| IED ID | IndEnz0001000155 |
| Enzyme Type ID | amylase000155 |
| Protein Name |
Isoamylase 1, chloroplastic OsISA1 EC 3.2.1.68 Protein SUGARY-1 |
| Gene Name | ISA1 ISA SU1 Os08g0520900 LOC_Os08g40930 |
| 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 | MASLPHCLSARPLVVAAAPGRPGPGPGPWLRGGARRRNAAFSAGNAGRRVGLRRSVASAVEVGVGEDEEEGVEEEEEEVEAVVMPERYALGGACRVLAGMPAPLGATALDGGVNFAVYSAGASAASLCLFTPDDLEADEVTEEVPLDPLFNRTGNVWHVFIEGELHNMLYGYRFDGMFAPHCGQYFDVSNVVVDPYAKAVISRGEYGVPGPGGDCWPQMAGMIPLPYSTFDWQGDLPLRYPQKDLVIYEMHLRGFTKHSSSNVEHPGTYIGAISKLDYLKELGVNCVELMPCHEFNELEYFSCSSKMNFWGYSTINFFSPMIRYSSGGIRNCGRDAINEFKTFVREAHKRGIEVIMDVVFNHTAEGNEKGPILSFRGIDNSTYYMLAPKGEFYNYSGCGNTFNCNHPVVREFIVDCLRYWVTEMHVDGFRFDLASIMTRGCSLWDPVNVYGSPVEGDMTTTGTPLATPPLIDMISNDPILGDVKLIAEAWDAGGLYQVGQFPHWKIWSEWNGKYRDIVRQFIKGTDGFAGGFAECLCGSPHLYQAGGRKPWHSINFVCAHDGFTLADLVTYNKKYNSSNGEDNRDGENHNLSWNCGEEGEFAGLSVKRLRKRQMRNFFVSLMVSQGVPMFYMGDEYGHTKGGNNNTYCHDHYVNYFRWDKKEESSDLQRFCSLMTKFRKQCESLGLADFPTAQRLHWHGHQPGKPDWSETSRFVAFSTKDETKGEIYVAFNASHLPAVVGLPERPGYRWEPLVDTGKPAPYDFLTDDLPDRAHAVHLFSHFLNSNLYPMLSYSSIILELQPDD |
| Enzyme Length | 803 |
| Uniprot Accession Number | D0TZF0 |
| Absorption | |
| Active Site | ACT_SITE 432; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04746; ACT_SITE 488; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P04746 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by copper chloride, mercury chloride, ammonium molybdate and para-chloromercuribenzoate. {ECO:0000269|PubMed:10333591}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins.; EC=3.2.1.68; Evidence={ECO:0000269|PubMed:10333591}; |
| DNA Binding | |
| EC Number | 3.2.1.68 |
| Enzyme Function | FUNCTION: Starch-debranching enzyme involved in amylopectin biosynthesis in endosperm. Functions by removing excess branches or improper branches that interfere with the formation of double helices of the cluster chains of amylopectin and crystallization of starch (PubMed:10517831, PubMed:15618430, PubMed:16953433, PubMed:21436381). Works as ISA1 homooligomer or together with ISA2 as heterooligomer. The heterooligomer ISA1 and ISA2 possesses higher affinity than the ISA1 homooligomer for various branched polyglucans in vitro, but no marked differences exist in chain preferences for debranching of amylopectin and phytoglycogen between these forms (PubMed:16953433, PubMed:21436381). {ECO:0000269|PubMed:10517831, ECO:0000269|PubMed:15618430, ECO:0000269|PubMed:16953433, ECO:0000269|PubMed:21436381}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 at 30 degrees Celsius. {ECO:0000269|PubMed:10333591}; |
| Pathway | PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}. |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Erroneous initiation (2); Frameshift (1); Sequence caution (1); Site (1); Transit peptide (1) |
| Keywords | Carbohydrate metabolism;Chloroplast;Direct protein sequencing;Glycosidase;Hydrolase;Plastid;Reference proteome;Starch biosynthesis;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 | 89,661 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.68; |