| IED ID | IndEnz0001000459 |
| Enzyme Type ID | amylase000459 |
| Protein Name |
Cyclomaltodextrin glucanotransferase EC 2.4.1.19 Cyclodextrin-glycosyltransferase CGTase |
| Gene Name | cgt |
| Organism | Niallia circulans (Bacillus circulans) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Niallia Niallia circulans (Bacillus circulans) |
| Enzyme Sequence | MKKFLKSTAALALGLSLTFGLFSPAQAAPDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFDGTCTNLRLYCGGDWQGIINKINDGYLTGMGVTAIWISQPVENIYSIINYSGVNNTAYHGYWARDFKKTNPAYGTIADFQNLIAAAHAKNIKVIIDFAPNHTSPASSDQPSFAENGRLYDNGTLLGGYTNDTQNLFHHNGGTDFSTTENGIYKNLYDLADLNHNNSTVDVYLKDAIKMWLDLGIDGIRMDAVKHMPFGWQKSFMAAVNNYKPVFTFGEWFLGVNEVSPENHKFANESGMSLLDFRFAQKVRQVFRDNTDNMYGLKAMLEGSAADYAQVDDQVTFIDNHDMERFHASNANRRKLEQALAFTLTSRGVPAIYYGTEQYMSGGTDPDNRARIPSFSTSTTAYQVIQKLAPLRKCNPAIAYGSTQERWINNDVLIYERKFGSNVAVVAVNRNLNAPASISGLVTSLPQGSYNDVLGGLLNGNTLSVGSGGAASNFTLAAGGTAVWQYTAATATPTIGHVGPMMAKPGVTITIDGRGFGSSKGTVYFGTTAVSGADITSWEDTQIKVKIPAVAGGNYNIKVANAAGTASNVYDNFEVLSGDQVSVRFVVNNATTALGQNVYLTGSVSELGNWDPAKAIGPMYNQVVYQYPNWYYDVSVPAGKTIEFKFLKKQGSTVTWEGGSNHTFTAPSSGTATINVNWQP |
| Enzyme Length | 713 |
| Uniprot Accession Number | P43379 |
| Absorption | |
| Active Site | ACT_SITE 256; /note=Nucleophile; ACT_SITE 284; /note=Proton donor |
| Activity Regulation | |
| Binding Site | BINDING 167; /note=Substrate; BINDING 254; /note=Substrate; BINDING 354; /note=Substrate; 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; Evidence={ECO:0000269|PubMed:7493956}; |
| 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 (12); Mutagenesis (3); Region (10); 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..27; /evidence=ECO:0000269|PubMed:8107143 |
| Structure 3D | X-ray crystallography (24) |
| Cross Reference PDB | 1CDG; 1CGV; 1CGW; 1CGX; 1CGY; 1CXE; 1CXF; 1CXH; 1CXI; 1CXK; 1CXL; 1D3C; 1DTU; 1EO5; 1EO7; 1KCK; 1KCL; 1OT1; 1OT2; 1PEZ; 1PJ9; 1TCM; 2CXG; 2DIJ; |
| Mapped Pubmed ID | 10574960; 10686101; 10869182; 11696539; 12706817; 12809508; 14705029; 7880832; 9860832; |
| Motif | |
| Gene Encoded By | |
| Mass | 77,309 |
| 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; METAL 342; /note=Calcium 3; via carbonyl oxygen; METAL 604; /note=Calcium 3 |
| Rhea ID | |
| Cross Reference Brenda | 2.4.1.19; |