| IED ID | IndEnz0001000121 |
| Enzyme Type ID | amylase000121 |
| Protein Name |
Cyclomaltodextrinase CDase EC 3.2.1.54 Cyclomaltodextrin hydrolase, decycling |
| Gene Name | Teth39_0676 |
| 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 | MIKEAIFHKSDVPYAYPLNENQLKIVLRTAVFDVDRVYVLYKDRYDWLGKFKIKPMVLTHTNELFDYYETTLELNKKFVYFFYLVSDGGEKLYYTEAGFYKKRPENHFWGFFHYPYIGEKDVFFAPEWTSDCMVYQIFPERFNNGDKSNDPENVKPWGEKPTADSFFGGDLQGIIDKIDYLKDLGINAIYLTPIFLSHSTHKYDTTDYYTIDPHFGDTQKARELVQKCHDNGIKVIFDAVFNHCGYDFFAFQDVIKNGKKSKYWDWFNIYEWPIKTHPKPSYEAFADTVWRMPKLMTKNPEVQKYLLEVAEYWIKEVDIDGWRLDVANEIDHHFWRKFREVVKAAKPEAIIVGEVWHDASPWLRGDQFDSVMNYPFRNAVVDFFAKRKISASRFNTMITEQLMRHMDSVNRVMFNLIGSHDTERFLTLANGMVARMKLALVFQFTFVGIPYIYYGDEVGMVGDYDPDCRRCMIWEEEKQNKSIFNFYKKLISIRRENEELKYGSFCTLYAIGRVFAFKREYKGKSIIVVLNNSSKQEVIFLNEVEGKEDILKMKELKRSGNLLYLQPNSAYILK |
| Enzyme Length | 574 |
| Uniprot Accession Number | P29964 |
| Absorption | |
| Active Site | ACT_SITE 325; /note=Nucleophile; /evidence=ECO:0000305|PubMed:8425614; ACT_SITE 354; /note=Proton donor; /evidence=ECO:0000305|PubMed:8425614 |
| Activity Regulation | |
| Binding Site | BINDING 243; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 323; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 465; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940; BINDING 469; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P38940 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=cyclomaltodextrin + H2O = linear maltodextrin; Xref=Rhea:RHEA:23980, Rhea:RHEA-COMP:14584, Rhea:RHEA-COMP:14707, ChEBI:CHEBI:15377, ChEBI:CHEBI:17623, ChEBI:CHEBI:18398; EC=3.2.1.54; |
| DNA Binding | |
| EC Number | 3.2.1.54 |
| Enzyme Function | FUNCTION: Hydrolyzes cyclodextrins. Can also act on linear maltodextrins, with the exception of maltose. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (4); Chain (1); Metal binding (6); Mutagenesis (3); Region (1); Sequence conflict (2); Site (1) |
| Keywords | Calcium;Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 68,066 |
| Kinetics | |
| Metal Binding | METAL 144; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 146; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 149; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 150; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 168; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q60053; METAL 170; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q60053 |
| Rhea ID | RHEA:23980 |
| Cross Reference Brenda |