| IED ID | IndEnz0001000002 |
| Enzyme Type ID | amylase000002 |
| Protein Name |
Beta-amylase 1, chloroplastic EC 3.2.1.2 1,4-alpha-D-glucan maltohydrolase Beta-amylase 7 Thioredoxin-regulated beta-amylase TR-BAMY |
| Gene Name | BAM1 BMY7 TRBAMY At3g23920 F14O13.12 |
| 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 | MALNLSHQLGVLAGTPIKSGEMTDSSLLSISPPSARMMTPKAMNRNYKAHGTDPSPPMSPILGATRADLSVACKAFAVENGIGTIEEQRTYREGGIGGKKEGGGGVPVFVMMPLDSVTMGNTVNRRKAMKASLQALKSAGVEGIMIDVWWGLVEKESPGTYNWGGYNELLELAKKLGLKVQAVMSFHQCGGNVGDSVTIPLPQWVVEEVDKDPDLAYTDQWGRRNHEYISLGADTLPVLKGRTPVQCYADFMRAFRDNFKHLLGETIVEIQVGMGPAGELRYPSYPEQEGTWKFPGIGAFQCYDKYSLSSLKAAAETYGKPEWGSTGPTDAGHYNNWPEDTQFFKKEGGGWNSEYGDFFLSWYSQMLLDHGERILSSAKSIFENMGVKISVKIAGIHWHYGTRSHAPELTAGYYNTRFRDGYLPIAQMLARHNAIFNFTCIEMRDHEQPQDALCAPEKLVNQVALATLAAEVPLAGENALPRYDDYAHEQILKASALNLDQNNEGEPREMCAFTYLRMNPELFQADNWGKFVAFVKKMGEGRDSHRCREEVEREAEHFVHVTQPLVQEAAVALTH |
| Enzyme Length | 575 |
| Uniprot Accession Number | Q9LIR6 |
| Absorption | |
| Active Site | ACT_SITE 279; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10050; ACT_SITE 477; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10050 |
| Activity Regulation | ACTIVITY REGULATION: Redox regulation; active in reducing conditions, inactive in oxidizing conditions. Thioredoxins f1, m1, and y1 mediate the reversible reductive activation of oxidized BAM1. {ECO:0000269|PubMed:16698902}. |
| Binding Site | BINDING 147; /note=Substrate; /evidence=ECO:0000250; BINDING 187; /note=Substrate; /evidence=ECO:0000250; BINDING 195; /note=Substrate; /evidence=ECO:0000250; BINDING 392; /note=Substrate; /evidence=ECO:0000250; BINDING 397; /note=Substrate; /evidence=ECO:0000250; BINDING 439; /note=Substrate; /evidence=ECO:0000250; BINDING 517; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.; EC=3.2.1.2; |
| DNA Binding | |
| EC Number | 3.2.1.2 |
| Enzyme Function | FUNCTION: Beta-amylase activity. Can use p-nitrophenyl maltopentaoside (PNPG5) as substrate only in reduced form. Can play a minor role in the starch degradation and maltose metabolism in chloroplasts during the night. More active on phosphorylated glucan. Interacts directly with starch or other alpha-1,4-glucan. {ECO:0000269|PubMed:17631522, ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:19664588}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8. {ECO:0000269|PubMed:16698902, ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:19664588}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (7); Chain (1); Disulfide bond (1); Modified residue (2); Mutagenesis (8); Region (1); Sequence conflict (1); Transit peptide (1) |
| Keywords | Carbohydrate metabolism;Chloroplast;Disulfide bond;Glycosidase;Hydrolase;Phosphoprotein;Plastid;Polysaccharide degradation;Reference proteome;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:16698902, ECO:0000269|PubMed:18390594}. |
| Modified Residue | MOD_RES 55; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18433157; MOD_RES 59; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18433157 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12535340; 15347792; 15862090; 16297066; 18650403; 18775970; 19502356; 20546137; 20876336; 22789914; 23393426; 25293962; 26139825; 26774787; 26792489; 26896394; 27436713; 27457991; 28152100; 29066669; 29309132; 29606214; 29932910; 30051514; 30348315; 30833711; 31186142; 31266901; 32072133; 32354788; |
| Motif | |
| Gene Encoded By | |
| Mass | 63,762 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.2; |