Detail Information for IndEnz0001000183
IED ID IndEnz0001000183
Enzyme Type ID amylase000183
Protein Name Cyclomaltodextrin glucanotransferase
EC 2.4.1.19
Cyclodextrin-glycosyltransferase
CGTase
Gene Name
Organism Paenibacillus macerans (Bacillus macerans)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Paenibacillaceae Paenibacillus Paenibacillus macerans (Bacillus macerans)
Enzyme Sequence MKKQVKWLTSVSMSVGIALGAALPVWASPDTSVNNKLNFSTDTVYQIVTDRFVDGNSANNPTGAAFSSDHSNLKLYFGGDWQGITNKINDGYLTGMGITALWISQPVENITAVINYSGVNNTAYHGYWPRDFKKTNAAFGSFTDFSNLIAAAHSHNIKVVMDFAPNHTNPASSTDPSFAENGALYNNGTLLGKYSNDTAGLFHHNGGTDFSTTESGIYKNLYDLADINQNNNTIDSYLKESIQLWLNLGVDGIRFDAVKHMPQGWQKSYVSSIYSSANPVFTFGEWFLGPDEMTQDNINFANQSGMHLLDFAFAQEIREVFRDKSETMTDLNSVISSTGSSYNYINNMVTFIDNHDMDRFQQAGASTRPTEQALAVTLTSRGVPAIYYGTEQYMTGNGDPNNRGMMTGFDTNKTAYKVIKALAPLRKSNPALAYGSTTQRWVNSDVYVYERKFGSNVALVAVNRSSTTAYPISGALTALPNGTYTDVLGGLLNGNSITVNGGTVSNFTLAAGGTAVWQYTTTESSPIIGNVGPTMGKPGNTITIDGRGFGTTKNKVTFGTTAVTGANIVSWEDTEIKVKVPNVAAGNTAVTVTNAAGTTSAAFNNFNVLTADQVTVRFKVNNATTALGQNVYLTGNVAELGNWTAANAIGPMYNQVEASYPTWYFDVSVPANTALQFKFIKVNGSTVTWEGGNNHTFTSPSSGVATVTVDWQN
Enzyme Length 713
Uniprot Accession Number P31835
Absorption
Active Site ACT_SITE 256; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 285; /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 355; /note=Substrate; /evidence=ECO:0000250; BINDING 399; /note=Substrate; /evidence=ECO:0000250; BINDING 403; /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); Domain (2); Metal binding (10); Region (9); Signal peptide (1); Site (1)
Keywords Calcium;Direct protein sequencing;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|Ref.1
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 76,857
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;