ID   J5JV80_BEAB2            Unreviewed;       710 AA.
AC   J5JV80;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=BBA_04844 {ECO:0000313|EMBL:EJP66351.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP66351.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP66351.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP66351.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
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; JH725160; EJP66351.1; -; Genomic_DNA.
DR   RefSeq; XP_008598163.1; XM_008599941.1.
DR   AlphaFoldDB; J5JV80; -.
DR   STRING; 655819.J5JV80; -.
DR   GeneID; 19887856; -.
DR   HOGENOM; CLU_015910_1_0_1; -.
DR   InParanoid; J5JV80; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000002762; Unassembled WGS sequence.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03793; GT3_GSY2-like; 1.
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:UP000002762};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          671..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   710 AA;  80631 MW;  6024D69A955D0EC3 CRC64;
     MASNGDKPTR DVKNHLLFEV ATEVAHRVGG IYSVIKSKAP VTTAEYGDRY TLIGPLNHQS
     AAVEVEEMEP NTPELADTLQ AMKDRGIGYM YGRWLIEGAP RVLLFDTKTA YGYLNDWKGD
     LWNVASIPSP PGDDETNEAI VFGYLVAWFL GEFVCHEKSK AVIAHFHEWL AGVALPLTKK
     RRIDVTTIFT THATLLGRYL CAGSVDFYNN LQNFDVDAEA GKRGIYHRYC IERAATHSCD
     VFTTVSHITA FESEHLLKRK PDGVLPNGLN VTKFSAVHEF QNLHQVYKEK IHDFVRGHFY
     GHYDFEPDNT IYIFTAGRYE FRNKGVDMFI ESLARLNHRL KSSGSKITVV AFIIMPAKTT
     SLTVEALKGQ AVLKSLRDTT HVIEQSIGRR IFERSLKWHE GDPMPDEKEL ISSQDRVLLR
     RRLFAMKRHG LPPIVTHNMV NDHEDPVLNQ IRRVELFNHP TDRVKVVFHP EFLNSANPVL
     PLDYDDFVRG CHLGVFASYY EPWGYTPAEC TVMGVPSITT NLSGFGCYME ELIENSSDYG
     IYIVDRRTKG VDDSVNELTG HMFDFCGKSR RQRINQRNRT ERLSDLLDWK RMGMEYVKAR
     QLALRRAYPD SFSPEDDADE DYIPGVEQKI SRPFSVPGSP RDRTGMMTPG DFASLQEGRE
     GLNTEDYVSW KLPAEEDPDE YPFPLTLRTK QPTVTDTLSP AAPAPLQGDN
//