GYS_NEUCR
ID GYS_NEUCR Reviewed; 706 AA.
AC O93869; Q7S7N0; V5IN77;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glycogen [starch] synthase;
DE EC=2.4.1.11;
GN Name=gsy-1; ORFNames=7F4.080, NCU06687;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA de Paula R., Terenzi H.F., Bertolini M.C.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis
CC of glycogen.
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 -!- ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate, and
CC phosphorylation by a cAMP-dependent kinase. {ECO:0000250}.
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 3 family. {ECO:0000305}.
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DR EMBL; AF056080; AAC98780.2; -; mRNA.
DR EMBL; BX294020; CAD70912.1; -; Genomic_DNA.
DR EMBL; CM002240; ESA42591.1; -; Genomic_DNA.
DR EMBL; CM002240; ESA42592.1; -; Genomic_DNA.
DR EMBL; CM002240; ESA42593.1; -; Genomic_DNA.
DR EMBL; CM002240; ESA42594.1; -; Genomic_DNA.
DR RefSeq; XP_011394695.1; XM_011396393.1.
DR RefSeq; XP_011394696.1; XM_011396394.1.
DR RefSeq; XP_011394697.1; XM_011396395.1.
DR RefSeq; XP_011394698.1; XM_011396396.1.
DR AlphaFoldDB; O93869; -.
DR SMR; O93869; -.
DR STRING; 5141.EFNCRP00000006623; -.
DR CAZy; GT3; Glycosyltransferase Family 3.
DR EnsemblFungi; ESA42591; ESA42591; NCU06687.
DR EnsemblFungi; ESA42592; ESA42592; NCU06687.
DR EnsemblFungi; ESA42593; ESA42593; NCU06687.
DR EnsemblFungi; ESA42594; ESA42594; NCU06687.
DR GeneID; 3877149; -.
DR KEGG; ncr:NCU06687; -.
DR VEuPathDB; FungiDB:NCU06687; -.
DR HOGENOM; CLU_015910_1_0_1; -.
DR InParanoid; O93869; -.
DR OMA; YFFTSGR; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IBA:GO_Central.
DR GO; GO:0005978; P:glycogen biosynthetic process; IBA:GO_Central.
DR InterPro; IPR008631; Glycogen_synth.
DR PANTHER; PTHR10176; PTHR10176; 1.
DR Pfam; PF05693; Glycogen_syn; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme; Glycogen biosynthesis; Glycosyltransferase;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..706
FT /note="Glycogen [starch] synthase"
FT /id="PRO_0000194772"
FT REGION 670..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
SQ SEQUENCE 706 AA; 80907 MW; CDF0DB45549FF4BB CRC64;
MAHDNREPRE VKNHLLFEVA TEVAHRVGGI YSVLKSKAPV TTAEYGDRYT LIGPLNHQSA
AVEVEELEPS NPELKATIQA MRDRGIGILY GRWLIEGAPR VLLFDTKTAY GYMNEWKTDL
WNVASIPSPD NDEETNEAIV FGYLVAWFLG EFVCHEKRKA VIAHFHEWLA GVALPLTKKR
QIDVTTIFTT HATLLGRYLC AGSVDFYNNL QWFDVDAEAG KRGIYHRYCI ERAAAHSCDV
FTTVSHITAY ESEHLLKRKP DGVLPNGLNV TKFSAMHEFQ NLHQQNKEKI HDFVRGHFYG
HYDFEPENTL YFFTAGRYEF RNKGVDMFIE SLARLNHRLK TAGSKTTVVA FIIMPAQTTS
LTVEALKGQA VIKSLRDTVD VIERGIGRRI FERSVKWHEG DPLPEEKELI TSQDRVLLRR
RLFAMKRHTL PPIVTHNMLN DHEDPILNQI RRVQLFNHPS DRVKIVFHPE FLSSANPVLP
LDYDDFVRGT HLGVFASYYE PWGYTPAECT VMGVPSITTN LSGFGCYMEE LIENSSDYGI
YIVDRRSKGV DDSVNQLTQY MFEFTQKSRR QRINQRNRTE RLSDLLDWKR MGMEYVKARQ
LALRRAYPTS FNGEEEEDFI PGVEQKISRP FSVPGSPRDR TGMMTPGDFA SLQESHEGLS
TEDYVAWKLP EEEDPEEYPF PLTLKQRTGP GSPLDSIQGL QLNGTR