| IED ID | IndEnz0001000414 |
| Enzyme Type ID | amylase000414 |
| Protein Name |
Glucan 1,4-alpha-maltotetraohydrolase G4-amylase EC 3.2.1.60 Exo-maltotetraohydrolase Maltotetraose-forming amylase Maltotetraose-forming exo-amylase |
| Gene Name | mta |
| Organism | Pelomonas saccharophila (Pseudomonas saccharophila) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Comamonadaceae Pelomonas Pelomonas saccharophila (Pseudomonas saccharophila) |
| Enzyme Sequence | MSHILRAAVLAAVLLPFPALADQAGKSPAGVRYHGGDEIILQGFHWNVVREAPNDWYNILRQQASTIAADGFSAIWMPVPWRDFSSWTDGGKSGGGEGYFWHDFNKNGRYGSDAQLRQAAGALGGAGVKVLYDVVPNHMNRGYPDKEINLPAGQGFWRNDCADPGNYPNDCDDGDRFIGGESDLNTGHPQIYGMFRDELANLRSGYGAGGFRFDFVRGYAPERVDSWMSDSADSSFCVGELWKGPSEYPSWDWRNTASWQQIIKDWSDRAKCPVFDFALKERMQNGSVADWKHGLNGNPDPRWREVAVTFVDNHDTGYSPGQNGGQHHWALQDGLIRQAYAYILTSPGTPVVYWSHMYDWGYGDFIRQLIQVRRTAGVRADSAISFHSGYSGLVATVSGSQQTLVVALNSDLANPGQVASGSFSEAVNASNGQVRVWRSGSGDGGGNDGGEGGLVNVNFRCDNGVTQMGDSVYAVGNVSQLGNWSPASAVRLTDTSSYPTWKGSIALPDGQNVEWKCLIRNEADATLVRQWQSGGNNQVQAAAGASTSGSF |
| Enzyme Length | 551 |
| Uniprot Accession Number | P22963 |
| Absorption | |
| Active Site | ACT_SITE 214; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 240; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 138; /note=Substrate; /evidence=ECO:0000250; BINDING 212; /note=Substrate; /evidence=ECO:0000250; BINDING 314; /note=Substrate; /evidence=ECO:0000250; BINDING 326; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends.; EC=3.2.1.60; |
| DNA Binding | |
| EC Number | 3.2.1.60 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; starch degradation. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (16); Binding site (4); Chain (1); Disulfide bond (2); Domain (1); Helix (21); Metal binding (10); Region (2); Signal peptide (1); Site (1); Turn (3) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21 |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 6IWK; 6IYG; 6J3X; 6JQB; 7CZJ; |
| Mapped Pubmed ID | 31751711; |
| Motif | |
| Gene Encoded By | |
| Mass | 59,898 |
| Kinetics | |
| Metal Binding | METAL 22; /note=Calcium 1; /evidence=ECO:0000250; METAL 23; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 34; /note=Calcium 1; /evidence=ECO:0000250; METAL 37; /note=Calcium 1; /evidence=ECO:0000250; METAL 38; /note=Calcium 1; /evidence=ECO:0000250; METAL 137; /note=Calcium 2; /evidence=ECO:0000250; METAL 172; /note=Calcium 2; /evidence=ECO:0000250; METAL 175; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 183; /note=Calcium 2; /evidence=ECO:0000250; METAL 218; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |