ID   G0WFG3_NAUDC            Unreviewed;       712 AA.
AC   G0WFG3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   Name=NDAI0H03510 {ECO:0000313|EMBL:CCD26524.1};
GN   OrderedLocusNames=NDAI_0H03510 {ECO:0000313|EMBL:CCD26524.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS   0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD26524.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD26524.1, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC       reducing end of alpha-1,4-glucan. {ECO:0000256|RuleBase:RU363104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC         alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:18549, Rhea:RHEA-
CC         COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00043769};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18550;
CC         Evidence={ECO:0000256|ARBA:ARBA00043769};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|RuleBase:RU363104}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000256|ARBA:ARBA00010686, ECO:0000256|RuleBase:RU363104}.
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DR   EMBL; HE580274; CCD26524.1; -; Genomic_DNA.
DR   RefSeq; XP_003671767.1; XM_003671719.1.
DR   AlphaFoldDB; G0WFG3; -.
DR   STRING; 1071378.G0WFG3; -.
DR   GeneID; 11496055; -.
DR   KEGG; ndi:NDAI_0H03510; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   HOGENOM; CLU_015910_1_0_1; -.
DR   OMA; RMHKSNV; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000689; Chromosome 8.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 6.10.260.10; -; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176:SF3; GLYCOGEN [STARCH] SYNTHASE; 1.
DR   PANTHER; PTHR10176; GLYCOGEN SYNTHASE; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
PE   3: Inferred from homology;
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056,
KW   ECO:0000256|RuleBase:RU363104};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          688..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   712 AA;  80809 MW;  1BC427E554171A90 CRC64;
     MTRDLKEHLL FEIATEVANR VGGIYSVLKS KAPITVAQYK ENYMLLGPLN KATYQNEIEQ
     LDWTSEEAFS GDLKPIQDTL HSLQSKGFNF VFGRWLIEGS PKVLLIDLDS IRWRLNEWKA
     DLWSLVGIPS PEYDSETNDA ILLGYAVVWF LGELTQLDHK HAIIAHFHEW LAGVALPLCR
     KKRIDVVTIF TTHATLLGRY LCAAGDVDFY NNLANFDVDQ EAGKRGIYHR YCIERAAAHT
     ADVFTTVSQI TAFEAEHLLK RKPDGILPNG LNVVKFQAVH EFQNLHALKK EKINEFVRGH
     FHGCFDFDLD NTLYFFIAGR YEYKNKGADM FIEALARLNY RLKVAGSKMT VVAFIIMPAK
     TNSFTVEALK SQAVVKSLEN TVDEVTKNIG KRIFEHAMRF PHMGITSEIP TDLNELLKPS
     DNVLLKRRVL GLRRADGQLP PVVTHNMVDD ANDPILNQIR HVQLFNNTSD RVKVIFHPEF
     LNANNPILGL DYDEFVRGCH LGVFPSYYEP WGYTPAECTV MGVPSITTNL SGFGAYMEDL
     IEANQAKDYG IYIVDRRFKN PDESVEQLVD CMEEFCKKTR RQRINQRNRT ERLSDLLDWK
     RMGLEYVKAR QLALRRAYPD QFKQLVGEEL NDTDMNTLAG GKKLKIARPL SVPGSPREPR
     SGSTVFMTPG DLGTLQDANN ADDYFNLSMD GRALDTDDTE EDEGIAGVDG PH
//