GLG1_YEAS7
ID GLG1_YEAS7 Reviewed; 616 AA.
AC A7A018;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Glycogenin-1;
DE EC=2.4.1.186;
DE AltName: Full=Glycogen synthesis initiator protein 1;
DE AltName: Full=Glycogenin glucosyltransferase 1;
GN Name=GLG1; ORFNames=SCY_3428;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: Self-glucosylating initiator of glycogen synthesis. Catalyzes
CC the formation of a short alpha (1,4)-glucosyl chain covalently attached
CC via a glucose 1-O-tyrosyl linkage to internal tyrosine residues. These
CC chains act as primers for the elongation reaction catalyzed by glycogen
CC synthase. Capable of transferring glucosyl residues to unbound
CC acceptors such as free oligoglucans or oligoglucan derivatives (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-
CC glucosyl-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:23360,
CC Rhea:RHEA-COMP:14604, Rhea:RHEA-COMP:14605, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:140573; EC=2.4.1.186;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin] + UDP-alpha-
CC D-glucose = [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin] + H(+)
CC + UDP; Xref=Rhea:RHEA:56560, Rhea:RHEA-COMP:14606, Rhea:RHEA-
CC COMP:14607, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:140574; EC=2.4.1.186;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P46976};
CC -!- INDUCTION: Induced during the diauxic transition.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDN59961.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AAFW02000152; EDN59961.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A7A018; -.
DR SMR; A7A018; -.
DR PRIDE; A7A018; -.
DR EnsemblFungi; EDN59961; EDN59961; SCY_3428.
DR HOGENOM; CLU_017171_4_1_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0008466; F:glycogenin glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102751; F:UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Glycogen biosynthesis; Glycoprotein; Manganese; Metal-binding; Transferase.
FT CHAIN 1..616
FT /note="Glycogenin-1"
FT /id="PRO_0000337759"
FT REGION 283..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..16
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 120..122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 158..160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 185..189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 247..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT SITE 104
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT CARBOHYD 230
FT /note="O-linked (Glc...) tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT CARBOHYD 598
FT /note="O-linked (Glc...) tyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 616 AA; 69830 MW; 3CBE0E1CD299ACE3 CRC64;
MYKKLAIATL LYSADYLPGV FALGHQVNKL LEEAGKKGDI ETCLIVTTSL FNDTLSELAK
NLLQSIYTKI VLVEPLDCQE ESIQKNSENL ALLERPELSF ALIKARLWEL TQFEQVLYLD
SDTLPLNKEF LKLFDIMSKQ TTSQVGAIAD IGWPDMFNSG VMMLIPDTDT ASVLQNYIIE
NTSIDGSDQG ILNQFFNQNC CTDELVKDSF SREWVQLSFT YNVTIPNLGY QSSPAMNYFK
PSIKLIHFIG KHKPWSLWSQ KNFIKNEYHD QWNEVYEEFK EEHQLNNEVS KPKISDSDKT
ETPETITPVD APPSNEPTTN QEIDTISTVE ENVDNQNAEP VPNSDHSPAP NPVPLDFTKW
LTTFINKDHL TNQPVNESRE YSKENDNNII NSSSNRDQES PPNSTQEPNS SYSVVSTQAD
SDEHQNAEEE DSTTDNASNS GEESHLDDIS TAASSNNNVS NQPDNKNFSN SKENNISVEP
SPSNPEQKRS TDNIQKPSVS TNDLPDDVEP HTSVDDNIQY LEKDKEGYEE FLPDVYESNA
IDNEEEFFDD DARDATEGET KTSAVADKQE DMKLTAEETN QPQQEMPNFK FDWEDSDYLS
KVERCFPDDI FEYAVE
