| IED ID | IndEnz0001000316 |
| Enzyme Type ID | amylase000316 |
| Protein Name |
Isoamylase EC 3.2.1.68 |
| Gene Name | iam |
| Organism | Pseudomonas amyloderamosa |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadales incertae sedis Pseudomonas amyloderamosa |
| Enzyme Sequence | MKCPKILAALLGCAVLAGVPAMPAHAAINSMSLGASYDAQQANITFRVYSSQATRIVLYLYSAGYGVQESATYTLSPAGSGVWAVTVPVSSIKAAGITGAVYYGYRAWGPNWPYASNWGKGSQAGFVSDVDANGDRFNPNKLLLDPYAQEVSQDPLNPSNQNGNVFASGASYRTTDSGIYAPKGVVLVPSTQSTGTKPTRAQKDDVIYEVHVRGFTEQDTSIPAQYRGTYYGAGLKASYLASLGVTAVEFLPVQETQNDANDVVPNSDANQNYWGYMTENYFSPDRRYAYNKAAGGPTAEFQAMVQAFHNAGIKVYMDVVYNHTAEGGTWTSSDPTTATIYSWRGLDNATYYELTSGNQYFYDNTGIGANFNTYNTVAQNLIVDSLAYWANTMGVDGFRFDLASVLGNSCLNGAYTASAPNCPNGGYNFDAADSNVAINRILREFTVRPAAGGSGLDLFAEPWAIGGNSYQLGGFPQGWSEWNGLFRDSLRQAQNELGSMTIYVTQDANDFSGSSNLFQSSGRSPWNSINFIDVHDGMTLKDVYSCNGANNSQAWPYGPSDGGTSTNYSWDQGMSAGTGAAVDQRRAARTGMAFEMLSAGTPLMQGGDEYLRTLQCNNNAYNLDSSANWLTYSWTTDQSNFYTFAQRLIAFRKAHPALRPSSWYSGSQLTWYQPSGAVADSNYWNNTSNYAIAYAINGPSLGDSNSIYVAYNGWSSSVTFTLPAPPSGTQWYRVTDTCDWNDGASTFVAPGSETLIGGAGTTYGQCGQSLLLLISK |
| Enzyme Length | 776 |
| Uniprot Accession Number | P10342 |
| Absorption | |
| Active Site | ACT_SITE 401; /note=Nucleophile; ACT_SITE 461; /note=Proton donor |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins.; EC=3.2.1.68; Evidence={ECO:0000269|PubMed:2248978}; |
| DNA Binding | |
| EC Number | 3.2.1.68 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (29); Chain (1); Disulfide bond (3); Frameshift (1); Helix (26); Metal binding (5); Sequence conflict (7); Signal peptide (1); Site (1); Turn (6) |
| Keywords | 3D-structure;Calcium;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: By maltose. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2248978}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1BF2; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 83,627 |
| Kinetics | |
| Metal Binding | METAL 154; /note="Calcium"; /evidence="ECO:0000269|PubMed:9719642, ECO:0007744|PDB:1BF2"; METAL 255; /note="Calcium"; /evidence="ECO:0000269|PubMed:9719642, ECO:0007744|PDB:1BF2"; METAL 256; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:9719642, ECO:0007744|PDB:1BF2"; METAL 258; /note="Calcium"; /evidence="ECO:0000269|PubMed:9719642, ECO:0007744|PDB:1BF2"; METAL 285; /note="Calcium"; /evidence="ECO:0000269|PubMed:9719642, ECO:0007744|PDB:1BF2" |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.68; |