| IED ID | IndEnz0001000890 |
| Enzyme Type ID | amylase000890 |
| Protein Name |
Beta-amylase 1, chloroplastic OsBamy1 EC 3.2.1.2 4-alpha-D-glucan maltohydrolase |
| Gene Name | BAMY1 Os10g0465700 LOC_Os10g32810 OSJNBa0006L06.1 |
| Organism | Oryza sativa subsp. japonica (Rice) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae BOP clade Oryzoideae Oryzeae Oryzinae Oryza Oryza sativa (Rice) Oryza sativa subsp. japonica (Rice) |
| Enzyme Sequence | MALNLAQSAAAAACFATAGDARRAASVVAMPSSSSSATTSLRMKRQAACEPVACRAVARHVAAAAASSRRNGVPVFVMMPLDTVSKCGSALNRRKAVAASLAALKSAGVEGIMVDVWWGIVESEGPGRYNFDGYVELMEMARKTGLKVQAVMSFHQCGGNVGDSVNIPLPRWVVEEMEKDNDLAYTDQWGRRNFEYISLGCDAMPVFKGRTPVECYTDFMRAFRDHFASFLGDTIVEIQVGMGPAGELRYPSYPESNGTWRFPGIGAFQCNDRYMRSSLKAAAEARGKPEWGHGGPTDAGGYNNWPEDTVFFRGDCGGWSTEYGEFFLSWYSQMLLEHGERVLSGATSVFGDGAGAKISVKVAGIHWHYGTRSHAPELTAGYYNTRHRDGYLPIARMLARHGAVLNFTCVEMRDHEQPQEAQCMPEALVRQVAAAARAAGVGLAGENALPRYDGTAHDQVVAAAADRAAEDRMVAFTYLRMGPDLFHPDNWRRFVAFVRRMSESGSPREAAESAAHGVAQATGSLVHEAAVALRS |
| Enzyme Length | 535 |
| Uniprot Accession Number | Q9AV88 |
| Absorption | |
| Active Site | ACT_SITE 247; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P10538, ECO:0000255|PROSITE-ProRule:PRU10050"; ACT_SITE 446; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P10538" |
| Activity Regulation | |
| Binding Site | BINDING 115; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 155; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 163; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 361; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 366; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 408; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 480; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538 |
| 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; Evidence={ECO:0000269|PubMed:21512221}; |
| DNA Binding | |
| EC Number | 3.2.1.2 |
| Enzyme Function | FUNCTION: Possesses beta-amylase activity in vitro (PubMed:21512221). May be involved in cold resistance by mediating the accumulation of maltose upon freezing stress, thus contributing to the protection of membranes (Probable). {ECO:0000269|PubMed:21512221, ECO:0000305}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:21512221}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:21512221}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (7); Chain (1); Region (1); Sequence conflict (3); Transit peptide (1) |
| Keywords | Carbohydrate metabolism;Chloroplast;Glycosidase;Hydrolase;Plastid;Polysaccharide degradation;Reference proteome;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 57,952 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |