ID A0A0C1JWI3_9BACT Unreviewed; 508 AA.
AC A0A0C1JWI3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:KIC74786.1};
GN ORFNames=DB42_AY00200 {ECO:0000313|EMBL:KIC74786.1};
OS Neochlamydia sp. EPS4.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Neochlamydia.
OX NCBI_TaxID=1478175 {ECO:0000313|EMBL:KIC74786.1, ECO:0000313|Proteomes:UP000031344};
RN [1] {ECO:0000313|EMBL:KIC74786.1, ECO:0000313|Proteomes:UP000031344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPS4 {ECO:0000313|EMBL:KIC74786.1,
RC ECO:0000313|Proteomes:UP000031344};
RX PubMed=25069652; DOI=10.1093/molbev/msu227;
RA Domman D., Collingro A., Lagkouvardos I., Gehre L., Weinmaier T.,
RA Rattei T., Subtil A., Horn M.;
RT "Massive expansion of Ubiquitination-related gene families within the
RT Chlamydiae.";
RL Mol. Biol. Evol. 31:2890-2904(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIC74786.1}.
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DR EMBL; JSDQ01000047; KIC74786.1; -; Genomic_DNA.
DR RefSeq; WP_044881891.1; NZ_JSDQ01000047.1.
DR AlphaFoldDB; A0A0C1JWI3; -.
DR STRING; 1478175.DB42_AY00200; -.
DR PATRIC; fig|1478175.3.peg.949; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000031344; 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; PTHR46083; -; 1.
DR PANTHER; PTHR46083:SF1; GLYCOGEN SYNTHASE 2-RELATED; 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..241
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 305..469
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 508 AA; 58690 MW; 68D83C16EDD8A785 CRC64;
MHIINIASEL APIAKVGGLG DVLLGLSREL SCKGHDIDLI IPKYDCMDTE SIRDFAIYND
SLPSFYKGTW HRNTIWKGWV ENLKVYFIEP HHPAHFFHRG CFYGCADDME RYLYFSRAAL
EFIDKEKLSP HIIHLHDWQT AVIAPLYHEL YRPQCVKEAK IVFTIHNIEY QGHCSSSDLD
NIGLNGSHYL LPDKMQDAQY KEAINLLKGA IIYADHITTV SPNYAKEVLT PLGGRGLDKT
LYKYKNKFKG ILNGIDYSYW NPEIDRYLPT HYSPREAPES KKDRHTLDKK AYIKNFLRER
LFLAEEHRPI VGCIARLVPQ KGIELIKHAL HYTLEKKGQF LLLGSSPIEG INAEFQQLNR
HFHEHPHVRL ILHHSEELAH LIYAASDMFI VPSLFEPCGL TQMIALKYGA IPIVRKTGGL
ADTIWDVDYS GKPIEKTNGY VFEYPDAKGI ESALDRAFEC WFHHPDRWRQ LIIRAMKTDF
SWHTPSDEYL NIYQSILATE KEAKKCPL
//
