ID   M7XI20_RHOT1            Unreviewed;       755 AA.
AC   M7XI20;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=RHTO_04065 {ECO:0000313|EMBL:EMS19773.1};
OS   Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS19773.1, ECO:0000313|Proteomes:UP000016926};
RN   [1] {ECO:0000313|EMBL:EMS19773.1, ECO:0000313|Proteomes:UP000016926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP11 {ECO:0000313|EMBL:EMS19773.1,
RC   ECO:0000313|Proteomes:UP000016926};
RX   PubMed=23047670; DOI=10.1038/ncomms2112;
RA   Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA   Ye M., Zou H., Zou H., Zhao Z.K.;
RT   "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL   Nat. Commun. 3:1112-1112(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}.
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; KB722666; EMS19773.1; -; Genomic_DNA.
DR   RefSeq; XP_016270892.1; XM_016417733.1.
DR   AlphaFoldDB; M7XI20; -.
DR   GeneID; 27368078; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   HOGENOM; CLU_015910_1_0_1; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000016926; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          690..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   755 AA;  85078 MW;  96199B1AAB7B7C10 CRC64;
     MAQQRSVHDH LLFEVAWEVA NKVGGIYTVI KTKAPVTCAE YGDRYTLMGP LSYKSAPMEV
     EAIDWEKPTP LNEDGTPTTT NVANAALVGT LSSMRDRGVK FLYGRWLIEG GPKVLLFDTG
     SVWNRLDEWK TDLWNLAGIP TPANDTETNE TVLLGYLVAW FLGEFSARER SRAIVAHLHE
     WQAGLAIPLC RKRHIDVTTV FTTHATLLGR YLCAGSVDFY NNLAYFDVDH EAGKRGIYHR
     YCIERSAAHC ADVFTTVSHI TAYEAEHLLK RKPDGVTPNG LNVTKFSAMH EFQNLHAVSK
     QKINDFIRGH FYGHYDFDLD NTLYFFTAGR YEYRNKGLDM YIESLARLNH RLQQSGTKQT
     VVAFIISPAA THSYTIEALK GQAVTKQLRD TVTEIQNRIG ARLFERTARY NGEHGTEVPD
     PAELLSTEDK ILLKRRVFAL RRNSLPPVVT HNMADDANDP ILNQVRRVQL FNRSSDRVKI
     IFHPEFLNAN NPILGLDYEE FVRGCHLGVF PSYYEPWGYT PAECTVMGVP SITTNLSGFG
     GFMEDLLEDS QDYGIYIVDR RMKSVEDSVN QLTDQMLSFC QKTRRQRINQ RNRTERLSDL
     LDWKRMGLEY AKARQLALRR AYPDAFEDDD FDFESGQVRL PRPLSAPASP RFTTGVVTPG
     EFATLTEEMQ GLGTSDYMGA QQTWESLIRG KDEEEEESGY PFPLVLKRKG GPGSVSGTTS
     GGSTPGGIFP NGRGKSLSEH DLARADEALS NHSTQ
//