| IED ID | IndEnz0001000360 |
| Enzyme Type ID | amylase000360 |
| Protein Name |
Sucrase-isomaltase, intestinal Cleaved into: Sucrase EC 3.2.1.48 ; Isomaltase EC 3.2.1.10 |
| Gene Name | SI |
| Organism | Oryctolagus cuniculus (Rabbit) |
| 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) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit) |
| Enzyme Sequence | MAKRKFSGLEITLIVLFVIVFIIAIALIAVLATKTPAVEEVNPSSSTPTTTSTTTSTSGSVSCPSELNEVVNERINCIPEQSPTQAICAQRNCCWRPWNNSDIPWCFFVDNHGYNVEGMTTTSTGLEARLNRKSTPTLFGNDINNVLLTTESQTANRLRFKLTDPNNKRYEVPHQFVTEFAGPAATETLYDVQVTENPFSIKVIRKSNNRILFDSSIGPLVYSDQYLQISTRLPSEYMYGFGEHVHKRFRHDLYWKTWPIFTRDQHTDDNNNNLYGHQTFFMCIEDTTGKSFGVFLMNSNAMEIFIQPTPIVTYRVIGGILDFYIFLGDTPEQVVQQYQELIGRPAMPAYWSLGFQLSRWNYNSLDVVKEVVRRNREALIPFDTQVSDIDYMEDKKDFTYDRVAYNGLPDFVQDLHDHGQKYVIILDPAISINRRASGEAYESYDRGNAQNVWVNESDGTTPIVGEVWPGDTVYPDFTSPNCIEWWANECNIFHQEVNYDGLWIDMNEVSSFVQGSNKGCNDNTLNYPPYIPDIVDKLMYSKTLCMDSVQYWGKQYDVHSLYGYSMAIATERAVERVFPNKRSFILTRSTFAGSGRHAAHWLGDNTATWEQMEWSITGMLEFGLFGMPLVGADICGFLAETTEELCRRWMQLGAFYPFSRNHNADGFEHQDPAFFGQDSLLVKSSRHYLNIRYTLLPFLYTLFYKAHAFGETVARPVLHEFYEDTNSWVEDREFLWGPALLITPVLTQGAETVSAYIPDAVWYDYETGAKRPWRKQRVEMSLPADKIGLHLRGGYIIPIQQPAVTTTASRMNPLGLIIALNDDNTAVGDFFWDDGETKDTVQNDNYILYTFAVSNNNLNITCTHELYSEGTTLAFQTIKILGVTETVTQVTVAENNQSMSTHSNFTYDPSNQVLLIENLNFNLGRNFRVQWDQTFLESEKITCYPDADIATQEKCTQRGCIWDTNTVNPRAPECYFPKTDNPYSVSSTQYSPTGITADLQLNPTRTRITLPSEPITNLRVEVKYHKNDMVQFKIFDPQNKRYEVPVPLDIPATPTSTQENRLYDVEIKENPFGIQIRRRSTGKVIWDSCLPGFAFNDQFIQISTRLPSEYIYGFGEAEHTAFKRDLNWHTWGMFTRDQPPGYKLNSYGFHPYYMALEDEGNAHGVLLLNSNAMDVTFMPTPALTYRVIGGILDFYMFLGPTPEVATQQYHEVIGHPVMPPYWSLGFQLCRYGYRNTSEIIELYEGMVAADIPYDVQYTDIDYMERQLDFTIDENFRELPQFVDRIRGEGMRYIIILDPAISGNETRPYPAFDRGEAKDVFVKWPNTSDICWAKVWPDLPNITIDESLTEDEAVNASRAHAAFPDFFRNSTAEWWTREILDFYNNYMKFDGLWIDMNEPSSFVNGTTTNVCRNTELNYPPYFPELTKRTDGLHFRTMCMETEHILSDGSSVLHYDVHNLYGWSQAKPTYDALQKTTGKRGIVISRSTYPTAGRWAGHWLGDNYARWDNMDKSIIGMMEFSLFGISYTGADICGFFNDSEYHLCTRWTQLGAFYPFARNHNIQFTRRQDPVSWNQTFVEMTRNVLNIRYTLLPYFYTQLHEIHAHGGTVIRPLMHEFFDDRTTWDIFLQFLWGPAFMVTPVLEPYTTVVRGYVPNARWFDYHTGEDIGIRGQVQDLTLLMNAINLHVRGGHILPCQEPARTTFLSRQKYMKLIVAADDNHMAQGSLFWDDGDTIDTYERDLYLSVQFNLNKTTLTSTLLKTGYINKTEIRLGYVHVWGIGNTLINEVNLMYNEINYPLIFNQTQAQEILNIDLTAHEVTLDDPIEISWS |
| Enzyme Length | 1827 |
| Uniprot Accession Number | P07768 |
| Absorption | |
| Active Site | ACT_SITE 505; /note=Nucleophile; for isomaltase activity; ACT_SITE 604; /note=For isomaltase activity; /evidence=ECO:0000250; ACT_SITE 1394; /note=Nucleophile; for sucrase activity; ACT_SITE 1397; /note=For sucrase activity; ACT_SITE 1500; /note=Proton donor; for sucrase activity; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 264; /note=Substrate; /evidence=ECO:0000250; BINDING 388; /note=Substrate; /evidence=ECO:0000250; BINDING 588; /note=Substrate; /evidence=ECO:0000250; BINDING 662; /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); Disulfide bond (5); Domain (2); Glycosylation (17); Initiator methionine (1); Modified residue (5); Region (3); 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 391; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 400; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 1382; /note=Sulfotyrosine; /evidence=ECO:0000255; MOD_RES 1385; /note=Sulfotyrosine; /evidence=ECO:0000255 |
| Post Translational Modification | PTM: The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen.; PTM: N- and O-glycosylated.; PTM: Sulfated. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 210,140 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.10; |