| IED ID | IndEnz0001000492 |
| Enzyme Type ID | amylase000492 |
| Protein Name |
Alpha-amylase inhibitor/endochitinase EC 3.2.1.14 Fragments |
| Gene Name | |
| Organism | Coix lacryma-jobi (Job's tears) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae PACMAD clade Panicoideae Andropogonodae Andropogoneae Rottboelliinae Coix Coix lacryma-jobi (Job's tears) |
| Enzyme Sequence | CCSKFGYCGLTDAYNFYTGQLTSFAHVTHETGNNAYCDPSKTQKPCAAGKKYYGRGPIQISXNYNYGPAGRAIGMDGLGNPDRVAQDALDDYKTALXFLVNGEEAVPGLSAANAVSYYRQYCQQLGVDPGPNL |
| Enzyme Length | 133 |
| Uniprot Accession Number | P15326 |
| Absorption | |
| Active Site | ACT_SITE 30; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P29022 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; |
| DNA Binding | |
| EC Number | 3.2.1.14 |
| Enzyme Function | FUNCTION: This protein functions both as an alpha-amylase inhibitor and as a chitinase. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Natural variant (3); Non-adjacent residues (5); Non-terminal residue (2) |
| Keywords | Alpha-amylase inhibitor;Carbohydrate metabolism;Chitin degradation;Chitin-binding;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation |
| 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 | 14,305 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |