UniProt: A0A0P9EPN5

Database: UniProt
Entry: A0A0P9EPN5_RHOGW

LinkDB:  A0A0P9EPN5_RHOGW 
Original site:  A0A0P9EPN5_RHOGW

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (2)   
   InterPro (1)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (9)   

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ID   A0A0P9EPN5_RHOGW        Unreviewed;       757 AA.
AC   A0A0P9EPN5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=RHOBADRAFT_67056 {ECO:0000313|EMBL:KPV71497.1};
OS   Rhodotorula graminis (strain WP1).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV71497.1, ECO:0000313|Proteomes:UP000053890};
RN   [1] {ECO:0000313|EMBL:KPV71497.1, ECO:0000313|Proteomes:UP000053890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:KPV71497.1,
RC   ECO:0000313|Proteomes:UP000053890};
RX   PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA   Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA   Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT   "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT   graminis WP1.";
RL   Front. Microbiol. 6:978-978(2015).
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; KQ474093; KPV71497.1; -; Genomic_DNA.
DR   RefSeq; XP_018267546.1; XM_018419165.1.
DR   AlphaFoldDB; A0A0P9EPN5; -.
DR   STRING; 578459.A0A0P9EPN5; -.
DR   GeneID; 28979611; -.
DR   OMA; RDVRNHI; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000053890; 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:UP000053890};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          640..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..740
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   757 AA;  85301 MW;  04E7F3E43858B26F CRC64;
     MAQQRSVHDH LLFEVAWEVA NVLGGIYTVI KTKAPVTCAE YGDRYTLMGP LSYKSAPMEV
     EAIEWDKPTP VNEDGNPTTT NASHDALVGT LSSMRDRGVK FLYGRWLIEG GPKVLLFDTG
     SVWNRLDEWK GDLWNLAGIP TPPNDTETNE TLLLGYLVAW FLGEFSARER NRAIICHLHE
     WQAGLAIPLC RKRHIDVTTV FTTHATLLGR YLCAGSVDFY NNLAYFDVDH EAGKRGIYHR
     YCIERSAAHC ADVFTTVSHI TAYEAEHLLK RKPDGVTPNG LNVNKFTAMH EFQNMHAVSK
     QKINEFVRGH FYGHFDFDLD NTLYMFTAGR YEYRNKGLDM FIESLARLNY RLQQMGTKQT
     VVAFIISPAA THSYTIEALK GQAVTKQLRD TVTEIQNRIG ARLFERTARY TGEHGTEVPD
     PAELLSNEDK ILLKRRVFAL RRNSLPPVTT HNMADDANDP ILNQIRRVQL FNRTTDRVKI
     VFHPEFLNSN NPILGMDYEE FVRGCHLGVF PSYYEPWGYT PAECTVMGVP SITTNLSGFG
     GFMEDLLEDS QDYGIYIVDR RQKSVEDSLN QLTDQMVSFC QKTRRQRINQ RNRTERLSDL
     LDWKRMGLEY AKARQLALRR AYPDSFEDDD FDFESGQVRI PRPMSAPASP RFTTARNGMA
     TPSDLATLTE ELQGLGTSDY RGTAQSWESV IRQGDEQDEE SYFPPLVLKK GKNNGGGVSG
     TTSGLTTPGG GSATGGRTTL SEQDLLAADA ALSHHSS
//

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