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Database: UniProt
Entry: C4R5J9_KOMPG
LinkDB: C4R5J9_KOMPG
Original site: C4R5J9_KOMPG 
ID   C4R5J9_KOMPG            Unreviewed;       703 AA.
AC   C4R5J9;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   OrderedLocusNames=PAS_chr3_0781 {ECO:0000313|EMBL:CAY70835.1};
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY70835.1, ECO:0000313|Proteomes:UP000000314};
RN   [1] {ECO:0000313|EMBL:CAY70835.1, ECO:0000313|Proteomes:UP000000314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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; FN392321; CAY70835.1; -; Genomic_DNA.
DR   RefSeq; XP_002493014.1; XM_002492969.1.
DR   AlphaFoldDB; C4R5J9; -.
DR   SMR; C4R5J9; -.
DR   STRING; 644223.C4R5J9; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   EnsemblFungi; CAY70835; CAY70835; PAS_chr3_0781.
DR   GeneID; 8200474; -.
DR   KEGG; ppa:PAS_chr3_0781; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   HOGENOM; CLU_015910_1_0_1; -.
DR   InParanoid; C4R5J9; -.
DR   OMA; RDVRNHI; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000314; Chromosome 3.
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; 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:UP000000314};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          612..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   703 AA;  79804 MW;  2C7B456D10EA6B56 CRC64;
     MGKDITNHLL FEIATEVANR VGGIYSVLKS KAPVTVAEYK DRYTLIGPLN ANSANVEVEE
     LPVLDPVLKR TLDSMSGRGI RYLYGRWLIE GAPRVILFDI GSAAGYLNEW KSDLWNIAGV
     PTPEHDVETN DAILLGYLVA WFLGELVHND GHKRAIICHA HEWLAAVCLP LCRKRKIDVT
     TVFTTHATLL GRYLCAGSVD FYNNLDKFDV DAEAGKRGIY HRYCIERAAA HSADVFTTVS
     HITAYEAEHL LKRKPDGVLP NGLNVIKFQA VHEFQNLHAE KKEKINEFIR GHFYGQLDFK
     LNNTLYFFIA GRYEYRNKGV DFFIESLARL NHRLKASNSN MTVVAFIIMP AKTNSYTVET
     LKGQAVIKQL ENTINDIEAL VGKRLFEFCQ HPATSSNSSH IEMPDIDDLL KPSDRVLLKR
     RMFAMKREGL PPIVTHNMAD DSTDPILNQI RNVQLFNRPE DRVKIIFHPE FLNSNNPILS
     LDYDEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSITTN LSGFGCYMED LIENSSDYGI
     YIVDRRLKSV DESIDQLTSY MFDFVDKTRR QRINQRNRVE RLSDLLDWRR MGLEYVKGRS
     LALRRAYPDE FKNQNNEHSN PFSESNSIKI TRPLSVPGSP RDKYSSSANI MTPGDLGTLQ
     ENNSTDYISW RLGNDTEEDG LDVTLRGLSV APSAEQSGDE FDA
//
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