| IED ID | IndEnz0001000829 |
| Enzyme Type ID | amylase000829 |
| Protein Name |
1,4-alpha-glucan branching enzyme GlgB EC 2.4.1.18 1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase Alpha- 1- 4 -glucan branching enzyme Glycogen-branching enzyme BE |
| Gene Name | glgB Rv1326c MTCY130.11c |
| Organism | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Enzyme Sequence | MSRSEKLTGEHLAPEPAEMARLVAGTHHNPHGILGAHEYDDHTVIRAFRPHAVEVVALVGKDRFSLQHLDSGLFAVALPFVDLIDYRLQVTYEGCEPHTVADAYRFLPTLGEVDLHLFAEGRHERLWEVLGAHPRSFTTADGVVSGVSFAVWAPNAKGVSLIGEFNGWNGHEAPMRVLGPSGVWELFWPDFPCDGLYKFRVHGADGVVTDRADPFAFGTEVPPQTASRVTSSDYTWGDDDWMAGRALRNPVNEAMSTYEVHLGSWRPGLSYRQLARELTDYIVDQGFTHVELLPVAEHPFAGSWGYQVTSYYAPTSRFGTPDDFRALVDALHQAGIGVIVDWVPAHFPKDAWALGRFDGTPLYEHSDPKRGEQLDWGTYVFDFGRPEVRNFLVANALYWLQEFHIDGLRVDAVASMLYLDYSRPEGGWTPNVHGGRENLEAVQFLQEMNATAHKVAPGIVTIAEESTPWSGVTRPTNIGGLGFSMKWNMGWMHDTLDYVSRDPVYRSYHHHEMTFSMLYAFSENYVLPLSHDEVVHGKGTLWGRMPGNNHVKAAGLRSLLAYQWAHPGKQLLFMGQEFGQRAEWSEQRGLDWFQLDENGFSNGIQRLVRDINDIYRCHPALWSLDTTPEGYSWIDANDSANNVLSFMRYGSDGSVLACVFNFAGAEHRDYRLGLPRAGRWREVLNTDATIYHGSGIGNLGGVDATDDPWHGRPASAVLVLPPTSALWLTPA |
| Enzyme Length | 731 |
| Uniprot Accession Number | P9WN45 |
| Absorption | |
| Active Site | ACT_SITE 411; /note=Nucleophile; ACT_SITE 464; /note=Proton donor |
| Activity Regulation | ACTIVITY REGULATION: Is inhibited by divalent cations such as Zn(2+) and Cu(2+), but not by Mg(2+), Mn(2+) and Ca(2+). Is not inhibited by several known inhibitors of the GH13 family such as ADP, ADP glucose, tunicamycin, castenospermine, nojirimycin, or acarbose. {ECO:0000269|PubMed:17005418, ECO:0000269|PubMed:20444687}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.; EC=2.4.1.18; Evidence={ECO:0000269|PubMed:17005418, ECO:0000269|PubMed:20444687}; |
| DNA Binding | |
| EC Number | 2.4.1.18 |
| Enzyme Function | FUNCTION: Essential enzyme that catalyzes the formation of the alpha-1,6-glucosidic linkages in glucan chains by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. Is involved in the biosynthesis of both glycogen and capsular alpha-D-glucan. {ECO:0000269|PubMed:17005418, ECO:0000269|PubMed:18808383}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. Loses 20% of its maximum activity at 37 degrees Celsius and is nearly inactive above 55 degrees Celsius. {ECO:0000269|PubMed:17005418}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:17005418}; |
| Pathway | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:18808383}.; PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis. {ECO:0000269|PubMed:18808383}. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (32); Chain (1); Disulfide bond (1); Helix (30); Turn (6) |
| Keywords | 3D-structure;Capsule biogenesis/degradation;Carbohydrate metabolism;Disulfide bond;Glycogen biosynthesis;Glycogen metabolism;Glycosyltransferase;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3K1D; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 81,729 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 2.4.1.18; |