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Database: UniProt
Entry: A7TT19_VANPO
LinkDB: A7TT19_VANPO
Original site: A7TT19_VANPO 
ID   A7TT19_VANPO            Unreviewed;       706 AA.
AC   A7TT19;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, 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=Kpol_295p5 {ECO:0000313|EMBL:EDO14589.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO14589.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480536; EDO14589.1; -; Genomic_DNA.
DR   RefSeq; XP_001642447.1; XM_001642397.1.
DR   AlphaFoldDB; A7TT19; -.
DR   STRING; 436907.A7TT19; -.
DR   GeneID; 5542604; -.
DR   KEGG; vpo:Kpol_295p5; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   HOGENOM; CLU_015910_1_0_1; -.
DR   InParanoid; A7TT19; -.
DR   OMA; RDVRNHI; -.
DR   OrthoDB; 9432at2759; -.
DR   PhylomeDB; A7TT19; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000267; 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   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:UP000000267};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
SQ   SEQUENCE   706 AA;  80203 MW;  89C32322D585148F CRC64;
     MGRDIQNHLL FEVATEVANR VGGIYSVLKS KAPTAVAQYG DNYTLVGPLN RSSYQSEVEE
     LDINDPNTFP EDILPIKYVL ESMRARGVHF VYGRWLIEGA PRVILFELGS VGHYLNDWKG
     DLWSLVGIPS PENDAETNDA ILLGYTVAWF LGELTTKDNN HAIVTHCHEW LAGVALPLCR
     KRRIDVVTIF TTHATLLGRY LCASGSVDFY NNLDKFDVDH EAGKYGIYHR YCIERAAAHT
     ADVFTTVSQI TALEAEHLLK RKPDGILPNG INVTKFQAVH EFQNLHALKK AKINDFVRGH
     FHGCFDFDLD ETLYFFIAGR YEYKNKGADM FIEALARLNY RLKVSGSKKT VVAFIIMPAK
     TNSFTVEALR SQAVVKALES SVKEVTHLIG ERIFDHAIKY PHLGITSELP TNLDDIIKPS
     DKVLLKRRVL ALRRSDGQLP PIVTHNMADD SHDPILNQIR HVQLFNNASD RVKVIFHPEF
     LNANNPILGL DYDEFVRGCH LGVFPSYYEP WGYTPAECTV MGVPSITTNL SGFGAYMEDL
     IETDQAKDYG IYIVDRRFKN PEESVEQLVD MMEEFVKKNR RQRINQRNRT ERLSDLLDWR
     RMGLEYVKAR QLALRRGYPD IFRQFTNGED VNDSNMYTMA GNKKFKIMKP ISVPGSPSES
     RLRSGSVTTP TVYMTPGDLG TLQEANNADD YFMLANDQED YEDNNE
//
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