGQNVFLTGNVSELGNWDPNNAIGPMYNQVVYQYPTWYYDVSVPAGQTIEFKFLKKQGSTVTWEGGANRTFTTPTSGTATVNVNWQP |
| Enzyme Length | 713 |
| Uniprot Accession Number | P05618 |
| 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; BINDING 402; /note=Substrate |
| 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 (48); Binding site (5); Chain (1); Disulfide bond (1); Domain (2); Helix (24); Metal binding (10); Region (9); Signal peptide (1); Site (1); Turn (5) |
| Keywords | 3D-structure;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..27 |
| Structure 3D | X-ray crystallography (11) |
| Cross Reference PDB | 1D7F; 1DED; 1I75; 1PAM; 1UKQ; 1UKS; 1UKT; 1V3J; 1V3K; 1V3L; 1V3M; |
| Mapped Pubmed ID | 10679895; 10731709; 11275559; 14739329; 14769878; |
| Motif | |
| Gene Encoded By | |
| Mass | 78,340 |
| Kinetics | |
| Metal Binding | METAL 54; /note=Calcium 1; METAL 56; /note=Calcium 1; via carbonyl oxygen; METAL 59; /note=Calcium 1; METAL 60; /note=Calcium 1; METAL 78; /note=Calcium 1; via carbonyl oxygen; METAL 80; /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; |