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; |