| IED ID | IndEnz0001000852 |
| Enzyme Type ID | amylase000852 |
| 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 MSMEG_4916 MSMEI_4789 |
| Organism | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycolicibacterium Mycolicibacterium smegmatis (Mycobacterium smegmatis) Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
| Enzyme Sequence | MRSGWVAGRIGIDDVAPVVSCGRYPAKAVVGEVVPVRATVWREGHDAVSATLVVRYLGTEFPRLASGPGTTPPAVPLGTVVQPGKRVKPQILQMSKGRTPDVFHGEFTPDAVGLWTFRVDGWGDPIATWRHAVEAKLEAGQSETELNNDLLVGARLLMRAAEGVPRKLRDPLLEAAQQLRTPGDPYQRAGGALSPEVADLLLQYPLREFVTRGEVHGVWVDRPLARFSSWYEMFPRSTGGWDENGHPVHGTFATAAAALPRIARMGFNVVYLPPIHPIGKVHRKGRNNSVTAAPGDVGSPWAIGSDEGGHDAVHPDLGTIDDFDAFVAAARDAGLEVALDLALQCAPDHPWAKEHPEWFTVLPDGTIAYAENPPKKYQDIYPLNFDNDPDGLFHEVLRVVKFWISHGVKVFRVDNPHTKPPNFWAWLIAEVKNEDPDILFLSEAFTRPARLYGLAKLGFTQSYTYFTWRTAKWELTEFGEEIAKYADHARPNLWVNTPDILHESLQHGGPGMFAIRAVLASTMSSSWGVYSGYELFEHRSVREGSEEYLDSEKYELRPRDFDGALARGESLEPFLTRLNEIRRLHPALRQLRTIKFHHLDNDALLAYSKFDPVTGDTVLVVVTLNPFGPEESTLWLDMEALGMEPYDRFWVRDEITGEEYQWGQSNYVRIEPAKAVAHVLNMPLIPYEKRLDLLRRE |
| Enzyme Length | 697 |
| Uniprot Accession Number | Q9RP48 |
| Absorption | |
| Active Site | ACT_SITE 414; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 443; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: The transfer reaction from maltose-1-P to glycogen is inhibited by micromolar amounts of inorganic phosphate or arsenate but is only slightly inhibited by millimolar concentrations of glucose-1-P, glucose-6-P, or inorganic pyrophosphate. Is also inhibited by ATP, by 1,4-dideoxy-1,4-imino-D-arabinitol (DIA), but not by isofagomine. {ECO:0000269|PubMed:20118231}. |
| Binding Site | BINDING 284; /note=Maltose 1-phosphate; /evidence=ECO:0000250; BINDING 344; /note=Maltose 1-phosphate; /evidence=ECO:0000250; BINDING 379; /note=Maltose 1-phosphate; /evidence=ECO:0000250; BINDING 415; /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:20118231}; |
| 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 also able to catalyze the reverse reaction in vitro. Cannot use glucose 1-phosphate as substrate. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB. {ECO:0000269|PubMed:20118231}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:20118231}. |
| nucleotide Binding | |
| Features | Active site (2); Binding site (4); Chain (1); Erroneous initiation (1); Mutagenesis (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 | 78,043 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=250 uM for maltose 1-phosphate {ECO:0000269|PubMed:20118231}; Vmax=25.2 nmol/min/mg enzyme {ECO:0000269|PubMed:20118231}; Note=The data are not very reliable because measures were done with a partially purified enzyme.; |
| Metal Binding | |
| Rhea ID | RHEA:42692 |
| Cross Reference Brenda | 2.4.99.16; |