| IED ID | IndEnz0001000274 |
| Enzyme Type ID | amylase000274 |
| Protein Name |
1,4-alpha-glucan branching enzyme TK1436 EC 2.4.1.18 1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase Alpha- 1- 4 -glucan branching enzyme Branching enzyme BE |
| Gene Name | TK1436 |
| Organism | Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Thermococcus Thermococcus kodakarensis Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
| Enzyme Sequence | MKGYLTFVLHTHIPYVRKHGKWPFGEEWVFEAISETYIPLLMEFERLRDSGVKFGIVINVTPVLAEQLTDEYMKKAFEEYMERKLKAMEEDLKSGKYDEKAVSYMLNYFRKVYDYWKAINGDIIGKLRELQDQGYVEVITSAATHGYLPLLGRDEAIRAQIANGVATYEKHFGMKPKGIWLPECAYRPAGEWELPGGRKVKRQGIEKFLEEFGLRYFFVESRLIDEGPASNVYGEVLIADTEKTTLRPYWIKGSNVAVFARNRETGHQVWSAHYGYPGDFWYREFHKKAPKSGGQYWRITSKEVGLGEKEFYDPDKAMERVEEHARHFVSLVERLLREHEEKFGEKGIIVAPYDTELFGHWWFEGVKWLGRVLELLYQRGVETPTLSRFLEEYSGEKHEIELPEGSWGANSDHSTWWNEETEWTWPHIYRAEDRMVAIVSRFRGRDELTNRVIEQLARELLILEASDWQFLITTGQAKEYAKRRVLIHSRDFHRLANELVRYVKIGEFDVKLLEELEERDNPFRPVVVGPYVSENPPELEEYVEPPEVPPEKEETEEKPKVLTEKATSLALAVKKVKPVKEETREVKKKAVEASKRGKRKSSKSKRLPRKVSKKAPSKGPSDLLSIKGIGPKTFQKLKRAGVETIEDLKNANIEDLARKTGISTKRLKKFIAQVE |
| Enzyme Length | 675 |
| Uniprot Accession Number | Q5JDJ7 |
| Absorption | |
| Active Site | ACT_SITE 183; /note=Nucleophile; /evidence=ECO:0000269|PubMed:21104698; ACT_SITE 354; /note=Proton donor; /evidence=ECO:0000269|PubMed:21104698 |
| Activity Regulation | |
| Binding Site | BINDING 261; /note=Substrate; BINDING 278; /note=Substrate; via amide nitrogen; BINDING 407; /note=Substrate; BINDING 467; /note=Substrate; BINDING 476; /note=Substrate |
| 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:16885460}; |
| DNA Binding | |
| EC Number | 2.4.1.18 |
| Enzyme Function | FUNCTION: Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 5 to 30, with two local maxima at DP 6 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Does not display alpha-galactosidase or pullulanase activity, since melibiose and pullulan are not substrates. Is not able to catalyze the hydrolysis or transglycosylation of maltoheptaose, suggesting that the TK1436 protein contains neither alpha-amylase nor 4-alpha-glucanotransferase activity. {ECO:0000269|PubMed:16885460}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. Is thermostable up to 90 degrees Celsius. {ECO:0000269|PubMed:16885460}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:16885460}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (15); Binding site (5); Chain (1); Compositional bias (2); Helix (26); Region (2); Site (1); Turn (7) |
| Keywords | 3D-structure;Carbohydrate metabolism;Glycosyltransferase;Reference proteome;Transferase |
| Interact With | |
| Induction | INDUCTION: Up-regulated by maltodextrin. {ECO:0000269|PubMed:16885460}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3N8T; 3N92; 3N98; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 78,549 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 2.4.1.18; |