IED ID | IndEnz0001000612 |
Enzyme Type ID | amylase000612 |
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 | Canis lupus familiaris (Dog) (Canis familiaris) |
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 Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris) |
Enzyme Sequence | MGHSKQIRILLLNEMEKLEKTLFRLEQGFELQFRLGPTLQGKAVTVYTNYPFPGETFNREKFRSLEWENPTEREDDSDKYCKLNLQQAGSFQYYFLQGNEKSGGGYIVVDPILYVGADNHVLPLDCVTLQTFLAKCLGPFDEWESRLRVAKESGYNMIHFTPLQTLGLSRSCYSLANQLELNPDFSRPNKKYTWSDVGQLVEKMKKEWNVLCITDVVYNHTAANSKWIQEHPESAYNLVNSPHLKPAWVLDRALWHLSCDVAEGKYKEKGVPALIENDHQMNCIRKIIWEDIFPKIQLWEFFQVDVYKAVEQFRRLLTQENRKITTKPDPKEHLKIIQDPEYRRLGCTVDMNIALATFIPHDKGPAAIDECCNWFRKRIEELNSEKHQLVNYHQEQAVNCLLGNVFYERMAGHGPKLGPVTRKHPLVTRYFTFPFEEMTVSTEESMIHNPNKACFLMAHNGWVMGDDPLRNFAEPGSEVYLRRELICWGDSVKLRYGNKPEDCPYLWAHMKKYTEITATYFQGVRLDNCHSTPLHVAEYMLDAARKLQPNLYVVAELFTGSEDLDNIFVTRLGISSLIREAMSAYNSHEEGRLVYRYGGEPVGSFVQPCLRPLMPAIAHALFMDITHDNECPIVHRSEYDALPSTTIVSMACCASGSTKGYDELVPHQISVVSEERFYTKWNPGASPSNTGEVNFQSGIIAARCAINKLHQELGAQGFIQVYVDQVDEDIVAVTRHSPSIHQSVVSVSRTAFRNPKTSFYSKEVPQMCIPGKIEEVVLEARTIERNTKPYQKDKNSINGMPNITVEIREHIQLSESKIVKQAGVATKGPNEYIQEIEFENLSPGSVIIFRVSLDPHAQVAVGILRNHLTQFSPHFKSGSLAVENSDPILKIPFAFIASKLTLAELNQVLYRCEAEEQEDGGGCYDIPNWSSLKYAGLQGLMSVLAEIRPKNDLGHPFCDNLRSGDWMIDYVSNRLISRSGTIAEVGKWFQAMFFYLKQIPRYLIPCYFDAILIGAYTTLLDIAWKQMSSFVQNGSTFVKHLSLGSVQMCGVGKCPSLPLLSPSLMDVPYRLNEITKEKEQCCVSLAAGLPHFSSGIFRCWGRDTFIALRGLLLITGRYLEARNIILAFAGTLRHGLIPNLLGEGTYARYNCRDAVWWWLQCIQDYCKMVPNGLDILKCPVSRMYPTDDSVPLSAGTLDQPLFEVIQEVMQRHIQGIQFRERNAGPQIDRNMKDEGFNITAGVDEETGFVYGGNRLNCGTWMDKMGESDRARNRGIPATPRDGSAVEIVGLSKSTVRWLLELSKKRIFPYHEVRVKRHGKVVTISYDEWNKKIQDNFEKLFHVSEDPXDFNEKHPNLVHKRGIYKDSYGASSPWCDYQLRPNFTIAMVVAPELFTAEKAWKALEIAEKKLLGPLGMKTLDPDDMVYCGIYDNALDNDNYNLAKGFNYHQGPEWLWPVGYFLRAKLYFSKLMGPEANAKTVFLVKNILSRHYVHLERSPWKGLPELTNENGQYCPFSCETQAWSIATVLETLYDL |
Enzyme Length | 1533 |
Uniprot Accession Number | Q2PQH8 |
Absorption | |
Active Site | ACT_SITE 527; /evidence=ECO:0000250; ACT_SITE 530; /evidence=ECO:0000250; ACT_SITE 628; /evidence=ECO:0000250 |
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; CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin.; EC=3.2.1.33; |
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}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Modified residue (1); Region (2) |
Keywords | Cytoplasm;Glycogen biosynthesis;Glycogen storage disease;Glycosidase;Glycosyltransferase;Hydrolase;Multifunctional enzyme;Phosphoprotein;Reference proteome;Transferase;Ubl conjugation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Under glycogenolytic conditions localizes to the nucleus. {ECO:0000250}. |
Modified Residue | MOD_RES 64; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35573 |
Post Translational Modification | PTM: Ubiquitinated. {ECO:0000250}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 174,828 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |