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Database: UniProt
Entry: C4YNH5_CANAW
LinkDB: C4YNH5_CANAW
Original site: C4YNH5_CANAW 
ID   C4YNH5_CANAW            Unreviewed;       661 AA.
AC   C4YNH5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=CAWG_01436 {ECO:0000313|EMBL:EEQ43208.1};
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748 {ECO:0000313|EMBL:EEQ43208.1, ECO:0000313|Proteomes:UP000001429};
RN   [1] {ECO:0000313|EMBL:EEQ43208.1, ECO:0000313|Proteomes:UP000001429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1 {ECO:0000313|EMBL:EEQ43208.1,
RC   ECO:0000313|Proteomes:UP000001429};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(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; CM000309; EEQ43208.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4YNH5; -.
DR   SMR; C4YNH5; -.
DR   PaxDb; 5476-C4YNH5; -.
DR   VEuPathDB; FungiDB:CAWG_01436; -.
DR   HOGENOM; CLU_015910_1_0_1; -.
DR   OMA; RDVRNHI; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001429; Chromosome R.
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
SQ   SEQUENCE   661 AA;  75580 MW;  6D892588E976CC90 CRC64;
     MARDIDNHLL FEVATEVAHK VGGIYSVLKS KAPVTVAEYR ERYTLLGPLH YDSAQIEVEE
     LPVTDPHIKQ TLDSMSSKGI RWLYGRWLIE GAPRVLLFDI WSAGHYLNEW KADLWNVAGI
     PTPDHDSETN DAILLGYLVA WFLGELVYND RDRAVICQCH EWLAGIALPL CRKRRIDVTT
     IFTTHATLLG RYLCAGSTDF YNNLDKFDVD AEAGKRGIYH RYCIERSATH SADVFTTVSD
     ITAYEAEHLL KRKPDGVLPN GLNVVKFQAV HEFQNLHAIK KAKINEFVKG HFYGNYDFDL
     DNTLYFFIAG RYEFRNKGCD FFIESLARLN HKLKEAGSKT TVVAFIIMPG KTQSYTVETL
     KGQAVVKQLE STIGEVQKKV GERLFEYCAR YPNTDHHGND EVPTIDELIK PADRVLLKRR
     IFALKRDGLP PIVTHNMVDD STDPVLNHIR RVQLFNKPED RVKIIFHPEF LNANNPILSL
     DYDEFVRGCH LGVFPSYYEP WGYTPAECTV MGIPSITTNL SGFGCYMNDL VENPTDYGIY
     IVDRRMKSVD ESINQLTDYM FDFCAKSRRQ RINQRNRTER LSVLLDWRSV HSEYSKARLL
     ALKRAYPDYV GEKVVESKMK ITRPMSVPGS PRSLLLTPGD LGSLQDANQD ISYFELGEEE
     T
//
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