ID K1WM00_MARBU Unreviewed; 706 AA.
AC K1WM00;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 03-MAY-2023, entry version 34.
DE RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN ORFNames=MBM_08435 {ECO:0000313|EMBL:EKD13352.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD13352.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD13352.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD13352.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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|RuleBase:RU363104};
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; JH921450; EKD13352.1; -; Genomic_DNA.
DR RefSeq; XP_007296324.1; XM_007296262.1.
DR AlphaFoldDB; K1WM00; -.
DR STRING; 1072389.K1WM00; -.
DR GeneID; 18764370; -.
DR KEGG; mbe:MBM_08435; -.
DR eggNOG; KOG3742; Eukaryota.
DR HOGENOM; CLU_015910_1_0_1; -.
DR InParanoid; K1WM00; -.
DR OMA; RDVRNHI; -.
DR OrthoDB; 9432at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000006753; 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; 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; 1.
PE 3: Inferred from homology;
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056,
KW ECO:0000256|RuleBase:RU363104};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU363104};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT REGION 629..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 706 AA; 80309 MW; A3DE9B666B895FE8 CRC64;
MRREIDTETK RDIRGHYLFE VATEVANRVG GIYSVIKSKA PVTTAEYGDR YCLIGPLHRQ
SAAVEVEALT PTNPQLAATI AAMESRGIGI VYGRWLIEGA PRVVLIDTKT GYRFLDEWKA
DLWHTAGIPS PPGDDETNEA VVFGYLVAWF LGEFVAHEKD KAVIAHFHEW LAGVALPLCK
KRQIDVTTIF TTHATLLGRY LCAGSVDFYN NLQYFDVDHE AGKRGIYHRY CIERAATHAC
DVFTTVSHIT AFESEHLLKR KPDGVLPNGL NVTKFSAMHE FQNLHQQAKE KIHDFVRGHF
YGHNDFDPEN TLYFFTAGRY EYRNKGVDMF IESLTRLNQR LKASGSKMTV VAFIIMPAQT
QSLTVEALKG QAVIKSLRDT VDTIERSVGR RIFERALKWH DGDPMPDDKD LITSQDRILL
RRRLFAMKRE GLPPIVTHNM ANDGDDPILN QIRRVQLFNQ EDDRVKIVFH PEFLNSANPV
LPMDYDEFVR GTHMGVFPSY YEPWGYTPAE CTVMGVPSIT TNLSGFGCYM EELIENSTDY
GIYIVDRRNK GVDDSVNQLA SYMFDFAEKS RRQRINQRNR TERLSDLLDW KRMGMEYVKA
RQLALRRAYP SSFSSEDKDD CIPGIEQKIS RPFSVPGSPR DRSGMMTPGD FASLQEGREG
LSTEDYVAWK LPEEEDPDEY PFPLTLRAKK STSPSSPAES LLTNGN
//