IED ID | IndEnz0001000238 |
Enzyme Type ID | amylase000238 |
Protein Name |
Alpha-amylase/trypsin inhibitor CMd Chloroform/methanol-soluble protein CMd |
Gene Name | IAT3 CMD2 |
Organism | Hordeum vulgare (Barley) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Pooideae Triticodae Triticeae Hordeinae Hordeum Hordeum vulgare (Barley) |
Enzyme Sequence | MACKSSRSLLLLATVMVSVFAAAAAAAAATDCSPGVAFPTNLLGHCRDYVLQQTCAVFTPGSKLPEWMTSAELNYPGQPYLAKLYCCQELAEIPQQCRCEALRYFMALPVPSQPVDPSTGNVGQSGLMDLPGCPREMQRDFVRLLVAPGQCNLATIHNVRYCPAVEQPLWI |
Enzyme Length | 171 |
Uniprot Accession Number | P11643 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Part of a complex with inhibitory activity, but CMd is inactive as a separate subunit. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Signal peptide (1) |
Keywords | Alpha-amylase inhibitor;Direct protein sequencing;Disulfide bond;Protease inhibitor;Secreted;Serine protease inhibitor;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | PTM: Five disulfide bonds are present (Probable), which are essential for the inhibitor activity. |
Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000269|PubMed:8125056 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 18,526 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |