GenomeNet

Database: UniProt
Entry: A0A143Y4B9_9FIRM
LinkDB: A0A143Y4B9_9FIRM
Original site: A0A143Y4B9_9FIRM 
ID   A0A143Y4B9_9FIRM        Unreviewed;       478 AA.
AC   A0A143Y4B9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
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_2 {ECO:0000313|EMBL:CVI73327.1};
GN   Synonyms=glgA {ECO:0000256|HAMAP-Rule:MF_00484};
GN   ORFNames=BN3660_03051 {ECO:0000313|EMBL:CVI73327.1};
OS   Eubacteriaceae bacterium CHKCI004.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae.
OX   NCBI_TaxID=1780380 {ECO:0000313|EMBL:CVI73327.1, ECO:0000313|Proteomes:UP000199324};
RN   [1] {ECO:0000313|EMBL:CVI73327.1, ECO:0000313|Proteomes:UP000199324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHKC4 {ECO:0000313|EMBL:CVI73327.1};
RA   Oliw E.H.;
RL   Submitted (JAN-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|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; FCNR01000063; CVI73327.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A143Y4B9; -.
DR   STRING; 1780380.BN3660_03051; -.
DR   OrthoDB; 9808590at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000199324; 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:UP000199324};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00484}.
FT   DOMAIN          3..238
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          291..451
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   478 AA;  54866 MW;  127B3594848FE719 CRC64;
     MKKILYAAAE CSPFIKTGGL GAVVGSLPKQ LKERGYDVRI VLPAYECIDE KWKNQMTVSL
     PFPVHMGWRR HPITINTLEY QGITCYFLAC DHYFSGDSPY SEMWMDIEKF SFFSKAVLEM
     LSYLEFEPDI IHCHDWQTGL IPVYLKTEYG NNPYYKNIKT VMTLHNMRFQ GTTDVNTLKD
     ITGLPDEVFA FDKLEFYGQG NMLKGGIAYA DKVTTVSSTY AKEIQEPEYG EGLEGLLQYR
     KNDLSGIVNG IDYQIYSPVQ DEYIKYHYNA NTFRRAKKKN KVYLQNEAGL PADKNIFTVC
     IISRLTEQKG LDLLIPQLND FLSGDVQLYI LGGGEERYEG IFASVKTRYP DKVFFDVNYS
     DAMAKYMYAG CDATLMPSKF EPCGLSQLMA LRYGTVPIVR LTGGLKDTVK VYDSRYHTGT
     GFGFEEYSME ALRDTLQEAM AVYRQQPEEW NRIAERGMRE NYSWNTSCLE YEKLYAGM
//
DBGET integrated database retrieval system