ID M9MDN9_PSEA3 Unreviewed; 744 AA.
AC M9MDN9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN ORFNames=PANT_7c00262 {ECO:0000313|EMBL:GAC72762.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC72762.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
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; DF196773; GAC72762.1; -; Genomic_DNA.
DR AlphaFoldDB; M9MDN9; -.
DR STRING; 1151754.M9MDN9; -.
DR OrthoDB; 9432at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000011976; 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; 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:UP000011976};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT REGION 631..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 84427 MW; 2401A44EC78AF15F CRC64;
MAPDHSQSPK RDVHNPLLFE CAWEVANKVG GIYTVIKTKA PVTHQEYGDR YTLIGPLSYK
TAPMEVEALE PEDPLLKETL DSMRDAGVKF LYGRWLIERA PRVLLFDTSS MYHRMDEWKG
DLWNLAGIPT PSHDHETNET LVFGYLTAWF LGEYSSRERK RAIIAHFHEW QAGLAIPLCR
KRHIDVTTIF TTHATLLGRY LCAGSVDFYN NLQYFDVDHE AGKRGIYHRY CVERAAAHCA
DVFTTVSHIT AYESEHLLKR KPDGVLPNGL NVVKFSAMHE FQNLHAVSKA KINEFVKGHF
YGHYDFDLEN TLYFFTAGRY EYRNKGVDMF IESLARLNYK LQKSGSKTTV VAFIIMPAAT
NSYTIEALKG QAVTKQLRDT VEQIQARVGE RLFDKMARYQ GETGSDVIDP ATLLSDADKI
ALKKRIFALK RNSLPPVVTH NMQDDDNDPI LNQIRRVQLF NRTSDRVKVI FHPEFLNANN
PILGLDYEEF VRGCHLGVFP SYYEPWGYTP AECTVMGVPS ITTNLSGFGC FMEDTIERGE
DYGIYIVDRR MKSVEDSVNQ LTDQMFQFSQ KTRRQRINQR NRTERLSELL DWKRLGLEYA
KARQLALRRA YPDSFEEDDT IESYFDDIHG DGKMPPPLSM PGSPSGAGAR TPGEFGTLTE
ELQGLSTSDY KGHQQFWKTM SQHGSDDEEE AYRFPLVIKS RNRGTSVGSM SGASTPGLGG
GKFLSSADLD RADAALSNHA PNGH
//
