Detail Information for IndEnz0001000612
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