| IED ID | IndEnz0001000361 |
| Enzyme Type ID | amylase000361 |
| Protein Name |
Sucrase-isomaltase, intestinal Cleaved into: Sucrase EC 3.2.1.48 ; Isomaltase EC 3.2.1.10 |
| Gene Name | Si |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MAKKKFSALEISLIVLFIIVTAIAIALVTVLATKVPAVEEIKSPTPTSNSTPTSTPTSTSTPTSTSTPSPGKCPPEQGEPINERINCIPEQHPTKAICEERGCCWRPWNNTVIPWCFFADNHGYNAESITNENAGLKATLNRIPSPTLFGEDIKSVILTTQTQTGNRFRFKITDPNNKRYEVPHQFVKEETGIPAADTLYDVQVSENPFSIKVIRKSNNKVLCDTSVGPLLYSNQYLQISTRLPSEYIYGFGGHIHKRFRHDLYWKTWPIFTRDEIPGDNNHNLYGHQTFFMGIGDTSGKSYGVFLMNSNAMEVFIQPTPIITYRVTGGILDFYIFLGDTPEQVVQQYQEVHWRPAMPAYWNLGFQLSRWNYGSLDTVSEVVRRNREAGIPYDAQVTDIDYMEDHKEFTYDRVKFNGLPEFAQDLHNHGKYIIILDPAISINKRANGAEYQTYVRGNEKNVWVNESDGTTPLIGEVWPGLTVYPDFTNPQTIEWWANECNLFHQQVEYDGLWIDMNEVSSFIQGSLNLKGVLLIVLNYPPFTPGILDKVMYSKTLCMDAVQHWGKQYDVHSLYGYSMAIATEQAVERVFPNKRSFILTRSTFGGSGRHANHWLGDNTASWEQMEWSITGMLEFGIFGMPLVGATSCGFLADTTEELCRRWMQLGAFYPFSRNHNAEGYMEQDPAYFGQDSSRHYLTIRYTLLPFLYTLFYRAHMFGETVARPFLYEFYDDTNSWIEDTQFLWGPALLITPVLRPGVENVSAYIPNATWYDYETGIKRPWRKERINMYLPGDKIGLHLRGGYIIPTQEPDVTTTASRKNPLGLIVALDDNQAAKGELFWDDGESKDSIEKKMYILYTFSVSNNELVLNCTHSSYAEGTSLAFKTIKVLGLREDVRSITVGENDQQMATHTNFTFDSANKILSITALNFNLAGSFIVRWCRTFSDNEKFTCYPDVGTATEGTCTQRGCLWQPVSGLSNVPPYYFPPENNPYTLTSIQPLPTGITAELQLNPPNARIKLPSNPISTLRVGVKYHPNDMLQFKIYDAQHKRYEVPVPLNIPDTPTSSNERLYDVEIKENPFGIQVRRRSSGKLIWDSRLPGFGFNDQFIQISTRLPSNYLYGFGEVEHTAFKRDLNWHTWGMFTRDQPPGYKLNSYGFHPYYMALENEGNAHGVLLLNSNGMDVTFQPTPALTYRTIGGILDFYMFLGPTPEIATRQYHEVIGFPVMPPYWALGFQLCRYGYRNTSEIEQLYNDMVAANIPYDVQYTDINYMERQLDFTIGERFKTLPEFVDRIRKDGMKYIVILAPAISGNETQPYPAFERGIQKDVFVKWPNTNDICWPKVWPDLPNVTIDETITEDEAVNASRAHVAFPDFFRNSTLEWWAREIYDFYNEKMKFDGLWIDMNEPSSFGIQMGGKVLNECRRMMTLNYPPVFSPELRVKEGEGASISEAMCMETEHILIDGSSVLQYDVHNLYGWSQVKPTLDALQNTTGLRGIVISRSTYPTTGRWGGHWLGDNYTTWDNLEKSLIGMLELNLFGIPYIGADICGVFHDSGYPSLYFVGIQVGAFYPYPRESPTINFTRSQDPVSWMKLLLQMSKKVLEIRYTLLPYFYTQMHEAHAHGGTVIRPLMHEFFDDKETWEIYKQFLWGPAFMVTPVVEPFRTSVTGYVPKARWFDYHTGADIKLKGILHTFSAPFDTINLHVRGGYILPCQEPARNTHLSRQNYMKLIVAADDNQMAQGTLFGDDGESIDTYERGQYTSIQFNLNQTTLTSTVLANGYKNKQEMRLGSIHIWGKGTLRISNANLVYGGRKHQPPFTQEEAKETLIFDLKNMNVTLDEPIQITWS |
| Enzyme Length | 1841 |
| Uniprot Accession Number | P23739 |
| Absorption | |
| Active Site | ACT_SITE 514; /note=Nucleophile; for isomaltase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10066; ACT_SITE 615; /note=For isomaltase activity; /evidence=ECO:0000250; ACT_SITE 1399; /note=Nucleophile; for sucrase activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU10066; ACT_SITE 1402; /note=For sucrase activity; /evidence=ECO:0000250; ACT_SITE 1512; /note=Proton donor; for sucrase activity; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 274; /note=Substrate; /evidence=ECO:0000250; BINDING 398; /note=Substrate; /evidence=ECO:0000250; BINDING 599; /note=Substrate; /evidence=ECO:0000250; BINDING 673; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action.; EC=3.2.1.48; CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.; EC=3.2.1.10; |
| DNA Binding | |
| EC Number | 3.2.1.48; 3.2.1.10 |
| Enzyme Function | FUNCTION: Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (5); Binding site (4); Chain (3); Compositional bias (1); Disulfide bond (4); Domain (2); Glycosylation (16); Modified residue (4); Region (3); Sequence conflict (21); Topological domain (2); Transmembrane (1) |
| Keywords | Cell membrane;Direct protein sequencing;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Membrane;Multifunctional enzyme;Phosphoprotein;Reference proteome;Repeat;Signal-anchor;Sulfation;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein. Note=Brush border. |
| Modified Residue | MOD_RES 7; /note=Phosphoserine; by PKA; /evidence=ECO:0000250|UniProtKB:P14410; MOD_RES 401; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 410; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 1387; /note=Sulfotyrosine; /evidence=ECO:0000255 |
| Post Translational Modification | PTM: The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen.; PTM: Sulfated. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10864000; 12940455; 15138292; 15309444; 15539244; 16964428; 17673438; 18313392; 18617558; 19352013; 22896899; 7873573; 8890076; 9202095; 9585003; 9618286; 9724271; 9878708; |
| Motif | |
| Gene Encoded By | |
| Mass | 210,350 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.10; |