ID A0A1I4GL24_9FIRM Unreviewed; 600 AA.
AC A0A1I4GL24;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=SAMN02983006_00785 {ECO:0000313|EMBL:SFL30579.1};
OS Halanaerobium salsuginis.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=29563 {ECO:0000313|EMBL:SFL30579.1, ECO:0000313|Proteomes:UP000199006};
RN [1] {ECO:0000313|EMBL:SFL30579.1, ECO:0000313|Proteomes:UP000199006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51327 {ECO:0000313|EMBL:SFL30579.1,
RC ECO:0000313|Proteomes:UP000199006};
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; FOTI01000007; SFL30579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4GL24; -.
DR STRING; 29563.SAMN02983006_00785; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000199006; 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 Gene3D; 1.10.150.320; Photosystem II 12 kDa extrinsic protein; 1.
DR HAMAP; MF_00484; Glycogen_synth; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR011835; GS/SS.
DR InterPro; IPR010994; RuvA_2-like.
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 Pfam; PF12836; HHH_3; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 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:UP000199006};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 6..240
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 293..442
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 510..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 19
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 600 AA; 67909 MW; 49E1D5892AE03010 CRC64;
MQKKLKILFV ASEADPFIKT GGLADVAGSL PQALREAGHD VRLVIPQYSQ IPAVYKEKMQ
SVCHFRTQLA WRDTYLGVNQ LTESGVPVYF IDNKYYFDRD SIYENEDRHE QFAFFCQAVL
DMLPVLNFKP DIIHLNDWQT GPLPLLLADH YRQQNFYRDI KTVFTIHNLR YQGQFSGHIA
ADVLGVAPEH WASGKIRHNG LLNYMKTAIM YADQLTTVSE TYAQEIQTAY FGEGLDYALR
MRGDDLTGII NGLSYSKFNP ETDSKIAVPY SAADVTKKLA NKVHLQQKLG LEVDVERPII
GFISRLVEQK GIELIKAVFP QIMESGAQLV VLGTGQPEYE KFFLNQQQYY PDSLSVTINY
NSNLASQIYA GIDLFLMPSR FEPCGLSQLI SFRYGVLPIV RETGGLNDTV LSYNEATGAG
TGFSFSNYNA HDMLHTIERA INFYQDEDLW HDLVQRVMKL DYSWHNSAQK YLSLYKNLMD
SLSAKKSSTV SKKISRFSKN KTAIKVFKPE PAPLSNKNSL PEKTNLKRTK KKKESGQLVN
INLATAAEFA LLPGIGDFYA ERIVAYRSAS SNGFNKKTDL KKVKGIGKKK YKQISDLITL
//
