ID   Q6FM65_CANGA            Unreviewed;       696 AA.
AC   Q6FM65;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   OrderedLocusNames=CAGL0K10626g {ECO:0000313|CGD:CAL0134357,
GN   ECO:0000313|EMBL:CAG61642.1};
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG61642.1, ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG61642.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380957; CAG61642.1; -; Genomic_DNA.
DR   RefSeq; XP_448679.1; XM_448679.1.
DR   AlphaFoldDB; Q6FM65; -.
DR   STRING; 284593.Q6FM65; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   EnsemblFungi; CAGL0K10626g-T; CAGL0K10626g-T-p1; CAGL0K10626g.
DR   GeneID; 2890101; -.
DR   KEGG; cgr:CAGL0K10626g; -.
DR   CGD; CAL0134357; CAGL0K10626g.
DR   VEuPathDB; FungiDB:CAGL0K10626g; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   HOGENOM; CLU_015910_1_0_1; -.
DR   InParanoid; Q6FM65; -.
DR   OMA; RDVRNHI; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000002428; Chromosome K.
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:UP000002428};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
SQ   SEQUENCE   696 AA;  79516 MW;  D44ED04556EF7C6B CRC64;
     MPRDLQNHLL FEVATEVANK VGGIYSVLKS KAPVTVAQYQ DNYTLIGPLN KGTYQGEVEE
     LDWEDPSIFS EELQPVQQAL KYMREKGVYF VYARWLIEGA PRVILFDLDS VRYKLNEWKA
     DLWSLVGIPS PENDWETNDA ILLGYTVVWF LGELTQLDHK HAIIGHFHEW LAGVALPLCR
     KKRIDVVTIF TTHATLLGRY LCAAGDVDFY NHLQYFDVDQ EAGKRGIYHR YCIERAAAHT
     ADVFTTVSQI TALEAEHLLK RKPDGILPNG LNVVKFQAVH EFQNLHALKK EKINDFVRAH
     FHGNFDFDLD NTLYFFIAGR YEYKNKGADM FVEALARLNY RLKMAGSKKT VVAFIIMPAQ
     NNSFTVEALR SQAVVKSLEN TVNEVTSLIG KRIFEHAMKF PHNGITNEIP NNLEELLKPS
     DKVLLKKRVL ALRRPYGELP PIVTHNMADD ANDPILNQIR HVQLFNNHSD RVKVIFHPEF
     LNANNPILGL DYDEFVRGCH LGVFPSYYEP WGYTPAECTV MGVPSITTNL SGFGAYMEDL
     IETNQAKDYG IYIVDRRYKA PDESVEQLVD YMEEFVNKTR RQRINQRNRT ERLSDLLDWK
     RMGLEYVKAR QLGLRRAYPD QFKEIVGEDV NDSSMEALAG GKKLKIARPL SVPGSPRDAA
     KSPSTVFMTP GDLGTIQDAN NVDDYFHLSV NDNEEE
//