ID A0A1Y1UMV2_9TREE Unreviewed; 743 AA.
AC A0A1Y1UMV2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN ORFNames=BD324DRAFT_617503 {ECO:0000313|EMBL:ORX38837.1};
OS Kockovaella imperatae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cuniculitremaceae; Kockovaella.
OX NCBI_TaxID=4999 {ECO:0000313|EMBL:ORX38837.1, ECO:0000313|Proteomes:UP000193218};
RN [1] {ECO:0000313|EMBL:ORX38837.1, ECO:0000313|Proteomes:UP000193218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17943 {ECO:0000313|EMBL:ORX38837.1,
RC ECO:0000313|Proteomes:UP000193218};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Louie K.B., Bewick A.J., Labutti K.,
RA Haridas S., Kuo A., Salamov A., Ahrendt S.R., Lau R., Bowen B.P.,
RA Lipzen A., Sullivan W., Andreopoulos W.B., Clum A., Lindquist E., Daum C.,
RA Northen T.R., Ramamoorthy G., Schmitz R.J., Gryganskyi A., Culley D.,
RA Magnuson J., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Widespread Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (MAR-2017) 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}.
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:ORX38837.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NBSH01000003; ORX38837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1UMV2; -.
DR STRING; 4999.A0A1Y1UMV2; -.
DR InParanoid; A0A1Y1UMV2; -.
DR OrthoDB; 9432at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000193218; 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; 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:UP000193218};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT REGION 692..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 83854 MW; CB1573A54F99F004 CRC64;
MVRNAHNPLL FECAWEVANK VGGIYTVIKT KVPVTVREFG DRVCLIGPLS YKTAPMEVEA
EEPEPGSAFA HTLEAMREKG VKMIYGRWLI EGAPRVLLFD TGSCYNRMDE WKTDLWNLAG
IPTPPNDHET NETIVFGYIV AWFLGEFSSR ETSKAIIAHF HEWQAGLAIP LCRKRHIDVT
TVFTTHATLL GRYLCAGSVD FYNNLQYFDV DHEAGKRGIY HRYCIERSAA HCADVFTTVS
HITAFESEHL LKRKPDGVLP NGLNVKKFAA MHEFQNLHIQ AKEKINDFIR GHFYGHYDFD
LDNTIYLFTA GRYEFRNKGV DMFIESLARL NYRLQNQGSK MTVVAFIIMP AATNSYTIEA
LKGQAVTQQL QETVNQVTKR IGKRIFEHAA RYTGEHGTEV PNAEDLLSAE DKVLIKRRVF
ALKRNSLPPI VTHNMADDAN DPILNQIRRV QLFNRSTDRV KVIFHPEFLN SNNPILPLDY
EEFVRGCHLG VFPSYYEPFG YTPAECTVMG IPNITTNLSG FGCFMEDLLE KPEDYGCYIV
DRRGQGIEES VSQLTNQMLD FASKSRRSRI NQRNRTERLS ELLDWKQLGL EYVKARQLAL
RRAYPDSFDD DEPDFTGVQR IGAPLSAPGS PRMRTGAMTP GDIGTLTEEM EHLGTQDYMG
AKSWRSINDE EEDETSYPFP LVMKARNRSD SFGSAFSGVS GQATPHGGRR LSEKDLAKAD
AALSSVQANG DDGDSESNGV NGH
//
