| IED ID | IndEnz0001000614 |
| Enzyme Type ID | amylase000614 |
| Protein Name |
Glycogen debranching enzyme Glycogen debrancher Includes: 4-alpha-glucanotransferase EC 2.4.1.25 Oligo-1,4-1,4-glucantransferase ; Amylo-alpha-1,6-glucosidase Amylo-1,6-glucosidase EC 3.2.1.33 Dextrin 6-alpha-D-glucosidase |
| Gene Name | AGL |
| Organism | Equus caballus (Horse) |
| 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 Laurasiatheria Perissodactyla (odd-toed ungulates) Equidae (horses) Equus Equus Equus caballus (Horse) |
| Enzyme Sequence | MGHSKQIRTLLLNEMEKLEKTLFRLEQGFELQFRLGPTLQGKAVTVYTNYPFPGETFNREKFHSLQWENPTEREDDSDKYCKLNLQQAGSFQYYFLQGNEKSGGGYIVVDPILRVGADNHVLPLDCVTLQTFLTKCLGPFDEWESRLRVAKESGYNMIHFTPLQTLGLSRSSYSLADQLELNPDFSRPNKKYTWHDVGQLVEKLKKEWDILCITDVVYNHTAANSKWIHEHPESAYNLVNSPHLKPAWVLDRALWHLSCDVAEGKYREKGVPALIENDHQMNCIRKIIWEDIYPKIHLWEFFQVDVHKAVEQFRGLLTQENRKIISQPDPKQHLKIIQDPEYRRLGCTVDMNIALATFIPHDNGPAAIDECCNWFRKRIEELNAEKHQLVNYHQEQAVNCLLGNVFYERLAGHGPKLGPVTRKHPLVTRYFTFPFEEMTPSTEESMIHLPNKACFLMAHNGWVMGDDPLRNFAEPGSDVYLRRELICWGDSVKLRYGNKPEDCPYLWAHMKKYTEITATHFQGVRLDNCHSTPIHVAEYMLDAARKLQPNLYVVAELFTGSEDLDNIFVTRLGISSLIREAMSAADSHEEGRLVYRYGGEPVGSFVQPCLRPLMPAIAHALFMDITHDNECPIVHRSAYDALPSSTIVSMASCASGSTKGYDELVPHQISVVSEERFYTKWNPEALPSNTGEVNFQSGIIAARRAINKLHQELGAKGFIQVYVDQVDQDIVAVTRHSPSIHQSVVSVSRTAFRNPKTSFYSKEVPHMYIPGKIEEVVLEARTIERHTIPYKKDENSINGMPDITVEIREHIQLNESKIVKHAGIVTKGPNEFVQEIEFENLTPGSVIIFRVSLDPHAQVAVGILRNHLTQFSPHFKSGSLAVDNADPILKIPFASIASKLTLAELNQVLYRCESEEQEDGGGCYNIPNWSSLKYAGLQGLMSILAEIRPRNDLGHPFCDNLRSGDWMIDYVSSRLISRSGTIAEVGKWLQAMFLYLKQIPRYLIPCYFDAILIGAYTTLLDIAWKQMSSFVQNGSTFVKHLSLGSVQMCGVGKFPSLPLLSPSLTDLPYRVNEITKEKEQCCGSLAAGLPHFSAGIFRCWGRDTFIALRGLLLVTGRYLEARNIILAFAGTLRHGLIPNLLGEGTHARYNCRDAVWWWLQCIQDYCKIVPNGLDILRCPVSRMYPTDDSVPLSAGTVDQPLFEVIQEAMQRHVQGIQFRERNAGPQIDRNMKDEGFNITAGVDEETGFVYGGNRFNCGTWMDKMGESDRARNRGIPATPRDGSAVEIVGLSKSAVRWLLELSRKNIFPYHEVRVKRHGKFVTVSYDEWNRKIQDNFEKLFHVSEDPSDFNEKHPELVHKRGIYKDSYGASSPWCDYQLRPNFTIAMVVAPELFTPEKAWKALEIAEKKLLGPLGMKTLDPDDMVYCGIYDNALDNDNYNLAKGFNYHQGPEWLWPTGYFLRAKLYFSKLMGPETNAKTMFLVKNVLSRHYVHLERSPWKGLPELTNENGQYCPFSCETQAWSIATVLETLYDL |
| Enzyme Length | 1533 |
| Uniprot Accession Number | A8BQB4 |
| Absorption | |
| Active Site | ACT_SITE 527; /evidence=ECO:0000250|UniProtKB:P35573; ACT_SITE 530; /evidence=ECO:0000250|UniProtKB:P35573; ACT_SITE 628; /evidence=ECO:0000250|UniProtKB:P35573 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.; EC=2.4.1.25; Evidence={ECO:0000250|UniProtKB:P35573}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin.; EC=3.2.1.33; Evidence={ECO:0000250|UniProtKB:P35573}; |
| DNA Binding | |
| EC Number | 2.4.1.25; 3.2.1.33 |
| Enzyme Function | FUNCTION: Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation. {ECO:0000250|UniProtKB:P35573}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Chain (1); Modified residue (1); Natural variant (2); Region (2) |
| Keywords | Alternative splicing;Cytoplasm;Glycogen biosynthesis;Glycosidase;Glycosyltransferase;Hydrolase;Multifunctional enzyme;Phosphoprotein;Reference proteome;Transferase;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35573}. Note=Under glycogenolytic conditions localizes to the nucleus. {ECO:0000250|UniProtKB:P35573}. |
| Modified Residue | MOD_RES 64; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35573 |
| Post Translational Modification | PTM: Ubiquitinated. {ECO:0000250|UniProtKB:P35573}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 174,666 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.2.1.33; |