| IED ID | IndEnz0001000196 |
| Enzyme Type ID | amylase000196 |
| Protein Name |
Cyclomaltodextrin glucanotransferase EC 2.4.1.19 Cyclodextrin-glycosyltransferase CGTase Raw-starch-digesting amylase |
| Gene Name | cgt |
| Organism | Bacillus sp. (strain B1018) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus unclassified Bacillus (in: Bacteria) Bacillus sp. (strain B1018) |
| Enzyme Sequence | MKKFLKMTAAFSLGLSLAFGLFSPAQAAPDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFDGTCTNLRLYCGGDWQGIINKINDGYLTGMGVTAIWISQPVENIYSIINYSGVNNTAYHGYWARDFKKTNPAYGTIADFQNLIAAAHAKNIKVIIDFAPNHTSPASSDQPSFAENGRLYDNGTLLGGYTNDTQNLFHHNGGTDFSTTENGIYKNLYDLADLNHNNSTSDVYLKDAIKMWLDLGIDGIRMDAVKHMPFGWQKSFMAAVNNYKPVFTFGEWFLGVNEVGPENHKFANESGMSLLDFRFAQKVRQVFRDNTDNMYGLKAMLEGSAADYAQVDDQVTFIDNHDMERFHASNANRRKLEQALAFTLILARVPAIYYGTEQYMSGGTDPDNRARIPSFSTSTTAYQVIQKLAPLRKSNPAIAYGSTQERWINNDVLIYERKFGSNVAVVAVNRNLNAPASISGLVTSLPQGSYNDVLGGLLNGNTLTVGSGGAASNFTLAAGGTAVWQYTAATATPTIGHVGPMMAKPGVTITIDGRGFGSSKGTVYFGTTAVSGANITSWEDTQIKVKIPAVAGGIYNIKVANAAGTASNVYDNFEVLSGDQVSVRFVVNNATTALGQNLYLTGNVSELGNWDPAKAIGPMYNQVVYQYPNWYYDVSVPAGKTIEFKFLKKQGSTVTWEGGSNHTFTAPSSGTATINVNWQP |
| Enzyme Length | 713 |
| Uniprot Accession Number | P17692 |
| Absorption | |
| Active Site | ACT_SITE 256; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 284; /note=Proton donor; /evidence=ECO:0000250 |
| 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; /evidence=ECO:0000250; BINDING 402; /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 | FUNCTION: This endo-type adsorbable amylase is capable to digest raw starch. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (5); Chain (1); Domain (2); Metal binding (10); Region (3); Signal peptide (1); Site (1) |
| Keywords | Calcium;Direct protein sequencing;Glycosyltransferase;Metal-binding;Secreted;Signal;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000269|PubMed:1689153 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 77,421 |
| Kinetics | |
| Metal Binding | METAL 54; /note=Calcium 1; /evidence=ECO:0000250; METAL 56; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 59; /note=Calcium 1; /evidence=ECO:0000250; METAL 60; /note=Calcium 1; /evidence=ECO:0000250; METAL 78; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 80; /note=Calcium 1; /evidence=ECO:0000250; METAL 166; /note=Calcium 2; /evidence=ECO:0000250; METAL 217; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 226; /note=Calcium 2; /evidence=ECO:0000250; METAL 260; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 2.4.1.19; |