| IED ID | IndEnz0001000195 |
| Enzyme Type ID | amylase000195 |
| Protein Name |
Cyclomaltodextrin glucanotransferase EC 2.4.1.19 Cyclodextrin-glycosyltransferase CGTase |
| Gene Name | amyA |
| Organism | Thermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Thermoanaerobacterales Thermoanaerobacterales Family III. Incertae Sedis Thermoanaerobacterium Thermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes) |
| Enzyme Sequence | MKKTFKLILVLMLSLTLVFGLTAPIQAASDTAVSNVVNYSTDVIYQIVTDRFVDGNTSNNPTGDLYDPTHTSLKKYFGGDWQGIINKINDGYLTGMGVTAIWISQPVENIYAVLPDSTFGGSTSYHGYWARDFKRTNPYFGSFTDFQNLINTAHAHNIKVIIDFAPNHTSPASETDPTYAENGRLYDNGTLLGGYTNDTNGYFHHYGGTDFSSYEDGIYRNLFDLADLNQQNSTIDSYLKSAIKVWLDMGIDGIRLDAVKHMPFGWQKNFMDSILSYRPVFTFGEWFLGTNEIDVNNTYFANESGMSLLDFRFSQKVRQVFRDNTDTMYGLDSMIQSTASDYNFINDMVTFIDNHDMDRFYNGGSTRPVEQALAFTLTSRGVPAIYYGTEQYMTGNGDPYNRAMMTSFNTSTTAYNVIKKLAPLRKSNPAIAYGTTQQRWINNDVYIYERKFGNNVALVAINRNLSTSYNITGLYTALPAGTYTDVLGGLLNGNSISVASDGSVTPFTLSAGEVAVWQYVSSSNSPLIGHVGPTMTKAGQTITIDGRGFGTTSGQVLFGSTAGTIVSWDDTEVKVKVPSVTPGKYNISLKTSSGATSNTYNNINILTGNQICVRFVVNNASTVYGENVYLTGNVAELGNWDTSKAIGPMFNQVVYQYPTWYYDVSVPAGTTIQFKFIKKNGNTITWEGGSNHTYTVPSSSTGTVIVNWQQ |
| Enzyme Length | 710 |
| Uniprot Accession Number | P26827 |
| Absorption | |
| Active Site | ACT_SITE 257; /note=Nucleophile; /evidence=ECO:0000269|PubMed:8604143; ACT_SITE 285; /note=Proton donor; /evidence=ECO:0000269|PubMed:8604143 |
| Activity Regulation | |
| Binding Site | BINDING 168; /note=Substrate; /evidence=ECO:0000250; BINDING 255; /note=Substrate; /evidence=ECO:0000250; BINDING 355; /note=Substrate; /evidence=ECO:0000250; BINDING 398; /note=Substrate; BINDING 402; /note=Substrate |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond.; EC=2.4.1.19; |
| DNA Binding | |
| EC Number | 2.4.1.19 |
| Enzyme Function | FUNCTION: Degrades starch to alpha-, beta-, and gamma-cyclodextrins, as well as linear sugars. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (44); Binding site (5); Chain (1); Domain (2); Helix (22); Metal binding (10); Region (3); Sequence conflict (3); Signal peptide (1); Site (1); Turn (5) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Glycosyltransferase;Metal-binding;Secreted;Signal;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1854207}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000269|PubMed:1854207 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1A47; 1CIU; 3BMV; 3BMW; |
| Mapped Pubmed ID | 18422488; |
| Motif | |
| Gene Encoded By | |
| Mass | 78,417 |
| Kinetics | |
| Metal Binding | METAL 54; /note=Calcium 1; METAL 56; /note=Calcium 1; via carbonyl oxygen; METAL 59; /note=Calcium 1; METAL 60; /note=Calcium 1; METAL 78; /note=Calcium 1; via carbonyl oxygen; METAL 80; /note=Calcium 1; METAL 167; /note=Calcium 2; METAL 218; /note=Calcium 2; via carbonyl oxygen; METAL 227; /note=Calcium 2; METAL 261; /note=Calcium 2; via carbonyl oxygen |
| Rhea ID | |
| Cross Reference Brenda | 2.4.1.19; |