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Database: UniProt
Entry: A0A135LKV3_PENPA
LinkDB: A0A135LKV3_PENPA
Original site: A0A135LKV3_PENPA 
ID   A0A135LKV3_PENPA        Unreviewed;       714 AA.
AC   A0A135LKV3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=PGRI_055370 {ECO:0000313|EMBL:KXG49569.1};
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG49569.1, ECO:0000313|Proteomes:UP000070168};
RN   [1] {ECO:0000313|EMBL:KXG49569.1, ECO:0000313|Proteomes:UP000070168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG3 {ECO:0000313|EMBL:KXG49569.1,
RC   ECO:0000313|Proteomes:UP000070168};
RX   PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA   Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA   Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT   "Genome sequencing and secondary metabolism of the postharvest pathogen
RT   Penicillium griseofulvum.";
RL   BMC Genomics 17:19-19(2016).
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:KXG49569.1}.
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DR   EMBL; LHQR01000048; KXG49569.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135LKV3; -.
DR   STRING; 5078.A0A135LKV3; -.
DR   OMA; RDVRNHI; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000070168; 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:UP000070168};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          673..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..687
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   714 AA;  81363 MW;  00F3AC2D933F223E CRC64;
     MEENGEPIKR DVRNHMLFEV ATEVANRVGG IYSVLKSKAP VTTAEYGERY TLIGPLNRAS
     AAVEVEELTP TNPAMRETIQ SMKERGIDMV YGRWLIEGAP RVLLIDTGTG YKWLDEWKGD
     LWTTSAIPSP AGDNETNEAI VFGYLVAWFL GEYIAHDRRR AVIAHFHEWL AGVALPLTKK
     RHMDLTTVFT THATLLGRYL CAGSVDFYNN LQYFDVDAEA GKRGIYHRYC IERAATHACD
     VFTTVSHITA FESEHLLKRK PDGVLPNGLN VKKFSAMHEF QNLHSQAKEK INDFVRGHFY
     GHNDFDLDNT LYLFTAGRYE YRNKGVDMFI ESLARLNHRL KTAGSAMTVV AFIIMPAQTS
     SLTVEALKGQ AVVKSLRDTI ENIEKGIGKR MYERCLSWKE GDNMPDDKDL ITSQDRVMLR
     RRLFGMKRHG LPPIVTHNMH NDSEDPILNQ LRRVQLFNHS SDRVKVVFHP EFLNSANPVL
     PLDYDDFVRG THLGVFPSYY EPWGYTPAEC TVMGVPSITT NLSGFGCYME ELIENSSDYG
     IYIVDRRAKG VDDSVNQLTD YMFNFTEKSR RQRINQRNRT ERLSDLLDWK RMGLEYVKAR
     QLALRRAYPS SFEGQEDYFD IIGGTEQKLS RPLSVPGSPR DRSGMMTPGD FASLQEGHEG
     LSTEDYIAWK LPEEEEPEEH FPLTLRTRKT GERAASPLDS VTVSRRASED SRAE
//
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