| IED ID | IndEnz0001000022 |
| Enzyme Type ID | amylase000022 |
| Protein Name |
Alpha-amylase 1 AtAMY1 EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
| Gene Name | AMY1 At4g25000 F13M23.140 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MTSLHTLLFSSLLFFIVFPTFTFSSTLLFQSFNWESWKKEGGFYNSLHNSIDDIANAGITHLWLPPPSQSVAPEGYLPGKLYDLNSSKYGSEAELKSLIKALNQKGIKALADIVINHRTAERKDDKCGYCYFEGGTSDDRLDWDPSFVCRNDPKFPGTGNLDTGGDFDGAPDIDHLNPRVQKELSEWMNWLKTEIGFHGWRFDYVRGYASSITKLYVQNTSPDFAVGEKWDDMKYGGDGKLDYDQNEHRSGLKQWIEEAGGGVLTAFDFTTKGILQSAVKGELWRLKDSQGKPPGMIGIMPGNAVTFIDNHDTFRTWVFPSDKVLLGYVYILTHPGTPCIFYNHYIEWGLKESISKLVAIRNKNGIGSTSSVTIKAAEADLYLAMIDDKVIMKIGPKQDVGTLVPSNFALAYSGLDFAVWEKK |
| Enzyme Length | 423 |
| Uniprot Accession Number | Q8VZ56 |
| Absorption | |
| Active Site | ACT_SITE 203; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04063; ACT_SITE 228; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04063 |
| Activity Regulation | |
| Binding Site | BINDING 230; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 292; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 311; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 393; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 420; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:17324226}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | FUNCTION: Possesses alpha-amylase activity in vitro, but seems not required for breakdown of transitory starch in leaves. {ECO:0000269|PubMed:17324226}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (5); Chain (1); Erroneous gene model prediction (2); Metal binding (13); Region (3); Sequence conflict (1); Signal peptide (1); Site (1) |
| Keywords | Apoplast;Carbohydrate metabolism;Glycosidase;Hydrolase;Metal-binding;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: By gibberellin, abscisic acid (ABA), heat shock and infection with the bacterial pathogen P.syringae. Not regulated by transition from dark to light. Triggered by NAC072/RD26 during senescence (PubMed:29659022). {ECO:0000269|PubMed:15347792, ECO:0000269|PubMed:15927942, ECO:0000269|PubMed:17324226, ECO:0000269|PubMed:29659022}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000305|PubMed:17324226}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10899464; 15047901; 15665241; 15749471; 15862090; 15908439; 16553896; 17189325; 18307990; 18650403; 19225807; 19250611; 23393426; 29490615; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,378 |
| Kinetics | |
| Metal Binding | METAL 116; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P04063; METAL 133; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P04063; METAL 136; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04063; METAL 138; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04063; METAL 142; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P04063; METAL 152; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P04063; METAL 162; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P04063; METAL 166; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P04063; METAL 167; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04063; METAL 170; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04063; METAL 172; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P04063; METAL 172; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P04063; METAL 207; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P04063 |
| Rhea ID | |
| Cross Reference Brenda |