ID A0A0P9C505_9GAMM Unreviewed; 487 AA.
AC A0A0P9C505;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=SAMN05661077_1344 {ECO:0000313|EMBL:SCY14546.1};
OS Thiohalorhabdus denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalorhabdales;
OC Thiohalorhabdaceae; Thiohalorhabdus.
OX NCBI_TaxID=381306 {ECO:0000313|EMBL:SCY14546.1, ECO:0000313|Proteomes:UP000183104};
RN [1] {ECO:0000313|Proteomes:UP000183104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL 19 {ECO:0000313|Proteomes:UP000183104};
RA Varghese N.;
RL Submitted (OCT-2016) 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; FMUN01000003; SCY14546.1; -; Genomic_DNA.
DR RefSeq; WP_054966066.1; NZ_LJCP01000010.1.
DR AlphaFoldDB; A0A0P9C505; -.
DR STRING; 381306.AN478_07890; -.
DR PATRIC; fig|381306.5.peg.220; -.
DR OrthoDB; 9808590at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000183104; Unassembled WGS sequence.
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:UP000183104};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 3..239
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 293..446
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT BINDING 16
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 487 AA; 52506 MW; DCAF3B077B1F3048 CRC64;
MLRILFVTSE VHPFVKTGGL ADVSASLPHA LHELGHDVRV LVPGYADALR RAGNLPVVEA
WRGLPGGPKA RLRAARLPDS GVPVWMLDTP GFSDRPGNPY LAPDGEPHPD NADRFHRLAR
AAAGIAGDRA GLDWRPDVVH CNDWQTGLVP VRMLLERIPA AAVFTIHNLA YQGLFPHATF
QGLGLPPWLW HPEALEFHGH LSFMKGGAVF ADRLTTVSPS YAREIHTAEH GWGLQGLFRQ
RAADLTGILN GIDHRAWDPT TDPYLPAHFS GEDLAGKRDV KAALQGELGL EADPEAPLLG
VVSRLADQKG IDLLLGAARG ILARGAQLAV VGTGDRYYET ALRRLAEYNP GKVGIHLGFS
EALAHRVEAG ADLLLMPSRF EPCGLNQLYA LRYGTVPVVR AVGGLADSVV DATSDALAAG
RATGIAFSGD TAAALTAAVD RALKLYRDGP RWRRMQAAGM EQDFTWERSA AEYVEVYRTA
LEAPVPT
//
