ID A0A1Y1VWV2_9FUNG Unreviewed; 768 AA.
AC A0A1Y1VWV2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN ORFNames=BCR32DRAFT_297715 {ECO:0000313|EMBL:ORX65466.1};
OS Anaeromyces robustus.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Anaeromyces.
OX NCBI_TaxID=1754192 {ECO:0000313|EMBL:ORX65466.1, ECO:0000313|Proteomes:UP000193944};
RN [1] {ECO:0000313|EMBL:ORX65466.1, ECO:0000313|Proteomes:UP000193944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4 {ECO:0000313|EMBL:ORX65466.1,
RC ECO:0000313|Proteomes:UP000193944};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX65466.1, ECO:0000313|Proteomes:UP000193944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4 {ECO:0000313|EMBL:ORX65466.1,
RC ECO:0000313|Proteomes:UP000193944};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-2016) 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:ORX65466.1}.
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DR EMBL; MCFG01000461; ORX65466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1VWV2; -.
DR STRING; 1754192.A0A1Y1VWV2; -.
DR OrthoDB; 9432at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000193944; 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; 2.
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:UP000193944};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT REGION 656..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..670
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 88218 MW; 0DF8A36EF794C7B5 CRC64;
MAETNETVDM SKPLLFEVAW EVANKVGGIY TVIKSKTPVT VGEYGDRYCL IGPLSWNTAP
MEVEEIEPSS QPLKETLESM KNSGIHFLYG RWLIEGAPAV LLFDISSAHN RMNEWKTDLW
CISGVPSPPD DFETNEAIVF GYLVAWFLGE FSHRLSTKAN KVPSDFQISP TANDLKNYQL
IHPMSQHPSI YSNYHSSDHP LIIAHFHEWL AGVALILIRK RNLPVATIFT THATLLGRYL
CAGDVDFYNN LKYFDVDAEA GKRQIYHRYC VERGAAHCAD VFTTVSHITA YESEWLLKRK
PDGVLPNGLN VVKFSAIHEF QNLHAQNKEK INEFIRGHFY GHFDFDLDNT LYFFTSGRYE
YRNKGVDMYI ESLARLNGRL KHYNSPVTVV AFIIMPAATH NFAVDALKGQ AVMKQLRQTV
GEMQEMIGKR ILDSAARGQT PDMAHILSDE EQIVLKRRIF ALRRANLPPI TTHNMADDSH
DPILNHIRRV QLFNSPSDRV KIIFHPEFLN QNNPLIGMDY EEFVRGCHLG VFPSYYEPWG
YTPAECTVMG VPSITTNLSG FGCFMEEMIT HPNDYGIYIV DRRMRGIEES VQQLTDFMFD
FSQKSRRQRI NQRNRTERLS DLLDWKRMGI EYQKARWVAV RRKWPEAALF EEIDDEDNKE
EVEEQNDAAL YSEGEETIRG RRTRKIPRPP SAPGSPRIKE SFEDEQVEDT WEEAVNEKDV
TKPENHDHIL IEQLKQLNVD GREKQIAAGH IVDDSYNDVP AEVKASED
//
