| IED ID | IndEnz0001000854 |
| Enzyme Type ID | amylase000854 |
| 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 1- 4 -alpha-D-glucan:phosphate alpha-D-maltosyltransferase |
| Gene Name | glgE Rv1327c MTCY130.12c |
| 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 | MSGRAIGTETEWWVPGRVEIDDVAPVVSCGVYPAKAVVGEVVPVSAAVWREGHEAVAATLVVRYLGVRYPHLTDRPRARVLPTPSEPQQRVKPLLIPMTSGQEPFVFHGQFTPDRVGLWTFRVDGWGDPIHTWRHGLIAKLDAGQGETELSNDLLVGAVLLERAATGVPRGLRDPLLAAAAALRTPGDPVTRTALALTPEIEELLADYPLRDLVTRGEQFGVWVDRPLARFGAWYEMFPRSTGGWDDDGNPVHGTFATAAAELPRIAGMGFDVVYLPPIHPIGKVHRKGRNNSPTAAPTDVGSPWAIGSDEGGHDTVHPSLGTIDDFDDFVSAARDLGMEVALDLALQCAPDHPWAREHRQWFTELPDGTIAYAENPPKKYQDIYPLNFDNDPEGLYDEVLRVVQHWVNHGVKFFRVDNPHTKPPNFWAWLIAQVKTVDPDVLFLSEAFTPPARQYGLAKLGFTQSYSYFTWRTTKWELTEFGNQIAELADYRRPNLFVNTPDILHAVLQHNGPGMFAIRAVLAATMSPAWGMYCGYELFEHRAVREGSEEYLDSEKYELRPRDFASALDQGRSLQPFITRLNIIRRLHPAFQQLRTIHFHHVDNDALLAYSKFDPATGDCVLVVVTLNAFGPEEATLWLDMAALGMEDYDRFWVRDEITGEEYQWGQANYIRIDPARAVAHIINMPAVPYESRNTLLRRR |
| Enzyme Length | 701 |
| Uniprot Accession Number | P9WQ17 |
| Absorption | |
| Active Site | ACT_SITE 418; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 447; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 288; /note=Maltose 1-phosphate; /evidence=ECO:0000250; BINDING 348; /note=Maltose 1-phosphate; /evidence=ECO:0000250; BINDING 383; /note=Maltose 1-phosphate; /evidence=ECO:0000250; BINDING 419; /note=Maltose 1-phosphate; /evidence=ECO:0000250 |
| 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:0000269|PubMed:20305657}; |
| DNA Binding | |
| EC Number | 2.4.99.16 |
| Enzyme Function | FUNCTION: Essential maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Maltooligosaccharides with a degree of polymerization (DP) superior or equal to 4 are efficient acceptors, with DP5 being optimal in the GlgE-catalyzed polymerization with M1P. Is specific for the alpha-anomer of M1P as substrate, since the beta-anomer of M1P gives no activity. Exhibits an alpha-retaining catalytic mechanism. Is also able to catalyze the reverse reaction in vitro, releasing M1P from glycogen in the presence of inorganic phosphate. Also catalyzes disproportionation reactions through maltosyl transfer between maltooligosaccharides. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB. {ECO:0000269|PubMed:20305657}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius with maltohexaose as acceptor substrate. {ECO:0000269|PubMed:20305657}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 with maltohexaose as acceptor substrate. {ECO:0000269|PubMed:20305657}; |
| Pathway | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. |
| nucleotide Binding | |
| Features | Active site (2); Binding site (4); Chain (1); Region (2); Site (1) |
| Keywords | Carbohydrate metabolism;Glycogen biosynthesis;Glycogen metabolism;Glycosyltransferase;Reference proteome;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 | 78,640 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=35 mM for maltohexaose (in the presence of 5 mM M1P) {ECO:0000269|PubMed:20305657}; KM=13.3 mM for maltohexaose (in the presence of 1 mM M1P) {ECO:0000269|PubMed:20305657}; KM=0.25 mM for alpha-maltose 1-phosphate {ECO:0000269|PubMed:20305657}; KM=6 mM for phosphate {ECO:0000269|PubMed:20305657}; |
| Metal Binding | |
| Rhea ID | RHEA:42692 |
| Cross Reference Brenda |