Detail Information for IndEnz0001000867
IED ID IndEnz0001000867
Enzyme Type ID amylase000867
Protein Name Glycogen debranching enzyme
EC 3.2.1.196
Limit dextrin alpha-1,6-maltotetraose-hydrolase
Gene Name glgX EC55989_3841
Organism Escherichia coli (strain 55989 / EAEC)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain 55989 / EAEC)
Enzyme Sequence MTQLAIGKPAPLGAHYDGQGVNFTLFSAHAERVELCVFDANGQEHRYDLPGHSGDIWHGYLPDARPGLRYGYRVHGPWQPAEGHRFNPAKLLIDPCARQIEGEFKDNPLLHAGHNEPDYRDNAAIAPKCVVVVDHYDWEDDAPPRTPWGSTIIYEAHVKGLTYLHPEIPVEIRGTYKALGHPVMINYLKQLGITALELLPVAQFASEPRLQRMGLSNYWGYNPVAMFALHPAYACSPETALDEFRDAIKALHKAGIEVILDIVLNHSAELDLDGPLFSLRGIDNRSYYWIREDGDYHNWTGCGNTLNLSHPAVVDYASACLRYWVETCHVDGFRFDLAAVMGRTPEFRQDAPLFTAIQNCPVLSQVKLIAEPWDIAPGGYQVGNFPPLFAEWNDHFRDAARRFWLHYDLPLGAFAGRFAASSDVFKRNGRLPSAAINLVTAHDGFTLRDCVCFNHKHNEANGEENRDGTNNNYSNNHGKEGLGGSLDLVERRRDSIHALLTTLLLSQGTPMLLAGDEHGHSQHGNNNAYCQDNQLTWLDWSQASSGLTAFTAALIHLRKRIPALVENRWWEEGDGNVRWLNRYAQPLSTDEWQNGPKQLQILLSDRFLIAINATLEVTEIVLPAGEWHAIPPFAGEDNPVITAVWQGPAHGLCVFQR
Enzyme Length 657
Uniprot Accession Number B7L4W3
Absorption
Active Site ACT_SITE 336; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_01248; ACT_SITE 371; /note=Proton donor; /evidence=ECO:0000255|HAMAP-Rule:MF_01248
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages to branches with degrees of polymerization of three or four glucose residues in limit dextrin.; EC=3.2.1.196; Evidence={ECO:0000255|HAMAP-Rule:MF_01248};
DNA Binding
EC Number 3.2.1.196
Enzyme Function FUNCTION: Removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin. {ECO:0000255|HAMAP-Rule:MF_01248}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan degradation; glycogen degradation. {ECO:0000255|HAMAP-Rule:MF_01248}.
nucleotide Binding
Features Active site (2); Chain (1); Compositional bias (1); Region (1); Site (1)
Keywords Carbohydrate metabolism;Glycogen metabolism;Glycosidase;Hydrolase
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 73,591
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda