| IED ID | IndEnz0001000054 |
| Enzyme Type ID | amylase000054 |
| Protein Name |
4-alpha-glucanotransferase EC 2.4.1.25 Amylomaltase Disproportionating enzyme D-enzyme |
| Gene Name | jgt OCC_10078 |
| Organism | Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Thermococci Thermococcales Thermococcaceae Thermococcus Thermococcus litoralis Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) |
| Enzyme Sequence | MERINFIFGIHNHQPLGNFGWVFEEAYNRSYRPFMEILEEFPEMKVNVHFSGPLLEWIEENKPDYLDLLRSLIKRGQLEIVVAGFYEPVLAAIPKEDRLVQIEMLKDYARKLGYDAKGVWLTERVWQPELVKSLREAGIEYVVVDDYHFMSAGLSKEELFWPYYTEDGGEVITVFPIDEKLRYLIPFRPVKKTIEYLESLTSDDPSKVAVFHDDGEKFGVWPGTYEWVYEKGWLREFFDAITSNEKINLMTYSEYLSKFTPRGLVYLPIASYFEMSEWSLPAKQAKLFVEFVEQLKEEGKFEKYRVFVRGGIWKNFFFKYPESNFMHKRMLMVSKAVRDNPEARKYILKAQCNDAYWHGVFGGIYLPHLRRTVWENIIKAQRYLKPENKILDVDFDGRAEIMVENDGFIATIKPHYGGSIFELSSKRKAVNYNDVLPRRWEHYHEVPEATKPEKESEEGIASIHELGKQIPEEIRRELAYDWQLRAILQDHFIKPEETLDNYRLVKYHELGDFVNQPYEYEMIENGVKLWREGGVYAEEKIPARVEKKIELTEDGFIAKYRVLLEKPYKALFGVEINLAVHSVMEKPEEFEAKEFEVNDPYGIGKVRIELDKAAKVWKFPIKTLSQSEAGWDFIQQGVSYTMLFPIEKELEFTVRFREL |
| Enzyme Length | 659 |
| Uniprot Accession Number | O32462 |
| Absorption | |
| Active Site | ACT_SITE 123; /note=Nucleophile; ACT_SITE 214; /note=Proton donor |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoic acid, monoiodoacetic acid, mercury and nickel ions. |
| 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; Evidence={ECO:0000269|PubMed:10348846}; |
| DNA Binding | |
| EC Number | 2.4.1.25 |
| Enzyme Function | FUNCTION: Catalyzes the transglycosylation of maltooligosaccharides, yielding maltooligosaccharides of various lengths and glucose. Maltose and glucose can be used as acceptors in the transfer reaction. {ECO:0000269|PubMed:10348846}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 85-100 degrees Celsius. {ECO:0000269|PubMed:10348846}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (24); Chain (1); Helix (29); Turn (9) |
| Keywords | 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Glycosyltransferase;Transferase |
| Interact With | |
| Induction | INDUCTION: Expressed constitutively. {ECO:0000269|PubMed:10348846}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1K1W; 1K1X; 1K1Y; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 77,885 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=13 umol/min/mg enzyme with maltose as substrate {ECO:0000269|PubMed:10348846}; Vmax=26 umol/min/mg enzyme with maltotriose as substrate {ECO:0000269|PubMed:10348846}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 2.4.1.25; |