| IED ID | IndEnz0001000001 |
| Enzyme Type ID | amylase000001 |
| Protein Name |
Beta-amylase 3, chloroplastic EC 3.2.1.2 1,4-alpha-D-glucan maltohydrolase Beta-amylase 8 Chloroplast beta-amylase CT-BMY |
| Gene Name | BAM3 BMY8 CTBMY At4g17090 dl4575c FCAALL.5 |
| 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 | MELTLNSSSSLIKRKDAKSSRNQESSSNNMTFAKMKPPTYQFQAKNSVKEMKFTHEKTFTPEGETLEKWEKLHVLSYPHSKNDASVPVFVMLPLDTVTMSGHLNKPRAMNASLMALKGAGVEGVMVDAWWGLVEKDGPMNYNWEGYAELIQMVQKHGLKLQVVMSFHQCGGNVGDSCSIPLPPWVLEEISKNPDLVYTDKSGRRNPEYISLGCDSVPVLRGRTPIQVYSDFMRSFRERFEGYIGGVIAEIQVGMGPCGELRYPSYPESNGTWRFPGIGEFQCYDKYMKSSLQAYAESIGKTNWGTSGPHDAGEYKNLPEDTEFFRRDGTWNSEYGKFFMEWYSGKLLEHGDQLLSSAKGIFQGSGAKLSGKVAGIHWHYNTRSHAAELTAGYYNTRNHDGYLPIAKMFNKHGVVLNFTCMEMKDGEQPEHANCSPEGLVKQVQNATRQAGTELAGENALERYDSSAFGQVVATNRSDSGNGLTAFTYLRMNKRLFEGQNWQQLVEFVKNMKEGGHGRRLSKEDTTGSDLYVGFVKGKIAENVEEAALV |
| Enzyme Length | 548 |
| Uniprot Accession Number | O23553 |
| Absorption | |
| Active Site | ACT_SITE 259; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 456; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Redox regulation; active in reducing conditions, inactive in oxidizing conditions. {ECO:0000250}. |
| Binding Site | BINDING 127; /note=Substrate; /evidence=ECO:0000250; BINDING 167; /note=Substrate; /evidence=ECO:0000250; BINDING 175; /note=Substrate; /evidence=ECO:0000250; BINDING 371; /note=Substrate; /evidence=ECO:0000250; BINDING 376; /note=Substrate; /evidence=ECO:0000250; BINDING 418; /note=Substrate; /evidence=ECO:0000250; BINDING 489; /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. No alpha-amylase activity. Involved in cold resistance. Mediates the accumulation of maltose upon freezing stress, thus contributing to the protection of the photosynthetic electron transport chain. Plays a role in the circadian-regulated starch degradation and maltose metabolism in chloroplasts, especially at night. More active on phosphorylated glucan. Interacts directly with starch or other alpha-1,4-glucan. {ECO:0000269|PubMed:10652124, ECO:0000269|PubMed:16055686, ECO:0000269|PubMed:16297066, ECO:0000269|PubMed:17631522, ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:19664588}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-7. {ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:19664588}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (7); Chain (1); Compositional bias (1); Erroneous initiation (2); Erroneous termination (2); Region (2); Transit peptide (1) |
| Keywords | Carbohydrate metabolism;Chloroplast;Glycosidase;Hydrolase;Plastid;Polysaccharide degradation;Reference proteome;Transit peptide |
| Interact With | |
| Induction | INDUCTION: By cold stress. Light-mediated circadian regulation; highest levels at dawn and at dusk in long days (LD) but only at dusk in short days (SD). Repressed by trehalose in a ABI4-dependent manner, this effect is reversed in the presence of sucrose. {ECO:0000269|PubMed:16055686, ECO:0000269|PubMed:16297066, ECO:0000269|PubMed:17031512}. |
| Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:10652124, ECO:0000269|PubMed:16698902, ECO:0000269|PubMed:18390594}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11118138; 11351099; 15347792; 15862090; 16258011; 18419779; 18650403; 18775970; 18818313; 19502356; 20546137; 20674078; 21683882; 22789914; 22898356; 23393426; 23452177; 24561248; 25293962; 26628055; 26792489; 26896394; 27436713; 28152100; 28225829; 29066669; 29309132; 29932910; 30065159; 30348315; 31186142; 31266901; 32072133; |
| Motif | |
| Gene Encoded By | |
| Mass | 61,353 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.2; |