| IED ID | IndEnz0001000845 |
| Enzyme Type ID | amylase000845 |
| Protein Name |
Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase GMPMT EC 2.4.99.16 1- 4 -alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase |
| Gene Name | glgE Balac_1458 |
| Organism | Bifidobacterium animalis subsp. lactis (strain Bl-04 / DGCC2908 / RB 4825 / SD5219) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Bifidobacteriales Bifidobacteriaceae Bifidobacterium Bifidobacterium animalis Bifidobacterium animalis subsp. lactis (Bifidobacterium lactis) Bifidobacterium animalis subsp. lactis (strain Bl-04 / DGCC2908 / RB 4825 / SD5219) |
| Enzyme Sequence | MEAQHNETEAAGKPAAKKTTRTRKPRASKQATFIAEAPAMPIAIKEPGQFGRVNILNCQPSVEDDVYAARVEIGEQFTVSAQVFMEGRTKVGATAVLKNPRGRIMARVPMTVENAGLDLYTAKLQAGEHSTLNPWDAEFAEVKKQLGNWRVAIEGWEDTYGAWLHDARIKVDVLSDVENTLTSGSELLTRWASTRDANLNAEQRKTLREAAKSMMDTSLDAKSRLTFADNADIEALHETNPLRDGLTSSGDHVFHVERPKSSFSAWYQFFPRSEGAYLDDNGKKVQGNFHTAVSGLERAKAEGFNIVYLPPIFPIGVTNRKGPDGALNAGPDDPGSPFGIGSELGGHDTVDPLLGTMDDFKAFCQRAHELNLEVALDFALQCSPDHPWVKEHPNWFRTKPDGSIAYAENPPKKYQDIYPIDFDNDLEGIEREVERIMNLWIDAGVTIFRVDNPHTKPVRFWQDVIAAVTKKHPEVLFLAEAFTRPAMVRALSYAGFTQSHCYFPWRNTKPQLEEFLQETNGKGGYYQHNTFWPTTPDILTAYVRDGGVAAHAIRAVLAALGSPSWGIYNGYELIENRQRADAEEQSSNEKFEIKVRDWSAANRIGISKLLTSLNEIRSKHAATTSYHNLTILPSANENIIAFARQTEGRFTKDGRTDTLIVVVNLDPYNEQQSSIHVDAKALGLPTEHPYRVKDQLTGREYDWSWDNFVSLAPWADVAHVFHVETGEQPLD |
| Enzyme Length | 731 |
| Uniprot Accession Number | C6A9K7 |
| Absorption | |
| Active Site | ACT_SITE 451; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_02124; ACT_SITE 480; /note=Proton donor; /evidence=ECO:0000255|HAMAP-Rule:MF_02124 |
| Activity Regulation | |
| Binding Site | BINDING 321; /note=Maltose 1-phosphate; /evidence=ECO:0000255|HAMAP-Rule:MF_02124; BINDING 381; /note=Maltose 1-phosphate; /evidence=ECO:0000255|HAMAP-Rule:MF_02124; BINDING 416; /note=Maltose 1-phosphate; /evidence=ECO:0000255|HAMAP-Rule:MF_02124; BINDING 452; /note=Maltose 1-phosphate; /evidence=ECO:0000255|HAMAP-Rule:MF_02124 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + alpha-maltose 1-phosphate = [(1->4)-alpha-D-glucosyl](n+2) + phosphate; Xref=Rhea:RHEA:42692, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:10183, ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:63576; EC=2.4.99.16; Evidence={ECO:0000255|HAMAP-Rule:MF_02124}; |
| DNA Binding | |
| EC Number | 2.4.99.16 |
| Enzyme Function | FUNCTION: Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB. {ECO:0000255|HAMAP-Rule:MF_02124}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (4); Chain (1); Compositional bias (1); Region (2); Site (1) |
| Keywords | Carbohydrate metabolism;Glycosyltransferase;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 81,693 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:42692 |
| Cross Reference Brenda |