Detail Information for IndEnz0001000463
IED ID IndEnz0001000463
Enzyme Type ID amylase000463
Protein Name Cyclomaltodextrin glucanotransferase
EC 2.4.1.19
Cyclodextrin-glycosyltransferase
CGTase
Gene Name cgt
Organism Bacillus sp. (strain 1-1)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus unclassified Bacillus (in: Bacteria) Bacillus sp. (strain 1-1)
Enzyme Sequence MNDLNDFLKTILLSFIFFLLLSLPTVAEADVTNKVNYSKDVIYQIVTDRFSDGNPGNNPSGAIFSQNCIDLHKYCGGDWQGIIDKINDGYLTDLGITALWISQPVENVYALHPSGYTSYHGYWARDYKKTNPYYGNFDDFDRLMSTAHSNGIKVIMDFTPNHSSPALETNPNYVENGAIYDNGALLGNYSNDQQNLFHHNGGTDFSSYEDSIYRNLYDLADYDLNNTVMDQYLKESIKFWLDKGIDGIRVDAVKHMSEGWQTSLMSEIYSHKPVFTFGEWFLGSGEVDPQNHHFANESGMSLLDFQFGQTIRNVLKDRTSNWYDFNEMITSTEKEYNEVIDQVTFIDNHDMSRFSVGSSSNRQTDMALAVLLTSRGVPTIYYGTEQYVTGGNDPENRKPLKTFDRSTNSYQIISKLASLRQTNSALGYGTTTERWLNEDIYIYERTFGNSIVLTAVNSSNSNQTITNLNTSLPQGNYTDELQQRLDGNTITVNANGAVNSFQLRANSVAVWQVSNPSTSPLIGQVGPMMGKAGNTITVSGEGFGDERGSVLFDSTSSEIISWSNTKISVKVPNVAGGYYDLSVVTAANIKSPTYKEFEVLSGNQVSVRFGVNNATTSPGTNLYIVGNVNELGNWDADKAIGPMFNQVMYQYPTWYYDISVPAGKNLEYKYIKKDQNGNVVWQSGNNRTYTSPTTGTDTVMINW
Enzyme Length 703
Uniprot Accession Number P31746
Absorption
Active Site ACT_SITE 251; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 279; /note=Proton donor; /evidence=ECO:0000250
Activity Regulation
Binding Site BINDING 162; /note=Substrate; /evidence=ECO:0000250; BINDING 249; /note=Substrate; /evidence=ECO:0000250; BINDING 349; /note=Substrate; /evidence=ECO:0000250; BINDING 393; /note=Substrate; /evidence=ECO:0000250; BINDING 397; /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
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Binding site (5); Chain (1); Disulfide bond (1); Domain (2); Metal binding (10); Region (9); Signal peptide (1); Site (1)
Keywords 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..29; /evidence=ECO:0000269|Ref.1
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 78,663
Kinetics
Metal Binding METAL 52; /note=Calcium 1; /evidence=ECO:0000250; METAL 54; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 57; /note=Calcium 1; /evidence=ECO:0000250; METAL 58; /note=Calcium 1; /evidence=ECO:0000250; METAL 76; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 78; /note=Calcium 1; /evidence=ECO:0000250; METAL 161; /note=Calcium 2; /evidence=ECO:0000250; METAL 212; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 221; /note=Calcium 2; /evidence=ECO:0000250; METAL 255; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda 2.4.1.19;