| IED ID | IndEnz0001000880 |
| Enzyme Type ID | amylase000880 |
| Protein Name |
Glycogen debranching enzyme EC 3.2.1.196 Glycogen operon protein GlgX Limit dextrin alpha-1,6-maltotetraose-hydrolase |
| Gene Name | glgX glyX b3431 JW3394 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MTQLAIGKPAPLGAHYDGQGVNFTLFSAHAERVELCVFDANGQEHRYDLPGHSGDIWHGYLPDARPGLRYGYRVHGPWQPAEGHRFNPAKLLIDPCARQIDGEFKDNPLLHAGHNEPDYRDNAAIAPKCVVVVDHYDWEDDAPPRTPWGSTIIYEAHVKGLTYLHPEIPVEIRGTYKALGHPVMINYLKQLGITALELLPVAQFASEPRLQRMGLSNYWGYNPVAMFALHPAYACSPETALDEFRDAIKALHKAGIEVILDIVLNHSAELDLDGPLFSLRGIDNRSYYWIREDGDYHNWTGCGNTLNLSHPAVVDYASACLRYWVETCHVDGFRFDLAAVMGRTPEFRQDAPLFTAIQNCPVLSQVKLIAEPWDIAPGGYQVGNFPPLFAEWNDHFRDAARRFWLHYDLPLGAFAGRFAASSDVFKRNGRLPSAAINLVTAHDGFTLRDCVCFNHKHNEANGEENRDGTNNNYSNNHGKEGLGGSLDLVERRRDSIHALLTTLLLSQGTPMLLAGDEHGHSQHGNNNAYCQDNQLTWLDWSQASSGLTAFTAALIHLRKRIPALVENRWWEEGDGNVRWLNRYAQPLSTDEWQNGPKQLQILLSDRFLIAINATLEVTEIVLPAGEWHAIPPFAGEDNPVITAVWQGPAHGLCVFQR |
| Enzyme Length | 657 |
| Uniprot Accession Number | P15067 |
| Absorption | |
| Active Site | ACT_SITE 336; /note="Nucleophile"; /evidence="ECO:0000255|HAMAP-Rule:MF_01248, ECO:0000305|PubMed:20187119"; ACT_SITE 371; /note="Proton donor"; /evidence="ECO:0000255|HAMAP-Rule:MF_01248, ECO:0000305|PubMed:20187119" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by iodoacetate, p-chloromercuribenzoate, HgCl(2), cupric sulfate and ammonium sulfate. {ECO:0000269|PubMed:779849}. |
| 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, ECO:0000269|PubMed:15687211, ECO:0000269|PubMed:779849, ECO:0000269|PubMed:8576033}; |
| 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. Shows only very little activity with native glycogen. {ECO:0000269|PubMed:15687211, ECO:0000269|PubMed:779849, ECO:0000269|PubMed:8576033}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45-50 degrees Celsius. {ECO:0000269|PubMed:779849}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.6 to 6.4. {ECO:0000269|PubMed:779849}; |
| Pathway | PATHWAY: Glycan degradation; glycogen degradation. {ECO:0000255|HAMAP-Rule:MF_01248, ECO:0000269|PubMed:15687211, ECO:0000269|PubMed:779849}. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (33); Chain (1); Compositional bias (1); Erroneous termination (1); Helix (28); Region (1); Sequence conflict (1); Site (1); Turn (5) |
| Keywords | 3D-structure;Carbohydrate metabolism;Glycogen metabolism;Glycosidase;Hydrolase;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2WSK; |
| Mapped Pubmed ID | 16606699; 24561554; |
| Motif | |
| Gene Encoded By | |
| Mass | 73,577 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.196; |