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Database: UniProt
Entry: A0A1H8Z2G4_9FIRM
LinkDB: A0A1H8Z2G4_9FIRM
Original site: A0A1H8Z2G4_9FIRM 
ID   A0A1H8Z2G4_9FIRM        Unreviewed;       482 AA.
AC   A0A1H8Z2G4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=SAMN02910289_00031 {ECO:0000313|EMBL:SEP58532.1};
OS   Lachnospiraceae bacterium RM5.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1200721 {ECO:0000313|EMBL:SEP58532.1, ECO:0000313|Proteomes:UP000199252};
RN   [1] {ECO:0000313|EMBL:SEP58532.1, ECO:0000313|Proteomes:UP000199252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM5 {ECO:0000313|EMBL:SEP58532.1,
RC   ECO:0000313|Proteomes:UP000199252};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOFK01000002; SEP58532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8Z2G4; -.
DR   STRING; 1200721.SAMN02910289_00031; -.
DR   OrthoDB; 9808590at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000199252; 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:UP000199252};
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          291..438
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   482 AA;  55605 MW;  0A5A2B844098F476 CRC64;
     MKNILFVASE AVPFIKTGGL ADVVGSLPKC FNKEEFDVRV ILPKYLSMPW HFTERLEFLA
     YFYMDIGYQS KYVGVFKLVH DGITFYFIDN EGYFGGPKPY GDLKYDLEKF AYFSRAALSV
     LPVIGFKPDI VHCHDWQTAM VPIYMKDSFR GGEFYQNMKS ILTIHNLKFQ GVWDIETIQG
     ITGLSDYYFT IDKLKVKEDA NLLKGGIAYA DYVTTVSETY AEEIKTPFYG EGLDGLMRAR
     SNSLCGIVNG IDYNEYNPET DDKIDFKYNA INFRKEKFKN KTALQQQLGL EVNKDKFMIG
     IVSRLTDQKG IDLVAYIMDE MCSRDDIQLV VLGTGDAKFE NMFRYFDWKY SNRVAACIYY
     SEEMSHKVYA SCDAFLMPSL FEPCGLSQLM ALRYGTIPIV RETGGLKDTV VPYNQFESTG
     TGFSFTNYNA HEMLGTIDFA KYVYYNKKRE WNKLVDRAMA ADFSWNKSAE RYANLYNWML
     SW
//
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