GLG2_YEAS7
ID GLG2_YEAS7 Reviewed; 380 AA.
AC A6ZQJ2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Glycogenin-2;
DE EC=2.4.1.186;
DE AltName: Full=Glycogen synthesis initiator protein 2;
DE AltName: Full=Glycogenin glucosyltransferase 2;
GN Name=GLG2; ORFNames=SCY_3153;
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 to internal tyrosine residues. These chains act as primers for the
CC elongation reaction catalyzed by glycogen synthase (By similarity).
CC {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 -!- SUBUNIT: Interacts with glycogen synthase GSY2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFW02000044; EDN63244.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZQJ2; -.
DR SMR; A6ZQJ2; -.
DR EnsemblFungi; EDN63244; EDN63244; SCY_3153.
DR HOGENOM; CLU_017171_4_1_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Cytoplasm; Glycogen biosynthesis; Glycoprotein; Manganese; Metal-binding;
KW Transferase.
FT CHAIN 1..380
FT /note="Glycogenin-2"
FT /id="PRO_0000333542"
FT REGION 331..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Basic and acidic 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 249..255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 249
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:P47011"
FT CARBOHYD 232
FT /note="O-linked (Glc...) tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P47011"
FT CARBOHYD 367
FT /note="O-linked (Glc...) tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P47011"
SQ SEQUENCE 380 AA; 44577 MW; E4513DE43046763E CRC64;
MAKKVAICTL LYSRDYLPGA LTLAYQLQKL LKHAVVEDEI TLCLLIEKKL FEDEFKPQEI
ALIRSLFKEI IIIEPLKDQE KSIEKNKANL ELLKRPELSH TLLKARLWEL VQFDQVLFLD
ADTLPLNKDF FEILRLYPEQ TRFQIAAVPD IGWPDMFNTG VLLLIPDLDM ATSLQDFLIK
TVSIDGADQG IFNQFFNPIC NYSKEVLHKV SPLMEWIRLP FTYNVTMPNY GYQSSPAMNF
FQQHIRLIHF IGTFKPWSRN TTDYDDHYYQ LWRSTQRELY SECHLSNYFT HLQLGNIETE
TNFYHEPPCL QDLLNHGTRE NQKHVDLDIT SVDRNASQKS TAEKHDIEKP TSKPQSAFKF
DWESTDYLDR VQRAFPKPDT
