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Database: UniProt
Entry: G4HFU1_9BACL
LinkDB: G4HFU1_9BACL
Original site: G4HFU1_9BACL 
ID   G4HFU1_9BACL            Unreviewed;       477 AA.
AC   G4HFU1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=PaelaDRAFT_2852 {ECO:0000313|EMBL:EHB64608.1};
OS   Paenibacillus lactis 154.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB64608.1, ECO:0000313|Proteomes:UP000003891};
RN   [1] {ECO:0000313|EMBL:EHB64608.1, ECO:0000313|Proteomes:UP000003891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=154 {ECO:0000313|EMBL:EHB64608.1,
RC   ECO:0000313|Proteomes:UP000003891};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Siebers A., Thelen M., Hugenholtz P.,
RA   Allgaier M., Woyke T.J.;
RT   "The draft genome of Paenibacillus lactis 154.";
RL   Submitted (SEP-2011) 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; AGIP01000005; EHB64608.1; -; Genomic_DNA.
DR   RefSeq; WP_007130022.1; NZ_AGIP01000005.1.
DR   AlphaFoldDB; G4HFU1; -.
DR   STRING; 743719.PaelaDRAFT_2852; -.
DR   PATRIC; fig|743719.3.peg.2879; -.
DR   eggNOG; COG0297; Bacteria.
DR   OrthoDB; 9808590at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000003891; 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          2..236
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          293..451
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   477 AA;  54393 MW;  F31FA56A59AF8126 CRC64;
     MKLLYAASEC GPFIKTGGLA DVIAALPKAL RSLGTDIRVV LPKYKDIPGE YRERMTHLGE
     TRVQVGWRQQ YCGIESLVED GVTIYFIDNE YYFGRDGIYG YMDDGERFAY FNRAVLDMLP
     VIDYQPDVLH CHDWHTAMIP LLLEDVYRHD PFYSGIKTVF TIHNLLYQGV FPYEVLVDLL
     GIHSRYFTAD GVEYYGNLNF MKAGIIYSDH VTTVSPTYAS EIQTGYYGYG LDGLLSAQGA
     RLSGIVNGID TKSYNPANDP HLAVKYRSDL QKKTQNKIEL QQELGLPVAP HVPMISMVTR
     LVDSKGLDLV IRILDELLYY DEVQFIVLGT GDPSYEHWFR EAANRYPNKM SAQIRFNEPL
     SRRFYAGSDL FLMPSKFEPC GISQLIAMRY GSVPIVRETG GLNDTVQSYN EFTGEGNGFS
     FKNYNAHDMM HTIRRAVSLY RQPEHWRKVT KNALSGDYSW SASAKQYMDI YERIITG
//
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