ID I0GN12_SELRL Unreviewed; 478 AA.
AC I0GN12;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 ECO:0000313|EMBL:BAL82149.1};
GN OrderedLocusNames=SELR_04410 {ECO:0000313|EMBL:BAL82149.1};
OS Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / TAM6421).
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=927704 {ECO:0000313|EMBL:BAL82149.1, ECO:0000313|Proteomes:UP000007887};
RN [1] {ECO:0000313|EMBL:BAL82149.1, ECO:0000313|Proteomes:UP000007887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103574 / TAM6421 {ECO:0000313|Proteomes:UP000007887};
RA Oguchi A., Ankai A., Kaneko J., Yamada-Narita S., Fukui S., Takahashi M.,
RA Onodera T., Kojima S., Fushimi T., Abe N., Kamio Y., Yamazaki S.,
RA Fujita N.;
RT "Whole genome sequence of Selenomonas ruminantium subsp. lactilytica
RT TAM6421.";
RL Submitted (OCT-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; AP012292; BAL82149.1; -; Genomic_DNA.
DR RefSeq; WP_014423593.1; NC_017068.1.
DR AlphaFoldDB; I0GN12; -.
DR KEGG; sri:SELR_04410; -.
DR PATRIC; fig|927704.6.peg.452; -.
DR eggNOG; COG0297; Bacteria.
DR HOGENOM; CLU_009583_18_2_9; -.
DR OrthoDB; 9808590at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000007887; 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..236
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 293..448
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 478 AA; 55317 MW; 90E545B5970D7E8A CRC64;
MKVLYVASEA VPFVKTGGLA DVAGSLPKAL LKEDVDIRVI MPKYGAIAKE YIDQMEHVYD
GELEVAWRSK YVGLDKLEKD GVTYYFVDNQ EYYNREGFYG YDDDAERFSF FSRAVLNLLP
AMDFWPDVIH SNDWHAGLVN VFLKLEHMDD ERYQHIKTLY TIHNLKYQGV FPKDIMQDVL
GLDWKYFNNG DLEFFDAVNF MKGGIIYSDY VSTVSKTYAQ EIQYEYFGEH LDGLLRSRRD
DLFGIVNGID YDVYNPMTDK NLFETYDVDS QDRKMDNKVA LQKMLGLPEG RRTPVVALVS
RLVAAKGLDL IVRMMDEILM HEDIQFIVLG TGDKEYEDWF KGLAWRFPHK VSANIKFSNE
LAQRIYAGAD IFLMPSNYEP CGIGQIVAMR YGTIPVVRET GGLKDTVQQY DKYTQTGNGF
VFNDYNAHEM MYALKRALSA YGNYEEWNNI VHNAMATDFS WTNSAKEYKK LYEQLVNK
//