| IED ID | IndEnz0001000863 |
| Enzyme Type ID | amylase000863 |
| Protein Name |
Glycogen debranching enzyme EC 3.2.1.196 Limit dextrin alpha-1,6-maltotetraose-hydrolase |
| Gene Name | glgX amyX |
| Organism | Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Pectobacteriaceae Dickeya Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi) |
| Enzyme Sequence | MGELLAGRPRPLGSHFDGEGVNFALFSSGASRVELCIFDGLREQRLPLTARTGDIWHGYLPDAQPGLCYGYRVDGAFDPSRGQRFNANKLLLDPCARQMDGWVVDDQRLHGGYHQPDPSDSAEVMPPSVVVDEHYDWQGDRLPRTPWSQTVLYEAHVRGLTRRHPGIPAAIRGTYAALAHPVMLDYLTQLGVTALELMPVQQHADEPRLQSMGLRNYWGYNTLLPFAVDNSLAASDDPLNEFRDTVRALHQAGIEVILDVVFNHSAELDVDGPTLTLRGIDNASYYWLTENGDYHNWAGCGNVLRLEHPAVLHWVIECLTFWHEVCHVDGFRFDLATILGRLPDFSSSAPFFTALRNHRSLRDCKLIAEPWDISPGGYQLGQFPAPFAEWNDRFRDDMRRFWLHGDLPIGVLARRFAASSEVFERGSRQPWASVNMLTSHDGFTLRDLVCFNHKHNDANGEQNRDGTNSNFSFNHGTEGLEADETTQARRRVSQQALLTTLLLSQGTPMLLAGDEFGNSQQGNNNAYCQDNALAWLHWDQADDALLAFTSGLIRLRRSIPALQRGRWWRDDDEDDVRWLNAQGEALTPYEWEQGTHQLQIQLSERWLLLVNATPQVSDFSLPEGEWRVAPPFSATDHLLDGQTWRGQANAVCVLVKQ |
| Enzyme Length | 657 |
| Uniprot Accession Number | Q8KR69 |
| Absorption | |
| Active Site | ACT_SITE 334; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_01248; ACT_SITE 369; /note=Proton donor; /evidence=ECO:0000255|HAMAP-Rule:MF_01248 |
| Activity Regulation | ACTIVITY REGULATION: Slightly activated by Ca(2+). Inhibited by divalent cations such as Zn(2+), Cu(2+), Fe(2+), Mg(2+), Mn(2+), but only slightly inhibited by EDTA. |
| 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 (By similarity). Hydrolyzes the alpha-1,6-glycosidic linkages in amylopectin while does not hydrolyze the alpha-1,4-glycosidic linkages in amylose. Native glycogen is a poor substrate (PubMed:11554733). {ECO:0000255|HAMAP-Rule:MF_01248, ECO:0000269|PubMed:11554733}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.; |
| 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;Cytoplasm;Direct protein sequencing;Glycogen metabolism;Glycosidase;Hydrolase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 74,152 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |