IED ID | IndEnz0001000357 |
Enzyme Type ID | amylase000357 |
Protein Name |
Isoamylase EC 3.2.1.68 |
Gene Name | iam |
Organism | Flavobacterium sp. |
Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Flavobacteriia Flavobacteriales Flavobacteriaceae Flavobacterium unclassified Flavobacterium Flavobacterium sp. |
Enzyme Sequence | MDPHAPQRQRSGQRLRALALAALACALSPAHAAIDAQQLGARYDAAQANLAFRVYSSRATRVEVFLYKNPTGSQEVARLALSKDPATQVWSLSLPTSTIKNTYGITGAVYYGYRAWGPNWPYDAAWTKGSATGFVSDVDNAGNRFNPNKLLLDPYAREISQDPNTATCADGTIYATGAAHRNKDSGLCASKGIALAADATSVGSKPTRALKDEVIYEVHVRGLTRNDDSVPAAERGTYKGAARKAAALAALGVTAVEFLPVQETQNDQNDVDPNSTAGDNYWGYMTLNYFAPDRRYAYDKSAGGPTREWKAMVKAFHDAGIKVYIDVVYNHTGEGGPWSGTDGLSVYNLLSFRGLDNPAYYSLSSDYKYPWDNTGVGGNYNTRHPIAQNLIVDSLAYWRDALGVDGFRFDLASVLGNSCQHGCFNFDKNDSGNALNRIVAELPPRPAAGGAGADLIAEPWAIGGNSYQVGGFPAGWAEWNGLYRDALRKKQNKLGVETVTPGTLATRFAGSNDLYGDDGRKPWHSINFVVAHDGFTLNDLYAYNDKQNNQPWPYGPSDGGEDHNLSWNQGGIVAEQRKAARTGLALLMLSAGVPMITGGDEALRTQFGNNNTYNLDSAANWLYWSRSALEADHETYTKRLIAFRKAHPALRPANFYSASDTNGNVMEQLRWFKPDGAQADSAYFNGADNHALAWRIDGSEFGDSASAIYVAYNGWSGAVDFKLPWPGTGKQWYRVTDTATWNEGPNAVALPGSETLIGGENTVYGMQARSLLLLIAK |
Enzyme Length | 777 |
Uniprot Accession Number | O32611 |
Absorption | |
Active Site | ACT_SITE 410; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 458; /note=Proton donor; /evidence=ECO:0000250 |
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; |
DNA Binding | |
EC Number | 3.2.1.68 |
Enzyme Function | FUNCTION: Has a high rate of hydrolysis for glycogen. Does not cleave pullulan. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-7.; |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Disulfide bond (1); Metal binding (5); Signal peptide (1); Site (1) |
Keywords | Calcium;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Signal |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..32; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 84,340 |
Kinetics | |
Metal Binding | METAL 162; /note=Calcium; /evidence=ECO:0000250; METAL 263; /note=Calcium; /evidence=ECO:0000250; METAL 264; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 266; /note=Calcium; /evidence=ECO:0000250; METAL 293; /note=Calcium; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |