ID E0IZU1_ECOLW Unreviewed; 477 AA.
AC E0IZU1;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=Glycogen synthase {ECO:0000256|ARBA:ARBA00019935, ECO:0000256|HAMAP-Rule:MF_00484};
DE EC=2.4.1.21 {ECO:0000256|ARBA:ARBA00012588, ECO:0000256|HAMAP-Rule:MF_00484};
DE AltName: Full=Starch [bacterial glycogen] synthase {ECO:0000256|ARBA:ARBA00031722, ECO:0000256|HAMAP-Rule:MF_00484};
GN Name=glgA {ECO:0000256|HAMAP-Rule:MF_00484,
GN ECO:0000313|EMBL:ADT77036.1};
GN OrderedLocusNames=ECW_m3689 {ECO:0000313|EMBL:ADT77036.1};
OS Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC
OS 13500 / NCIMB 8666 / NRRL B-766 / W).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=566546 {ECO:0000313|EMBL:ADT77036.1, ECO:0000313|Proteomes:UP000008525};
RN [1] {ECO:0000313|EMBL:ADT77036.1, ECO:0000313|Proteomes:UP000008525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 /
RC NCIMB 8666 / NRRL B-766 / W {ECO:0000313|Proteomes:UP000008525};
RX PubMed=21208457; DOI=10.1186/1471-2164-12-9;
RA Archer C.T., Kim J.F., Jeong H., Park J.H., Vickers C.E., Lee S.Y.,
RA Nielsen L.K.;
RT "The genome sequence of E. coli W (ATCC 9637): comparative genome analysis
RT and an improved genome-scale reconstruction of E. coli.";
RL BMC Genomics 12:9-9(2011).
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|ARBA:ARBA00004964, 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; CP002185; ADT77036.1; -; Genomic_DNA.
DR RefSeq; WP_001197646.1; NZ_WBMH01000007.1.
DR AlphaFoldDB; E0IZU1; -.
DR SMR; E0IZU1; -.
DR GeneID; 75202274; -.
DR KEGG; elw:ECW_m3689; -.
DR PATRIC; fig|566546.30.peg.3746; -.
DR OMA; TWCPWYM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000008525; Chromosome.
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..234
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 288..438
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; 52822 MW; 177CF37F8C97CF42 CRC64;
MQVLHVCSEM FPLLKTGGLA DVIGALPAAQ IADGVDARVL LPAFPDIRRG VTDAQVVSRR
DTFAGHITLL FGHYNGVGIY LIDAPHLYDR PGSPYHDTNL FAYTDNVLRF ALLGWVGAEM
ASGLDPFWRP DVVHAHDWHA GLAPAYLAAR GRPAKSVFTV HNLAYQGMFY AHHMNDIQLP
WSFFNIHGLE FNGQISFLKA GLYYADHITA VSPTYAREIT EPQFAYGMEG LLQQRHREGR
LSGVLNGVDE KIWSPETDLL LASRYTRDTL EDKAENKRQL QIAMGLKVDD KVPLFAVVSR
LTSQKGLDLV LEALPGLLEQ GGQLALLGAG DPVLQEGFLA AAAEYPGQVG VQIGYHEAFS
HRIMGGADVI LVPSRFEPCG LTQLYGLKYG TLPLVRRTGG LADTVSDCSL ENLADGVASG
FVFEDSNAWS LLRAIRRAFV LWSRPSLWRF VQRQAMAMDF SWQVAAKSYR ELYYRLK
//