IED ID | IndEnz0001000193 |
Enzyme Type ID | amylase000193 |
Protein Name |
Cyclomaltodextrin glucanotransferase EC 2.4.1.19 Cyclodextrin-glycosyltransferase CGTase |
Gene Name | |
Organism | Niallia circulans (Bacillus circulans) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Niallia Niallia circulans (Bacillus circulans) |
Enzyme Sequence | MFQMAKRAFLSTTLTLGLLAGSALPFLPASAVYADPDTAVTNKQSFSTDVIYQVFTDRFLDGNPSNNPTGAAYDATCSNLKLYCGGDWQGLINKINDNYFSDLGVTALWISQPVENIFATINYSGVTNTAYHGYWARDFKKTNPYFGTMADFQNLITTAHAKGIKIVIDFAPNHTSPAMETDTSFAENGRLYDNGTLVGGYTNDTNGYFHHNGGSDFSSLENGIYKNLYDLADFNHNNATIDKYFKDAIKLWLDMGVDGIRVDAVKHMPLGWQKSWMSSIYAHKPVFTFGEWFLGSAASDADNTDFANKSGMSLLDFRFNSAVRNVFRDNTSNMYALDSMINSTATDYNQVNDQVTFIDNHDMDRFKTSAVNNRRLEQALAFTLTSRGVPAIYYGTEQYLTGNGDPDNRAKMPSFSKSTTAFNVISKLAPLRKSNPAIAYGSTQQRWINNDVYVYERKFGKSVAVVAVNRNLSTSASITGLSTSLPTGSYTDVLGGVLNGNNITSTNGSINNFTLAAGATAVWQYTTAETTPTIGHVGPVMGKPGNVVTIDGRGFGSTKGTVYFGTTAVTGAAITSWEDTQIKVTIPSVAAGNYAVKVAASGVNSNAYNNFTILTGDQVTVRFVVNNASTTLGQNLYLTGNVAELGNWSTGSTAIGPAFNQVIHQYPTWYYDVSVPAGKQLEFKFFKKNGSTITWESGSNHTFTTPASGTATVTVNWQ |
Enzyme Length | 718 |
Uniprot Accession Number | P30920 |
Absorption | |
Active Site | ACT_SITE 263; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 291; /note=Proton donor; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | BINDING 174; /note=Substrate; BINDING 230; /note=Substrate; BINDING 261; /note=Substrate; /evidence=ECO:0000250; BINDING 267; /note=Substrate; BINDING 361; /note=Substrate; BINDING 405; /note=Substrate; BINDING 409; /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 (7); Chain (1); Disulfide bond (1); Domain (2); Helix (22); Metal binding (10); Region (9); Signal peptide (1); Site (1); Turn (4) |
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..34 |
Structure 3D | X-ray crystallography (9) |
Cross Reference PDB | 1CGT; 1CGU; 3CGT; 4CGT; 5CGT; 6CGT; 7CGT; 8CGT; 9CGT; |
Mapped Pubmed ID | 1390660; |
Motif | |
Gene Encoded By | |
Mass | 78,047 |
Kinetics | |
Metal Binding | METAL 61; /note=Calcium 1; METAL 63; /note=Calcium 1; via carbonyl oxygen; METAL 66; /note=Calcium 1; METAL 67; /note=Calcium 1; METAL 85; /note=Calcium 1; via carbonyl oxygen; METAL 87; /note=Calcium 1; METAL 173; /note=Calcium 2; METAL 224; /note=Calcium 2; via carbonyl oxygen; METAL 233; /note=Calcium 2; METAL 267; /note=Calcium 2; via carbonyl oxygen |
Rhea ID | |
Cross Reference Brenda | 2.4.1.19; |