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Database: UniProt
Entry: A0A091UIH7_PHORB
LinkDB: A0A091UIH7_PHORB
Original site: A0A091UIH7_PHORB 
ID   A0A091UIH7_PHORB        Unreviewed;       603 AA.
AC   A0A091UIH7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
DE   Flags: Fragment;
GN   ORFNames=N337_05031 {ECO:0000313|EMBL:KFQ90012.1};
OS   Phoenicopterus ruber ruber.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Phoenicopteriformes; Phoenicopteridae;
OC   Phoenicopterus.
OX   NCBI_TaxID=9218 {ECO:0000313|EMBL:KFQ90012.1, ECO:0000313|Proteomes:UP000053700};
RN   [1] {ECO:0000313|EMBL:KFQ90012.1, ECO:0000313|Proteomes:UP000053700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N337 {ECO:0000313|EMBL:KFQ90012.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Glycogen synthase participates in the glycogen biosynthetic
CC       process along with glycogenin and glycogen branching enzyme. Extends
CC       the primer composed of a few glucose units formed by glycogenin by
CC       adding new glucose units to it. In this context, glycogen synthase
CC       transfers the glycosyl residue from UDP-Glc to the non-reducing end of
CC       alpha-1,4-glucan. {ECO:0000256|ARBA:ARBA00043883}.
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; KK435085; KFQ90012.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091UIH7; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000053700; 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   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176:SF1; GLYCOGEN [STARCH] SYNTHASE, LIVER; 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|RuleBase:RU363104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053700};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          520..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ90012.1"
FT   NON_TER         603
FT                   /evidence="ECO:0000313|EMBL:KFQ90012.1"
SQ   SEQUENCE   603 AA;  69830 MW;  019C5D57F1D0C908 CRC64;
     VFFGRWLIEG SPYVLLFDIG SAAWNLDRWK GEFWDVSNIG IPFHDREAND AVIFGSLTAW
     FLKELSCQFD DKPNIIAHFH EWQAGVGLIL SRSQKLPVAT IFTTHATLLG RYLCAASIDF
     YNNLDQFDID KEAGERQIYH RYCMERASVH CAHVFTTVSQ ITAIEAEHML KRNPDVVTPN
     GLNIKKFSAM HEFQNLHSMY KARIQEFIRG HFYGHLDFSL EKTLFFFIAG RYEFSNKGAD
     MFLEALSRLN FLLRVHKTDV TVVVFFIMPA KTNNFNVETL KGQAVRKQLW DTAQSVKEKF
     GKKLYNALLK GEIPDLNKIL DRDDITIMKR AIFSTQRHCL PPVTTHNMID DGNDPILNTI
     RRIGLFNNRT DRVKVILHPE FLSSTSPLLP LDYEEFVRGC HLGVFPSYYE PWGYTPAECT
     VMGIPSVTTN LSGFGCFMQE HVADPAAYGI YIVDRRFRSP DESCNQLTQF LYGFCQQSRR
     QRIIQRNRTE RLSDLLDWRY LGRYYMHARH LALSRTFPDK FEMEPSAPPK TEGFRYPRPS
     SVPPSPSVSQ HSSPHHSEDE DEDEDERYDE DEEAERDRQN IKSPFSLGVL PQGKKKQHGE
     YRN
//
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