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Database: UniProt
Entry: F0ZA00_DICPU
LinkDB: F0ZA00_DICPU
Original site: F0ZA00_DICPU 
ID   F0ZA00_DICPU            Unreviewed;       853 AA.
AC   F0ZA00;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=DICPUDRAFT_148003 {ECO:0000313|EMBL:EGC39239.1};
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC39239.1, ECO:0000313|Proteomes:UP000001064};
RN   [1] {ECO:0000313|Proteomes:UP000001064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX   PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA   Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA   Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA   Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA   Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA   Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA   Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT   "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT   Dictyostelium purpureum.";
RL   Genome Biol. 12:R20.1-R20.23(2011).
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; GL870961; EGC39239.1; -; Genomic_DNA.
DR   RefSeq; XP_003284266.1; XM_003284218.1.
DR   AlphaFoldDB; F0ZA00; -.
DR   STRING; 5786.F0ZA00; -.
DR   EnsemblProtists; EGC39239; EGC39239; DICPUDRAFT_148003.
DR   GeneID; 10510170; -.
DR   KEGG; dpp:DICPUDRAFT_148003; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   InParanoid; F0ZA00; -.
DR   OMA; RDVRNHI; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001064; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IBA:GO_Central.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:EnsemblProtists.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IBA:GO_Central.
DR   GO; GO:0031288; P:sorocarp morphogenesis; IEA:EnsemblProtists.
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:UP000001064};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          641..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..853
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   853 AA;  95435 MW;  C8152CB53B0AEFF4 CRC64;
     MIFGTPNSTF LESKLHSSQG MTFSSMASGS GSGGLLHSSS GSSITEEVSL PPSNTVLFDI
     SWEVAKKVGG IYTVLKSKAP VTVEEYKSRY ALIGPYNSET APTEFEPLVP GPLSSPIIEN
     MMKKYGIQVH FGKWLVEGYP KVFLIDLPSS SHKLGEWRWD LMSGFEQPGD HETNESIVFG
     YQSALLLKEF AEANPNDKYI AHFHEWQASV GLILLKKWKI PVSTIFTTHA TLLGRYLAAG
     GVDLYNQIQN LNIDYEASKR GIYHRHWIEK KSANDAHVFT TVSEITAYES ESILSRKADV
     ILPNGLKLDK FTALHEFQNL HAKYKNVLHE FVRGHFYGHY DFDLDNTLYV FTAGRSEYFN
     KGVDMFLDAL AGLNKLLQQS GSTMTIVAFI IMPSKTNNFN IDTLKGQSHN RDLRRTCNSI
     VESMGERLFE ATSRGRIISP EELLTQEDLV FLKRRIFALK QRPSLPPIVT HNMMDDVNDP
     ILNHLRKIKL FNSKEDRVKI IYHPEFLNST NPLIPLDYTE FVRGCHLGIF VSYYEPWGYT
     PAECTVLGVP SITSNLTGFA NYMSRGLNEP ESKGIFIVDR RFKSPNESVE QVTQYLWKFC
     QMDRRQRIEL RNRTEKLSEL LDWKTLGKFY RSARSLAIER AFPPSKPISR SPSPSPTSNT
     LKNSTSIQQL QQQLKQQVEQ QQKEQQQQQQ QQQTIPINIG KGETSQLSPN TMSSLLSDSL
     NISNKKSSSL SGGAKFAEST INPTPNNTPS IITTSVGSSS KPPLPTTTTA TVSNTPTNTP
     TIATVSSASV NTTKNSFQPS SQKSSSVNPI EQLTKLNSPT DRDFKNPLNE SGDGTSPSKA
     KSKSIPIPSN KFK
//
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