IED ID | IndEnz0001000617 |
Enzyme Type ID | amylase000617 |
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 | GDB1 YPR184W |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Enzyme Sequence | MNRSLLLRLSDTGEPITSCSYGKGVLTLPPIPLPKDAPKDQPLYTVKLLVSAGSPVARDGLVWTNCPPDHNTPFKRDKFYKKIIHSSFHEDDCIDLNVYAPGSYCFYLSFRNDNEKLETTRKYYFVALPMLYINDQFLPLNSIALQSVVSKWLGSDWEPILSKIAAKNYNMVHFTPLQERGESNSPYSIYDQLQFDQEHFKSPEDVKNLVEHIHRDLNMLSLTDIVFNHTANNSPWLVEHPEAGYNHITAPHLISAIELDQELLNFSRNLKSWGYPTELKNIEDLFKIMDGIKVHVLGSLKLWEYYAVNVQTALRDIKAHWNDESNESYSFPENIKDISSDFVKLASFVKDNVTEPNFGTLGERNSNRINVPKFIQLLKLINDGGSDDSESSLATAQNILNEVNLPLYREYDDDVSEILEQLFNRIKYLRLDDGGPKQGPVTVDVPLTEPYFTRFKGKDGTDYALANNGWIWNGNPLVDFASQNSRAYLRREVIVWGDCVKLRYGKSPEDSPYLWERMSKYIEMNAKIFDGFRIDNCHSTPIHVGEYFLDLARKYNPNLYVVAELFSGSETLDCLFVERLGISSLIREAMQAWSEEELSRLVHKHGGRPIGSYKFVPMDDFSYPADINLNEEHCFNDSNDNSIRCVSEIMIPKILTATPPHALFMDCTHDNETPFEKRTVEDTLPNAALVALCSSAIGSVYGYDEIFPHLLNLVTEKRHYDISTPTGSPSIGITKVKATLNSIRTSIGEKAYDIEDSEMHVHHQGQYITFHRMDVKSGKGWYLIARMKFSDNDDPNETLPPVVLNQSTCSLRFSYALERVGDEIPNDDKFIKGIPTKLKELEGFDISYDDSKKISTIKLPNEFPQGSIAIFETQQNGVDESLDHFIRSGALKATSSLTLESINSVLYRSEPEEYDVSAGEGGAYIIPNFGKPVYCGLQGWVSVLRKIVFYNDLAHPLSANLRNGHWALDYTISRLNYYSDEAGINEVQNWLRSRFDRVKKLPSYLVPSYFALIIGILYGCCRLKAIQLMSRNIGKSTLFVQSLSMTSIQMVSRMKSTSILPGENVPSMAAGLPHFSVNYMRCWGRDVFISLRGMLLTTGRFDEAKAHILAFAKTLKHGLIPNLLDAGRNPRYNARDAAWFFLQAVQDYVYIVPDGEKILQEQVTRRFPLDDTYIPVDDPRAFSYSSTLEEIIYEILSRHAKGIKFREANAGPNLDRVMTDKGFNVEIHVDWSTGLIHGGSQYNCGTWMDKMGESEKAGSVGIPGTPRDGAAIEINGLLKSALRFVIELKNKGLFKFSDVETQDGGRIDFTEWNQLLQDNFEKRYYVPEDPSQDADYDVSAKLGVNRRGIYRDLYKSGKPYEDYQLRPNFAIAMTVAPELFVPEHAIKAITIADEVLRGPVGMRTLDPSDYNYRPYYNNGEDSDDFATSKGRNYHQGPEWVWLYGYFLRAFHHFHFKTSPRCQNAAKEKPSSYLYQQLYYRLKGHRKWIFESVWAGLTELTNKDGEVCNDSSPTQAWSSACLLDLFYDLWDAYEDDS |
Enzyme Length | 1536 |
Uniprot Accession Number | Q06625 |
Absorption | |
Active Site | ACT_SITE 535; /evidence=ECO:0000250; ACT_SITE 538; /evidence=ECO:0000250; ACT_SITE 670; /evidence=ECO:0000250 |
Activity Regulation | ACTIVITY REGULATION: Activity is inhibited by IGD1. {ECO:0000269|PubMed:21585652}. |
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:0000269|PubMed:11094287, ECO:0000269|PubMed:21585652}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Region (2); Sequence conflict (6) |
Keywords | Cytoplasm;Direct protein sequencing;Glycogen biosynthesis;Glycosidase;Glycosyltransferase;Hydrolase;Mitochondrion;Multifunctional enzyme;Reference proteome;Transferase |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 11152943; 11283351; 11743162; 11805837; 12200270; 14690591; 16429126; 16554755; 18467557; 19536198; 20412306; 22842922; 23029052; 24040173; 24491554; 27085523; 27274529; 27312010; 27660105; |
Motif | |
Gene Encoded By | |
Mass | 174,972 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |