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Database: UniProt
Entry: C9Y2B3_CROTZ
LinkDB: C9Y2B3_CROTZ
Original site: C9Y2B3_CROTZ 
ID   C9Y2B3_CROTZ            Unreviewed;       477 AA.
AC   C9Y2B3;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
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:CBA34262.1};
GN   OrderedLocusNames=Ctu_39380 {ECO:0000313|EMBL:CBA34262.1};
OS   Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA34262.1, ECO:0000313|Proteomes:UP000002069};
RN   [1] {ECO:0000313|Proteomes:UP000002069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC   {ECO:0000313|Proteomes:UP000002069};
RX   PubMed=21037008; DOI=10.1128/JB.01162-10;
RA   Stephan R., Lehner A., Tischler P., Rattei T.;
RT   "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT   pathogen causing deaths in neonates.";
RL   J. Bacteriol. 193:309-310(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; FN543093; CBA34262.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9Y2B3; -.
DR   KEGG; ctu:CTU_39380; -.
DR   PATRIC; fig|693216.3.peg.3734; -.
DR   HOGENOM; CLU_009583_18_4_6; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000002069; 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..233
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          287..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;  52545 MW;  C23B3BA9558404AE CRC64;
     MQVLHVCSEL FPLLKTGGLA DVLGALPAAQ IAEGVDTRVL LPGFPDLRRG VADAKVITRR
     DTFAGPISLL FGHFNGVGIY LIDAPHLYDR PGSPYHDTNL YAYSDNVIRF ALLGWVGSEM
     AAGLDPFWRP DIVHAHDWHA GLTPAYLAAR GRPAKSVFTV HNLAYKGMFY AHHMDDIGLP
     WSMFNMNGLE FNGEISFLKA GLYYADHITA VSPTYAREIT EPQFSYGLEG LLKQRHSEGR
     LSGILNGVDE NIWNPAHDLL LASRYTRDTL EEKAENKRQL QIAMGLKVND KAPLFAVVSR
     LTSQKGLDLV LEALPGLLEQ GGQLALLGAG DPVLQEGFLA AAAEHPGQVG VQIGYHEAFS
     HRIMGGADVI LVPSRFEPCG LTQLYGLKYG TLPLVRRTGG LADTVSDSSL ENLADGIASG
     FVFEDSNAWS LLRAIRRAFV LWSRPSLWRF VQRQAMGMDF SWQVAAKSYR ELYQRLL
//
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