| IED ID | IndEnz0001000003 |
| Enzyme Type ID | amylase000003 |
| 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 | amyP |
| Organism | Pseudomonas stutzeri (Pseudomonas perfectomarina) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas stutzeri group Pseudomonas stutzeri subgroup Pseudomonas stutzeri (Pseudomonas perfectomarina) |
| Enzyme Sequence | MSHILRAAVLAAMLLPLPSMADQAGKSPNAVRYHGGDEIILQGFHWNVVREAPNDWYNILRQQAATIAADGFSAIWMPVPWRDFSSWSDGSKSGGGEGYFWHDFNKNGRYGSDAQLRQAASALGGAGVKVLYDVVPNHMNRGYPDKEINLPAGQGFWRNDCADPGNYPNDCDDGDRFIGGDADLNTGHPQVYGMFRDEFTNLRSQYGAGGFRFDFVRGYAPERVNSWMTDSADNSFCVGELWKGPSEYPNWDWRNTASWQQIIKDWSDRAKCPVFDFALKERMQNGSIADWKHGLNGNPDPRWREVAVTFVDNHDTGYSPGQNGGQHHWALQDGLIRQAYAYILTSPGTPVVYWSHMYDWGYGDFIRQLIQVRRAAGVRADSAISFHSGYSGLVATVSGSQQTLVVALNSDLGNPGQVASGSFSEAVNASNGQVRVWRSGTGSGGGEPGALVSVSFRCDNGATQMGDSVYAVGNVSQLGNWSPAAALRLTDTSGYPTWKGSIALPAGQNEEWKCLIRNEANATQVRQWQGGANNSLTPSEGATTVGRL |
| Enzyme Length | 548 |
| Uniprot Accession Number | P13507 |
| Absorption | |
| Active Site | ACT_SITE 214; /note="Nucleophile"; /evidence="ECO:0000305|PubMed:10556241"; ACT_SITE 240; /note="Proton donor"; /evidence="ECO:0000305|PubMed:10556241, ECO:0000305|PubMed:9281429" |
| Activity Regulation | |
| Binding Site | BINDING 138; /note="Substrate"; /evidence="ECO:0000305|PubMed:10556241, ECO:0000305|PubMed:9281429"; BINDING 212; /note="Substrate"; /evidence="ECO:0000305|PubMed:10556241, ECO:0000305|PubMed:9281429"; BINDING 314; /note="Substrate"; /evidence="ECO:0000305|PubMed:10556241, ECO:0000305|PubMed:9281429"; BINDING 326; /note="Substrate"; /evidence="ECO:0000305|PubMed:10556241" |
| 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; Evidence={ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:2646279, ECO:0000269|PubMed:9281429}; |
| DNA Binding | |
| EC Number | 3.2.1.60 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; starch degradation. {ECO:0000305|PubMed:10556241, ECO:0000305|PubMed:9281429}. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (20); Binding site (4); Chain (1); Disulfide bond (2); Domain (1); Helix (21); Metal binding (10); Mutagenesis (3); Region (4); Sequence conflict (1); Signal peptide (1); Site (1); Turn (3) |
| Keywords | 3D-structure;Calcium;Carbohydrate metabolism;Direct protein sequencing;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:2646279}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21 |
| Structure 3D | X-ray crystallography (9) |
| Cross Reference PDB | 1GCY; 1JDA; 1JDC; 1JDD; 1QI3; 1QI4; 1QI5; 1QPK; 2AMG; |
| Mapped Pubmed ID | 11272837; |
| Motif | |
| Gene Encoded By | |
| Mass | 59,876 |
| Kinetics | |
| Metal Binding | METAL 22; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429"; METAL 23; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429"; METAL 34; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429"; METAL 37; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429"; METAL 38; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429"; METAL 137; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429"; METAL 172; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429"; METAL 175; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429"; METAL 183; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429"; METAL 218; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429" |
| Rhea ID | |
| Cross Reference Brenda |