| IED ID | IndEnz0001000901 |
| Enzyme Type ID | amylase000901 |
| Protein Name |
Glucan 1,4-alpha-maltohexaosidase EC 3.2.1.98 Exo-maltohexaohydrolase G6-amylase Maltohexaose-producing amylase |
| Gene Name | |
| Organism | Bacillus sp. (strain 707) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus unclassified Bacillus (in: Bacteria) Bacillus sp. (strain 707) |
| Enzyme Sequence | MKMRTGKKGFLSILLAFLLVITSIPFTLVDVEAHHNGTNGTMMQYFEWYLPNDGNHWNRLNSDASNLKSKGITAVWIPPAWKGASQNDVGYGAYDLYDLGEFNQKGTVRTKYGTRSQLQAAVTSLKNNGIQVYGDVVMNHKGGADATEMVRAVEVNPNNRNQEVTGEYTIEAWTRFDFPGRGNTHSSFKWRWYHFDGVDWDQSRRLNNRIYKFRGHGKAWDWEVDTENGNYDYLMYADIDMDHPEVVNELRNWGVWYTNTLGLDGFRIDAVKHIKYSFTRDWINHVRSATGKNMFAVAEFWKNDLGAIENYLQKTNWNHSVFDVPLHYNLYNASKSGGNYDMRNIFNGTVVQRHPSHAVTFVDNHDSQPEEALESFVEEWFKPLAYALTLTREQGYPSVFYGDYYGIPTHGVPAMRSKIDPILEARQKYAYGKQNDYLDHHNIIGWTREGNTAHPNSGLATIMSDGAGGSKWMFVGRNKAGQVWSDITGNRTGTVTINADGWGNFSVNGGSVSIWVNK |
| Enzyme Length | 518 |
| Uniprot Accession Number | P19571 |
| Absorption | |
| Active Site | ACT_SITE 269; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 299; /note=Proton donor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non-reducing chain ends.; EC=3.2.1.98; Evidence={ECO:0000250|UniProtKB:P06278}; |
| DNA Binding | |
| EC Number | 3.2.1.98 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycan degradation; starch degradation. |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (30); Chain (1); Helix (16); Metal binding (13); Signal peptide (1); Site (1); Turn (7) |
| Keywords | 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000269|PubMed:3258152 |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 1WP6; 1WPC; 2D3L; 2D3N; 2GJP; 2GJR; |
| Mapped Pubmed ID | 15518553; 16452622; 16946462; |
| Motif | |
| Gene Encoded By | |
| Mass | 59,009 |
| Kinetics | |
| Metal Binding | METAL 139; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P00692; METAL 196; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P00692; METAL 196; /note=Sodium; /evidence=ECO:0000250|UniProtKB:P00692; METAL 219; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00692; METAL 221; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P00692; METAL 221; /note=Sodium; /evidence=ECO:0000250|UniProtKB:P00692; METAL 232; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P00692; METAL 232; /note=Sodium; /evidence=ECO:0000250|UniProtKB:P00692; METAL 238; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P00692; METAL 238; /note=Sodium; /evidence=ECO:0000250|UniProtKB:P00692; METAL 240; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P00692; METAL 242; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P00692; METAL 273; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P00692 |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.98; |