ID D4KRG1_9FIRM Unreviewed; 485 AA.
AC D4KRG1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=ROI_25000 {ECO:0000313|EMBL:CBL09463.1};
OS Roseburia intestinalis M50/1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=657315 {ECO:0000313|EMBL:CBL09463.1, ECO:0000313|Proteomes:UP000008807};
RN [1] {ECO:0000313|EMBL:CBL09463.1, ECO:0000313|Proteomes:UP000008807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M50/1 {ECO:0000313|EMBL:CBL09463.1,
RC ECO:0000313|Proteomes:UP000008807};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Roseburia intestinalis M50/1.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL09463.1, ECO:0000313|Proteomes:UP000008807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M50/1 {ECO:0000313|EMBL:CBL09463.1,
RC ECO:0000313|Proteomes:UP000008807};
RA Pajon A.;
RL Submitted (MAR-2010) 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; FP929049; CBL09463.1; -; Genomic_DNA.
DR RefSeq; WP_015560641.1; NC_021040.1.
DR AlphaFoldDB; D4KRG1; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR KEGG; rim:ROI_25000; -.
DR PATRIC; fig|657315.3.peg.3629; -.
DR HOGENOM; CLU_009583_18_2_9; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000008807; 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 3..237
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 290..442
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 485 AA; 55665 MW; 0AAC70241C11AFB0 CRC64;
MKKILFAASE AVPFMKTGGL ADVTGSLPKY FDKKNYDVRV ILPKYVCMEE RWKGQLHFLC
HFYVNLSWRK QYVGIFETTY DGITYYLVDN EFYFAGNAPY NNIYEDVEKF AFFSKAVLEA
LPYLDFCPDI IHCHDWQTGL LPVFLRTLYG DEEYYTGIKT VFSIHNLKFQ GRWKLPAVMD
ITGLPEQIFT SDKLESYGEA NYLKGGVVYA DAVTTVSPTY AYEITTPEGG EGLEGLMYAC
RDKLSGILNG LDYTEYDPQK DVYLTNHYNE VNYKEGKALN KTRLQKNVSL PVDGDVFLIG
MVSRMTDQKG FDLIAYIMDE LLSTERVQFV VAGTGEARYQ DMLSYFAGKY PDKMKVHIGY
SEELAHQIYA SCDAFLMPSL FEPCGLSQLM SLRYGTVPIV RETGGLKDTV IPYNEYTKEG
TGFSFANYNA HEMLATIRYA LSVFYQHKND WDILIKHGMS QDFSWNASVA EYEKLYDSLM
TKFTW
//
