ID G0V7J7_NAUCC Unreviewed; 705 AA.
AC G0V7J7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN Name=NCAS0A08870 {ECO:0000313|EMBL:CCC67445.1};
GN OrderedLocusNames=NCAS_0A08870 {ECO:0000313|EMBL:CCC67445.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC67445.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC67445.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) 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; HE576752; CCC67445.1; -; Genomic_DNA.
DR RefSeq; XP_003673826.1; XM_003673778.1.
DR AlphaFoldDB; G0V7J7; -.
DR STRING; 1064592.G0V7J7; -.
DR GeneID; 11529313; -.
DR KEGG; ncs:NCAS_0A08870; -.
DR eggNOG; KOG3742; Eukaryota.
DR HOGENOM; CLU_015910_1_0_1; -.
DR InParanoid; G0V7J7; -.
DR OMA; RDVRNHI; -.
DR OrthoDB; 9432at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001640; Chromosome 1.
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; 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:UP000001640};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
SQ SEQUENCE 705 AA; 79994 MW; BBB63FA4837C0571 CRC64;
MARDLQNHLL FETATEVANR VGGIYSVLKS KAPITVAQYK DNYHLIGPLN KATYQNEVDQ
MDWEAPDSFP DEIKPIQSTL RSMRSRGVNF IYGRWLIEGS PRLILFDLDS VRGFLNEWKG
DLWYLVGIPS PENDFETNDA ILLGYTVAWF LGELTAEDTT HAIIAHFHEW LAGVALPLCR
KRRIDVVTIF TTHATLLGRY LCAAGDVDFY NNLENFDVDH EAGKRGIYHR YCVERAAAHT
ADVFTTVSQI TAFEAEHLLK RKPDGILPNG LNVIKFQAVH EFQNLHALKK EKINEFVRGH
FHGCFDFDLD NTVYFFIAGR YEYKNKGADM FIESLARLNY RLKVAGSKKT VIAFIIMPAK
NNSFTVEALK GQAVVKALET TVDEVTNSIG KRIFDHAMRF PNNGTTSEIP VDIHELLKPS
DNVLLKKRVL GLRRPAGELP AIVTHNMVDD ANDPILNQIR HVQLFNGSSD RVKVIFHPEF
LNANNPILGL DYDEFVRGCH LGVFPSYYEP WGYTPAECTV MGVPSITTNL SGFGAYMEDL
IETNQAKDYG IYIVDRRFKA PDESVEQLVD YMEEFVKKTR RQRINQRNRT ERLSDLLDWK
RMGLEYVKAR QLALRRAYPD QFKQLVGEEL NDTNMDTLAG GKKLKIARPL SVPGSPRETR
QASAIYMTPG DLGTLQEANT ADDYFNLSIG SHDGDDEQGP YADEN
//
