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Database: UniProt
Entry: A0A1B9HVL8_9TREE
LinkDB: A0A1B9HVL8_9TREE
Original site: A0A1B9HVL8_9TREE 
ID   A0A1B9HVL8_9TREE        Unreviewed;       734 AA.
AC   A0A1B9HVL8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=I206_07096 {ECO:0000313|EMBL:OCF47317.1};
OS   Kwoniella pini CBS 10737.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1296096 {ECO:0000313|EMBL:OCF47317.1, ECO:0000313|Proteomes:UP000094020};
RN   [1] {ECO:0000313|EMBL:OCF47317.1, ECO:0000313|Proteomes:UP000094020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10737 {ECO:0000313|EMBL:OCF47317.1,
RC   ECO:0000313|Proteomes:UP000094020};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cryptococcus pinus CBS10737.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000094020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10737 {ECO:0000313|Proteomes:UP000094020};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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; KV700117; OCF47317.1; -; Genomic_DNA.
DR   RefSeq; XP_019008536.1; XM_019158790.1.
DR   AlphaFoldDB; A0A1B9HVL8; -.
DR   STRING; 1296096.A0A1B9HVL8; -.
DR   GeneID; 30175465; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000094020; 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:UP000094020};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          611..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   734 AA;  82761 MW;  8C22F03BC168742A CRC64;
     MARSVHSPLL FECAWEVANK VGGIYTVIKT KVPVTTKEYG DRACLIGPLS YKTAPMEVES
     EEPEPGTPFA LTLKSMQERG VKLIYGRWLI EGNPRVLLFD TGSCYDRMDE WKTDLWNLAG
     IPSPPNDHET NETIVFGYMV AWFLGEFSSR ETSTAIIAHF HEWQAGLAIP LCRKRHIDVT
     TIFTTHATLL GRYLCAGSVD FYNNLQYFDV DHEAGKRGIY HRYCIERSAA HCADVFTTVS
     HITAFESEHL LKRKPDGVLP NGLNVVKFAA MHEFQNMHMQ SKEKINDFIR GHFYGHYDFD
     LENTVYMFTA GRYEFRNKGV DMFIESLARL NHRLKEMGSK TTVVAFIIMP AATNSYTIEA
     LKGQAVTAQL KECVKQITGR IEKRIFEHAA RYSGEHGTEV PNPEDLLSKE DAVALKRRVF
     ALKRNSLPPI VTHNMADDAN DPILNQFRRV SLFNQSSDRV KVIFHPEFLN SNNPILGLDY
     EEFVRGCHLG VFPSYYEPFG YTPAECTVMG IPNVTTNLSG FGCFMEDLLE TPEDYGCYIV
     DRRGQGVDDS VNQLTNQLLS FTTKSRRQRI NQRNRTERLS ELLDWKSLGL EYVKARQLAL
     RRAYPDSFDD DEPDFTGVQR VGAPLSAPGS PKMRTGMMTP GDFATLTEEM EHLGTQDYMG
     GKSWRGINDD DDENHYPFPL VMKPRNRSDS LASAISGTAT PSGGRKLSEK DLEKADAVLS
     SMGQNGLNGN GNGH
//
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