| IED ID | IndEnz0001000467 |
| Enzyme Type ID | amylase000467 |
| Protein Name |
Beta-amylase 2, chloroplastic OsBamy2 EC 3.2.1.2 4-alpha-D-glucan maltohydrolase |
| Gene Name | BAMY2 Os03g0141200 LOC_Os03g04770 OsJ_09355 |
| 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 | MMSLNLAHQTGAAAAVAPAAPRTAVVAAAAGTVSAPAVAPAAAPSLQLQTQTVDPAAPAQGPDLPMAFQALVESLPEEQHPDVGGEERRKVGVPVYVMMPLDTVRKDGNGLNRRKAVEASLKALKSAGAEGIMVDVWWGIAECEGPGRYNFTGYMELMEMAKKNGLKVQAVMSFHQCGGNVGDSVTIPLPKWVLEEMDKDQDLAYTDRSGRRNYEYLSLGADAMPVLKGRTPVQCYGDFMRAFRDHFAAFMGNTIVEIQVGMGPAGELRYPSYPESNGTWRFPGIGEFQCYDRYMLSSLKAAAEAVGKPEWGNAGPGDSGGYNDWPEDSPFFRREGGWNTPYGEFFMSWYSQMLLEHGERILSAASGVYTGTPGVKISVKVAGIHWHYGTRSHAAELTAGYYNTRHHDGYQPIARMLARHGAVLNFTCVEMRNHEQPQDAQCRPEELVQQVAAAARESGVGLAGENALPRYDETAHDQIVTTAAEKAEEERMVAFTYLRMGPDLFQPDNWRRFAAFVKRMTESGVRDVCREQVEREAQGVAHATGSLVHEAAVALSN |
| Enzyme Length | 557 |
| Uniprot Accession Number | Q10RZ1 |
| Absorption | |
| Active Site | ACT_SITE 267; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P10538, ECO:0000255|PROSITE-ProRule:PRU10050"; ACT_SITE 465; /note="Proton acceptor"; /evidence="ECO:0000250|UniProtKB:P10538" |
| Activity Regulation | |
| Binding Site | BINDING 135; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 175; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 183; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 380; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 385; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 427; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P10538; BINDING 499; /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); Erroneous initiation (1); Region (1); 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 | 60,757 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |