IED Industry Enzyme Database

Detail Information for IndEnz0001000148
IED ID IndEnz0001000148
Enzyme Type ID amylase000148
Protein Name Glycogenin-1
GN-1
GN1
EC 2.4.1.186
Gene Name GYG1 GYG
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRLVVLATPQVSDSMRKVLETVFDEVIMVDVLDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFDREELSAAPDPGWPDCFNSGVFVYQPSVETYNQLLHLASEQGSFDGGDQGILNTFFSSWATTDIRKHLPFIYNLSSISIYSYLPAFKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPNMTHPEFLILWWNIFTTNVLPLLQQFGLVKDTCSYVNVLSDLVYTLAFSCGFCRKEDVSGAISHLSLGEIPAMAQPFVSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ
Enzyme Length 350
Uniprot Accession Number P46976
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by palladium ions. {ECO:0000269|PubMed:30356213}.
Binding Site BINDING 77; /note="Substrate"; /evidence="ECO:0000269|PubMed:22160680, ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N, ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V, ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X"
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-glucosyl-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:23360, Rhea:RHEA-COMP:14604, Rhea:RHEA-COMP:14605, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140573; EC=2.4.1.186; Evidence={ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213}; CATALYTIC ACTIVITY: Reaction=[1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:56560, Rhea:RHEA-COMP:14606, Rhea:RHEA-COMP:14607, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140574; EC=2.4.1.186; Evidence={ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213};
DNA Binding
EC Number 2.4.1.186
Enzyme Function FUNCTION: Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. {ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213}.
nucleotide Binding
Features Alternative sequence (2); Beta strand (14); Binding site (1); Chain (1); Glycosylation (1); Helix (16); Initiator methionine (1); Metal binding (3); Modified residue (2); Mutagenesis (1); Natural variant (3); Region (6); Site (1); Turn (2)
Keywords 3D-structure;Acetylation;Alternative splicing;Disease variant;Glycogen biosynthesis;Glycogen storage disease;Glycoprotein;Manganese;Metal-binding;Phosphoprotein;Reference proteome;Transferase
Interact With P13807; P13807
Induction
Subcellular Location
Modified Residue MOD_RES 2; /note="N-acetylthreonine"; /evidence="ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895"; MOD_RES 44; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P13280"
Post Translational Modification PTM: Self-glycosylated by the transfer of glucose residues from UDP-glucose to itself, forming an alpha-1,4-glycan of around 10 residues attached to Tyr-195. {ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213}.; PTM: Phosphorylated. {ECO:0000250|UniProtKB:P13280}.
Signal Peptide
Structure 3D X-ray crystallography (14)
Cross Reference PDB 3Q4S; 3QVB; 3RMV; 3RMW; 3T7M; 3T7N; 3T7O; 3U2T; 3U2U; 3U2V; 3U2W; 3U2X; 6EQJ; 6EQL;
Mapped Pubmed ID 10949035; 12958597; 14532330; 15860684; 15870102; 15930137; 16189514; 17311895; 17928598; 18040046; 18070875; 19699667; 20538597; 20562859; 21356517; 21767668; 21988832; 22198226; 22248338; 22815132; 23414517; 23650620; 23663739; 24239874; 25416783; 25416956; 25538239; 25544560; 26216881; 26652229; 2667896; 29143313; 29321365; 2961257; 3049072; 31689353; 33989636; 5264799; 8420990; 8613547; 8755644; 9691087; 9771710; 9931343;
Motif
Gene Encoded By
Mass 39,384
Kinetics
Metal Binding METAL 102; /note="Manganese"; /evidence="ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3QVB, ECO:0007744|PDB:3RMV, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N, ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2T, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V, ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X"; METAL 104; /note="Manganese"; /evidence="ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3QVB, ECO:0007744|PDB:3RMV, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N, ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2T, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V, ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X"; METAL 212; /note="Manganese"; /evidence="ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3QVB, ECO:0007744|PDB:3RMV, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N, ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2T, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V, ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X"
Rhea ID RHEA:23360; RHEA:56560
Cross Reference Brenda 2.4.1.186;