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Database: UniProt
Entry: T0KMX3_COLGC
LinkDB: T0KMX3_COLGC
Original site: T0KMX3_COLGC 
ID   T0KMX3_COLGC            Unreviewed;       712 AA.
AC   T0KMX3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=CGLO_06885 {ECO:0000313|EMBL:EQB53389.1};
OS   Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS   (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB53389.1, ECO:0000313|Proteomes:UP000015530};
RN   [1] {ECO:0000313|Proteomes:UP000015530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX   PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA   Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA   Thon M., Fluhr R., Prusky D.;
RT   "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT   gloeosporioides as revealed by transcriptome analysis.";
RL   Mol. Plant Microbe Interact. 26:1345-1358(2013).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQB53389.1}.
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DR   EMBL; AMYD01001376; EQB53389.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0KMX3; -.
DR   STRING; 1237896.T0KMX3; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   HOGENOM; CLU_015910_1_0_1; -.
DR   OMA; RDVRNHI; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000015530; 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:UP000015530};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          679..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   712 AA;  81061 MW;  41136179243DFCB3 CRC64;
     MSTLPEGTRD NPDRPPRDVK NHLLFEIATE VAHRVGGIYS VIKSKAPVTT AEYGDRYTLI
     GPLNHHSAAV EVEELEPTTP ELAATIQSMR DRGIGILYGR WLIDGAPRVL LIDTKTAYHF
     LDEWKTDLWN VASIPSPPND DETNEAVVFG YLVAWFLGEF VCHEKNKAVI AHFHEWLAGV
     ALPLTKKRRI DVTTIFTTHA TLLGRYLCAG SVDFYNNLQW FDVDAEAGKR GIYHRYCIER
     AAAHACDVFT TVSHITAYES EHLLKRKPDG VLPNGLNVTK FSAMHEFQNL HQQAKEKIHD
     FVRGHFYGHY DFDPENTLYF FTAGRYEFRN KGVDMFIESL ARLNHRLKVA GSKMTVVAFV
     IMPAQTTSLT VEALKGQAVI KSLRDTVDII EKGIGRRIFE RSLKWHDGDP MPDEKELISS
     QDRVLIRRRL FAMKRHGLPP IVTHNMISDS EDPILNQIRR VQLFNHPTDR VKIVFHPEFL
     NSANPVLPLD YDEFVRGTHM GIFASYYEPW GYTPAECTVM GVPSITTNLS GFGCYMEELI
     ENSSDYGIYI VDRRTKGVDD SVNQLTTHMF DFCQKSRRQR INQRNRTERL SDLLDWKRMG
     MEYVKARQLA LRRAYPGSFS GDEEEDFIPG VEQKISRPFS VPGSPRDRTG MMTPGDFASL
     QEGREGLSTE DYVAWKLPEE EDPDEYPFPL TLRAKRPSGP ASPLDGVQLN GN
//
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