| IED ID | IndEnz0001000023 |
| Enzyme Type ID | amylase000023 |
| Protein Name |
Alpha-amylase 3, chloroplastic AtAMY3 EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase |
| Gene Name | AMY3 At1g69830 T17F3.14 |
| 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 | MSTVPIESLLHHSYLRHNSKVNRGNRSFIPISLNLRSHFTSNKLLHSIGKSVGVSSMNKSPVAIRATSSDTAVVETAQSDDVIFKEIFPVQRIEKAEGKIYVRLKEVKEKNWELSVGCSIPGKWILHWGVSYVGDTGSEWDQPPEDMRPPGSIAIKDYAIETPLKKLSEGDSFFEVAINLNLESSVAALNFVLKDEETGAWYQHKGRDFKVPLVDDVPDNGNLIGAKKGFGALGQLSNIPLKQDKSSAETDSIEERKGLQEFYEEMPISKRVADDNSVSVTARKCPETSKNIVSIETDLPGDVTVHWGVCKNGTKKWEIPSEPYPEETSLFKNKALRTRLQRKDDGNGSFGLFSLDGKLEGLCFVLKLNENTWLNYRGEDFYVPFLTSSSSPVETEAAQVSKPKRKTDKEVSASGFTKEIITEIRNLAIDISSHKNQKTNVKEVQENILQEIEKLAAEAYSIFRSTTPAFSEEGVLEAEADKPDIKISSGTGSGFEILCQGFNWESNKSGRWYLELQEKADELASLGFTVLWLPPPTESVSPEGYMPKDLYNLNSRYGTIDELKDTVKKFHKVGIKVLGDAVLNHRCAHFKNQNGVWNLFGGRLNWDDRAVVADDPHFQGRGNKSSGDNFHAAPNIDHSQDFVRKDIKEWLCWMMEEVGYDGWRLDFVRGFWGGYVKDYMDASKPYFAVGEYWDSLSYTYGEMDYNQDAHRQRIVDWINATSGAAGAFDVTTKGILHTALQKCEYWRLSDPKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPEGKEMQGYAYILTHPGTPAVFFDHIFSDYHSEIAALLSLRNRQKLHCRSEVNIDKSERDVYAAIIDEKVAMKIGPGHYEPPNGSQNWSVAVEGRDYKVWETS |
| Enzyme Length | 887 |
| Uniprot Accession Number | Q94A41 |
| Absorption | |
| Active Site | ACT_SITE 666; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04063; ACT_SITE 691; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04063 |
| Activity Regulation | ACTIVITY REGULATION: Redox-regulated, with the highest activity under reducing conditions. The midpoint redox potential is -329 mV. The disulfide bridge between Cys-499 and Cys-587 inhibits catalysis. Inhibited by CuCl(2) and H(2)O(2). {ECO:0000269|PubMed:24089528}. |
| Binding Site | BINDING 693; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 695; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P04063; BINDING 712; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 754; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 773; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 779; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 857; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P00693; BINDING 884; /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:24089528}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | FUNCTION: Possesses endoamylolytic activity in vitro, but seems not required for breakdown of transitory starch in leaves. May be involved in the determination of the final structure of glucans by shortening long linear phospho-oligosaccharides in the chloroplast stroma. Can act on both soluble and insoluble glucan substrates to release small linear and branched malto-oligosaccharides (PubMed:24089528). Works synergistically with beta-amylase toward efficient starch degradation (PubMed:24089528). Has activity against p-nitrophenyl maltoheptaoside (BPNP-G7), amylopectin and beta-limit dextrin (PubMed:24089528). Involved in stress-induced starch degradation (PubMed:27436713). {ECO:0000269|PubMed:15637061, ECO:0000269|PubMed:19074683, ECO:0000269|PubMed:19141707, ECO:0000269|PubMed:21294843, ECO:0000269|PubMed:24089528, ECO:0000269|PubMed:27436713}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 with p-nitrophenyl maltoheptaoside or amylopectin as substrate. {ECO:0000269|PubMed:24089528}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (8); Chain (1); Disulfide bond (1); Erroneous gene model prediction (1); Mutagenesis (6); Region (3); Site (1); Transit peptide (1) |
| Keywords | Carbohydrate metabolism;Chloroplast;Disulfide bond;Glycosidase;Hydrolase;Metal-binding;Plastid;Reference proteome;Transit peptide |
| Interact With | |
| Induction | INDUCTION: Circadian-regulation. Expression increases during the light phase and decreases during the dark phase. Up-regulated during osmotic stress and by abscisic acid (PubMed:27436713). {ECO:0000269|PubMed:15347792, ECO:0000269|PubMed:15637061, ECO:0000269|PubMed:27436713}. |
| Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:15637061, ECO:0000269|PubMed:21294843}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 14576160; 15028209; 15052571; 15665241; 15749471; 15862090; 16297066; 16367961; 16495218; 17324226; 17764576; 18230142; 18431481; 18616834; 18633119; 18650403; 18710561; 19038037; 19250611; 20674078; 22789914; 23019330; 23393426; 26774787; 27458017; 28152100; 31417599; 32354788; |
| Motif | |
| Gene Encoded By | |
| Mass | 99,842 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |