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Database: UniProt
Entry: A0A369XWP5_9FUSO
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ID   A0A369XWP5_9FUSO        Unreviewed;       475 AA.
AC   A0A369XWP5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Glycogen synthase {ECO:0000256|HAMAP-Rule:MF_00484};
DE            EC=2.4.1.21 {ECO:0000256|HAMAP-Rule:MF_00484};
DE   AltName: Full=Starch [bacterial glycogen] synthase {ECO:0000256|HAMAP-Rule:MF_00484};
GN   Name=glgA {ECO:0000256|HAMAP-Rule:MF_00484};
GN   ORFNames=DV867_12755 {ECO:0000313|EMBL:RDE59516.1};
OS   Psychrilyobacter sp. S5.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Psychrilyobacter.
OX   NCBI_TaxID=2283384 {ECO:0000313|EMBL:RDE59516.1, ECO:0000313|Proteomes:UP000253914};
RN   [1] {ECO:0000313|EMBL:RDE59516.1, ECO:0000313|Proteomes:UP000253914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S5 {ECO:0000313|EMBL:RDE59516.1,
RC   ECO:0000313|Proteomes:UP000253914};
RA   Yadav S., Villanueva L., Damste J.S.S.;
RT   "Draft genome sequence of Psychrilyobacter sp. strain S5.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
CC       {ECO:0000256|ARBA:ARBA00002764, ECO:0000256|HAMAP-Rule:MF_00484}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-
CC         alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA-
CC         COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001478, ECO:0000256|HAMAP-
CC         Rule:MF_00484};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00484}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010281, ECO:0000256|HAMAP-Rule:MF_00484}.
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:RDE59516.1}.
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DR   EMBL; QQOU01000027; RDE59516.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369XWP5; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000253914; Unassembled WGS sequence.
DR   GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR   GO; GO:0009011; F:starch synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   HAMAP; MF_00484; Glycogen_synth; 1.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR011835; GS/SS.
DR   InterPro; IPR013534; Starch_synth_cat_dom.
DR   NCBIfam; TIGR02095; glgA; 1.
DR   PANTHER; PTHR45825; GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR   PANTHER; PTHR45825:SF11; STARCH SYNTHASE 1, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW   Rule:MF_00484};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00484}; Reference proteome {ECO:0000313|Proteomes:UP000253914};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00484}.
FT   DOMAIN          2..233
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          288..445
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   BINDING         15
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ   SEQUENCE   475 AA;  54868 MW;  23B2B97EE2FC1FD1 CRC64;
     MKILFVTSEA HPFAKSGGLG DVAHSLPKAL VKTTDIRVIM PKYTSIHDRY RSGMKLISKF
     TTKVSWREKY VGLYRMKYDK IPFYFIDNEG YFNRPNAYGY FDDGERFSYF SRAVIDAIEH
     MDFVPDIIHC NDWQSALIPV FLKAFYGEKY KDIKVVYTIH NLKFQGVYSK QTLHDILGLS
     DYYFDEEKLK FNDAISYMKG GITFSDYITT VSDTYANEIK YPFFGEGLHG LFQKLDYKVT
     GIVNGIDYET FNPRKDKELH TKYGISTREK KIENKLALQR ELGLLESENI PVIGIVTRLT
     GQKGLDLIAH ILEELLILDI QLVVLGTGDI QFEDLFKYYA HIYPSKLSAN ITFDSTLAKK
     IYAGSDMFLM PSLFEPCGLS QLISMRYGTI PIVRETGGLK DTVIPYNEFK GTGTGFGFRN
     YNAHELLETL KYALKIYEKK EHWDKLVKNA MERKSSWANA AKEYKKIYKE LINKK
//
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