ID B5ECG7_CITBB Unreviewed; 518 AA. AC B5ECG7; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 04-NOV-2026, entry version 92. 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-1 {ECO:0000313|EMBL:ACH37595.1}; GN Synonyms=glgA {ECO:0000256|HAMAP-Rule:MF_00484}; GN OrderedLocusNames=Gbem_0567 {ECO:0000313|EMBL:ACH37595.1}; OS Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 / OS Bem) (Geobacter bemidjiensis). OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfuromonadia; OC Geobacterales; Geobacteraceae; Citrifermentans. OX NCBI_TaxID=404380 {ECO:0000313|EMBL:ACH37595.1, ECO:0000313|Proteomes:UP000008825}; RN [1] {ECO:0000313|EMBL:ACH37595.1, ECO:0000313|Proteomes:UP000008825} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem RC {ECO:0000313|Proteomes:UP000008825}; 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., Kiss H., Brettin T., Detter J.C., Han C., RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Lovley D., Richardson P.; RT "Complete sequence of Geobacter bemidjiensis BEM."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACH37595.1, ECO:0000313|Proteomes:UP000008825} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem RC {ECO:0000313|Proteomes:UP000008825}; RX PubMed=20828392; DOI=10.1186/1471-2164-11-490; RA Aklujkar M., Young N.D., Holmes D., Chavan M., Risso C., Kiss H.E., RA Han C.S., Land M.L., Lovley D.R.; RT "The genome of Geobacter bemidjiensis, exemplar for the subsurface clade of RT Geobacter species that predominate in Fe(III)-reducing subsurface RT environments."; RL BMC Genomics 11:490-490(2010). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001124; ACH37595.1; -; Genomic_DNA. DR RefSeq; WP_012529002.1; NC_011146.1. DR AlphaFoldDB; B5ECG7; -. DR STRING; 404380.Gbem_0567; -. DR KEGG; gbm:Gbem_0567; -. DR eggNOG; COG0297; Bacteria. DR HOGENOM; CLU_009583_18_2_7; -. DR OMA; AAECGPW; -. DR OrthoDB; 9808590at2; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000008825; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0009011; F:alpha-1,4-glucan glucosyltransferase (ADP-glucose donor) activity; IEA:UniProtKB-UniRule. DR GO; GO:0004373; F:alpha-1,4-glucan glucosyltransferase (UDP-glucose donor) activity; IEA:InterPro. 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; NF001899; glgA; 1. DR NCBIfam; TIGR02095; glgA; 1. DR PANTHER; PTHR45825:SF11; ALPHA AMYLASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR45825; GRANULE-BOUND 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}; Reference proteome {ECO:0000313|Proteomes:UP000008825}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00484}. FT DOMAIN 4..246 FT /note="Starch synthase catalytic" FT /evidence="ECO:0000259|Pfam:PF08323" FT DOMAIN 297..419 FT /note="Glycosyl transferase family 1" FT /evidence="ECO:0000259|Pfam:PF00534" FT REGION 493..518 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 17 FT /ligand="ADP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:57498" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484" SQ SEQUENCE 518 AA; 58595 MW; FA2F9EDFAB0F66DD CRC64; MRLNILITAS EAVPFAKEGG LADVVGALPK YLEARGHDVR VVMPRYYNVD RDRYRLRQLP GALVVPMGII GEMYCGVLEG RIPGSDVPIY FLEHEEFYGR DSLYERDNKG YLDNDNRFIF LSKASLELCK MIRFTPDLVH AHDWHTAAVP VLMNSWYRHD QYLSQSASLL TIHNMQHQGS FYEGAMDVLG IGWEHFTYLE LEKENQVNLL KGGIYHATLL NTVSQGYARE IQTSEYGWGL EGVVRERAGE LSGILNGVDY EEWNPEGDPL LPANYSARDL AGKGICKREL QRALGLPERE DVPLIGMVSR LVKQKGIDVL AQALPRILEL DVQLVLLGAG EPWAHFYFGG MAAGRPDRFA CRIGYDNALA HRIEGGCDFF LMPSAFEPCG LNQMYSMRYG TIPIVRATGG LDDSVQNYDA QNRSGDGFKF WDLNAGALFD TVGWAVHTWY QDKEGIHSLR QNAMAKRFTW EDAAAKYERL YLEAMRRKLG EERYGQATSR VTPRKFRNRP TIPGCNTP //