ID A0A0X1KQL7_9THEM Unreviewed; 486 AA.
AC A0A0X1KQL7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ORFNames=AJ81_04545 {ECO:0000313|EMBL:AJC73595.1};
OS Pseudothermotoga hypogea DSM 11164 = NBRC 106472.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=1123384 {ECO:0000313|EMBL:AJC73595.1, ECO:0000313|Proteomes:UP000077469};
RN [1] {ECO:0000313|EMBL:AJC73595.1, ECO:0000313|Proteomes:UP000077469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11164 {ECO:0000313|EMBL:AJC73595.1,
RC ECO:0000313|Proteomes:UP000077469};
RA Zhang X., Alvare G., Fristensky B., Chen L., Suen T., Chen Q., Ma K.;
RT "Genome sequencing of Thermotog hypogea.";
RL Submitted (JAN-2014) 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; CP007141; AJC73595.1; -; Genomic_DNA.
DR RefSeq; WP_031504818.1; NZ_JONI01000007.1.
DR AlphaFoldDB; A0A0X1KQL7; -.
DR STRING; 1123384.AJ81_04545; -.
DR PaxDb; 1123384-AJ81_04545; -.
DR KEGG; phy:AJ81_04545; -.
DR PATRIC; fig|1123384.7.peg.889; -.
DR OrthoDB; 9808590at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000077469; 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}; Reference proteome {ECO:0000313|Proteomes:UP000077469};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 2..241
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 294..443
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 486 AA; 55707 MW; 53220B1A910495EE CRC64;
MKVAMIAYEV YPFAKVGGLA DVLGALPKAV ERSGAKVTIF MPLHKVVLKN SQKFGYQLSE
VAKSIPVENV QTKETFDLYK SQLPGSGVAV YFIANEYYFS AENVYEGPDL AEQAIFFSAA
SIQAMRHLSE QFDVVHAHDW QTGLVPVYLK TLYRVDPFFS RTAIVFTIHN LGYQGIFSPS
YMKFAGLPGY LFNIDGLEFY GKINFLKGGI LFSDIVTTVS PTYAQEIQTE EYGEKLDGVL
RLRSEDLYGI LNGIDYEEFN PATDRRIYVN YDINSIEKKY ENKKMLQKEL NLPVREEVPL
IGMINRLVDQ KGLDLIEKIA DYMFLFDLQF VVLGTGEKKY EEMFLQLQKR YASKVSSNIK
FDIELAQKIY AGCDMFLMPS RYEPCGLGQM YSLRYGTIPI VRYTGGLADT VKEYDPETGL
GNGFGFREYD PAHLFMAIAK AVHFFKNEKR HWEKIVQNAM QTDVSWERSA KQYMRIYQEA
LKKRRV
//
