| IED ID | IndEnz0001000909 |
| Enzyme Type ID | amylase000909 |
| Protein Name |
Amylopullulanase Alpha-amylase/pullulanase Includes: Alpha-amylase EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase ; Pullulanase EC 3.2.1.41 1,4-alpha-D-glucan glucanohydrolase Alpha-dextrin endo-1,6-alpha-glucosidase |
| Gene Name | apu Teth39_2173 |
| Organism | Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium thermohydrosulfuricum) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Thermoanaerobacterales Thermoanaerobacteraceae Thermoanaerobacter Thermoanaerobacter pseudethanolicus Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium thermohydrosulfuricum) |
| Enzyme Sequence | MFKRRTLGFLLSFLLIYTAVFGSMPVQFAKAETDTAPAIANVVGDFQSKIGDSDWNINSDKTVMTYKGNGFYEFTTPVALPAGDYEYKVALNHSWEGGGVPSQGNLSLHLDSDSVVTFYYNYNTSSVTDSTKYTPIPEEKLPRIVGTIQSAIGAGDDWKPETSTAIMRDYKFNNVYEYTANVPKGYYEFKVTLGPSWDINYGLNGEQNGPNIPLNVAYDTKITFYYDSVSHNIWTDYNPPLTGPDNNIYYDDLKHDTHDPFFRSPFGAIKTGDTVTLRIQAKNHDLESAKISYWDDIKKTRTEVPMYKIGQSPDGQYEYWEVKLSFDYPTRIWYYFILKDGTKTAYYGDNDEQLGGVGKATDTVNKDFELTVYDKNLDTPDWMKGAVMYQIFPDRFYNGDPLNDRLKEYSRGFDPVEYHDDWYDLPDNPNDKDKPGYTGDGIWNNDFFGGDLQGINDKLDYLKNLGISVIYLNPIFQSPSNHRYDTTDYTKIDELLGDLDTFKTLMKEAHARGIKVILDGVFNHTSDDSIYFDRYGKYLDNELGAYQAWKQGDQSKSPYGDWYEIKPDGTYEGWWGFDSLPVIRQINGSEYNVKSWADFIINNPNAISKYWLNPDGDKDAGADGWRLDVANEIAHDFWVHFRAAINTVKPNAPMIAELWGDASLDLLGDSFNSVMNYLFRNAVIDFILDKQFDDGNVVHNPIDAAKLDQRLMSIYERYPLPVFYSTMNLLGSHDTMRILTVFGYNSANENQNSQEAKDLAVKRLKLAAILQMGYPGMPSIYYGDEAGQSGGKDPDNRRTFSWGREDKDLQDFFKKVVNIRNENQVLKTGDLETLYANGDVYAFGRRIINGKDVFGNSYPDSVAIVVINKGEAKSVQIDTTKFVRDGVAFTDALSGKTYTVRDGQIVVEVVALDGAILISDPGQNLTAPQPITDLKAVSGNGQVDLSWSAVDRAVSYNIYRSTVKGGLYEKIASNVTQITYIDTDVTNGLKYVYSVTAVDSDGNESALSNEVEAYPAFSIGWAGNMNQVDTHVIGVNNPVEVYAEIWAEGLTDKPGQGENMIAQLGYRYIGDGGQDATRNKVEGVEINKDWTWVDARYVGDSGNNDKYMAKFVPDMVGTWEYIMRFSSNQGQDWTYTKGPDGKTDEAKQFIVVPSNDVEPPTALGLQQPGIESSRVTLNWSLSTDNVAIYGYEIYKSLSETGPFVKIATVADTVYNYVDTDVVNGKVYYYKVVAVDTSFNRTASNIVKATPDIIPIKVIFNVTVPDYTPDDGANIAGNFHDAFWNPSAHQMTKTGPNTYSITLTLNEGTQLEYKYARGSWDKVEKGEYGEEIANRKITVVNQGSNTMVVNDTVQRWRDLPIYIYSPKDNTTVDANTNEIEIKGNTYKGAKVTINDESFVQQENGVFTKVVPLEYGVNTTKIHVEPSGDKNNELTKDITITVIREEPVQEKEPTPTPESEPAPMPEPQPTPTPEPQPSAIMAL |
| Enzyme Length | 1481 |
| Uniprot Accession Number | P38939 |
| Absorption | |
| Active Site | ACT_SITE 628; /note=Nucleophile; /evidence=ECO:0000305|PubMed:8344920; ACT_SITE 657; /note=Proton donor; /evidence=ECO:0000305|PubMed:8344920 |
| Activity Regulation | |
| Binding Site | BINDING 524; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 626; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 793; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 797; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.; EC=3.2.1.41; Evidence={ECO:0000269|PubMed:8344920}; |
| DNA Binding | |
| EC Number | 3.2.1.1; 3.2.1.41 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (4); Chain (1); Compositional bias (1); Domain (3); Frameshift (1); Metal binding (10); Mutagenesis (3); Region (2); Sequence conflict (4); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding;Repeat;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 166,230 |
| Kinetics | |
| Metal Binding | METAL 245; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 247; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 285; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 340; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 398; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 400; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 403; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 404; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 449; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 451; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q60053 |
| Rhea ID | |
| Cross Reference Brenda |