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Database: UniProt
Entry: W3AMN1_9FIRM
LinkDB: W3AMN1_9FIRM
Original site: W3AMN1_9FIRM 
ID   W3AMN1_9FIRM            Unreviewed;       481 AA.
AC   W3AMN1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=UYO_2190 {ECO:0000313|EMBL:ETP71874.1};
OS   Lachnospiraceae bacterium JC7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1165092 {ECO:0000313|EMBL:ETP71874.1, ECO:0000313|Proteomes:UP000018967};
RN   [1] {ECO:0000313|EMBL:ETP71874.1, ECO:0000313|Proteomes:UP000018967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC7 {ECO:0000313|EMBL:ETP71874.1,
RC   ECO:0000313|Proteomes:UP000018967};
RA   Rosewarne C.P., Cheung J.L., Evans P.N., Tomkins N.W., Denman S.E.,
RA   O Cuiv P., Morrison M.;
RT   "Isolation and genomic characterisation of Lachnospiraceae sp. JC7, a newly
RT   identified member of the bovine rumen core microbiota.";
RL   Submitted (JUL-2012) 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:ETP71874.1}.
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DR   EMBL; ALYD01000027; ETP71874.1; -; Genomic_DNA.
DR   AlphaFoldDB; W3AMN1; -.
DR   PATRIC; fig|1165092.3.peg.2167; -.
DR   OrthoDB; 9808590at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000018967; 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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00484}.
FT   DOMAIN          3..238
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          294..446
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   BINDING         16
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ   SEQUENCE   481 AA;  56498 MW;  7965EE38489B9358 CRC64;
     MKNVLMLASE AVPFIKTGGL ADVVGSLPKT IDKRYYDCRV MIPKYMCIPW EWRQKMEYVT
     HFYMDYLGQS RYVGVLKYEL EGVTYYFIDN ESYFSGDRPY GDWYWDLEKF SFFCYAALSA
     LPLLGWHPDL IHCHDWQTGL IPVLLHDNFA GGEFYRSIKS VITIHNLKFQ GVWDVKTIQR
     FTQLSDYYFT ADKLECKKDG NLLKGGIVYA DAITTVSDTY AEEIKMPFYG EGLDGLLRAR
     EHDLRGIVNG IDYNEWDPET DKYLVKNYNA KNFRKEKFKN KKALQEDWGM DVDPGKMMIG
     IVSRLTDQKG LDLVECIMDE LCQDNIQFVV LGTGDEKYEN MFRHYDWKYH NKVSAQIYYS
     NEISHKMYAA CDAYLMPSLF EPCGLSQLIA LRYGTIPIVR ETGGLRDTVE PFNEYEDKGT
     GFSFSNYNAH EMLNTIRYAE KIYYDRKRDW NKMVDRAMAK DYSWRTSAMK YQELYDWLIG
     Y
//
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