| IED ID | IndEnz0001000542 |
| Enzyme Type ID | amylase000542 |
| Protein Name |
4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic EC 2.4.1.25 Amylomaltase Disproportionating enzyme D-enzyme Protein DISPROPORTIONATING ENZYME 1 |
| Gene Name | DPE1 At5g64860 MXK3.9 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MSILLRPSSSPSLCSSLKLFRLSSPDSLIDAAVLRNRTKPSQSFRMEVVSSNSTCLSSISVGEDFPSEYEQWLPVPDPESRRRAGVLLHPTSFRGPHGIGDLGEEAFRFIDWLHSTGCSVWQVLPLVPPDEGGSPYAGQDANCGNTLLISLDELVKDGLLIKDELPQPIDADSVNYQTANKLKSPLITKAAKRLIDGNGELKSKLLDFRNDPSISCWLEDAAYFAAIDNTLNAYSWFEWPEPLKNRHLSALEAIYESQKEFIDLFIAKQFLFQRQWQKVREYARRQGVDIMGDMPIYVGYHSADVWANKKHFLLNKKGFPLLVSGVPPDLFSETGQLWGSPLYDWKAMESDQYSWWVNRIRRAQDLYDECRIDHFRGFAGFWAVPSEAKVAMVGRWKVGPGKSLFDAISKGVGKIKIIAEDLGVITKDVVELRKSIGAPGMAVLQFAFGGGADNPHLPHNHEVNQVVYSGTHDNDTIRGWWDTLDQEEKSKAMKYLSIAGEDDISWSVIQAAFSSTAQTAIIPMQDILGLGSSARMNTPATEVGNWGWRIPSSTSFDNLETESDRLRDLLSLYGRL |
| Enzyme Length | 576 |
| Uniprot Accession Number | Q9LV91 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.; EC=2.4.1.25; |
| DNA Binding | |
| EC Number | 2.4.1.25 |
| Enzyme Function | FUNCTION: Chloroplastic alpha-glucanotransferase involved in maltotriose metabolism. Probably uses maltotriose as substrate to transfer a maltosyl unit from one molecule to another, resulting in glucose and maltopentaose. The latter can then be further metabolized to maltose and maltotriose by beta-amylase. Required for normal starch degradation in leaves. {ECO:0000269|PubMed:11359613, ECO:0000269|PubMed:19946617}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (17); Chain (1); Helix (33); Transit peptide (1); Turn (1) |
| Keywords | 3D-structure;Amyloplast;Carbohydrate metabolism;Chloroplast;Glycosyltransferase;Plastid;Reference proteome;Transferase;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 5CPQ; 5CPS; 5CPT; 5CQ1; 5CSU; 5CSY; |
| Mapped Pubmed ID | 12508068; 14576160; 14996213; 15862090; 16297066; 17151136; 18431481; 18650403; 18787712; 20700743; 20736450; 21242321; 21691153; 22027553; 23393426; 26504082; 28152100; 28225829; 28627464; |
| Motif | |
| Gene Encoded By | |
| Mass | 64,412 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 2.4.1.25; |