Detail Information for IndEnz0001000193
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;