ID B2UHJ4_RALPJ Unreviewed; 543 AA.
AC B2UHJ4;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 100.
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 OrderedLocusNames=Rpic_3940 {ECO:0000313|EMBL:ACD29045.1};
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29045.1};
RN [1] {ECO:0000313|EMBL:ACD29045.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=12J {ECO:0000313|EMBL:ACD29045.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome2 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) 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|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; CP001069; ACD29045.1; -; Genomic_DNA.
DR AlphaFoldDB; B2UHJ4; -.
DR STRING; 402626.Rpic_3940; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR KEGG; rpi:Rpic_3940; -.
DR PATRIC; fig|402626.5.peg.179; -.
DR eggNOG; COG0297; Bacteria.
DR HOGENOM; CLU_009583_18_4_4; -.
DR UniPathway; UPA00164; -.
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 6..238
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 285..445
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 502..523
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 543 AA; 58339 MW; 7B9BFDA9A5D32A6C CRC64;
MTLSLNVLFV ASEAVPLAKT GGLGDMVGAC ANALRRAGMK VTVMLPGYPD AITQLQHTRT
VCEWTDLPGG PARLLSGHMG AQGIPVLLFD APALFARPGN PYLDAHGEPY EDNALRFASF
SQAAARVAGG VPGVHRSDTV QAHDWHAGLV PLFVKRAQAP VKTVFTIHNL AFQGNFPMHV
VPDIGVPPDA AHEAEFWGQF SFLKAGLLWA DRITTVSHAY AREILTDTAG CGMQDLLRAR
QRDLIAILNG IDNDVWNPSK DPLLPQPFVA SNLSGKHTAK RVLQQRFGLP EDAKAPLLAV
GSRLTHQKMA DVTLQALPQL LESNPQLQVA VLGCGEHAYE TGMADLAARY PRQVAAKIGY
TEAFAHLLHA GADILLHGSR FEPCGLTPLY SMRYGTVPVA SRVGGLMDTI TDRGSPEAAL
HGATGFLFDG DTADAMVAAV ERALHVFAQP QAWRILQYNG MTTDFGWSQP AREYIALYRT
LVPAATPMPA VALVQAPVAP DAVHTPRPEQ PVRTPARRRS TALSDEIRAH AVARAASAEK
IRA
//
