ID R5LUC2_9FIRM Unreviewed; 605 AA.
AC R5LUC2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=BN569_00372 {ECO:0000313|EMBL:CCY76681.1};
OS Butyrivibrio crossotus CAG:259.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1263062 {ECO:0000313|EMBL:CCY76681.1, ECO:0000313|Proteomes:UP000018300};
RN [1] {ECO:0000313|EMBL:CCY76681.1, ECO:0000313|Proteomes:UP000018300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:259 {ECO:0000313|Proteomes:UP000018300};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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 -!- 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:CCY76681.1}.
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DR EMBL; CAYU010000039; CCY76681.1; -; Genomic_DNA.
DR AlphaFoldDB; R5LUC2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000018300; 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:UP000018300};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 125..361
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 416..573
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 28..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 137
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 605 AA; 68267 MW; 8E84F12C57B742C9 CRC64;
MDNKKSAANS GVKDNLTEVK VTNEEVLASK KATETAKKTT AKTTSTAKKT TAKTTTAAKK
TTAKTTGTAK KTTAKTTATT KKTTAKKAEI AAESVAAENI PVTQESVVTE NIPAAPVDLG
PRRSVAFIGS ECYPFAKTGG LGDVMSALPK SLAKLNLDVK VILPRYKCIP WKYQEKMEYR
GSFYMNLCAD GRQYYVGIME YQEDGVVYDF IDNDDFFSWG NPYTNLIDDI PKFCFFAKAS
LAALNYLDWT PDVVHCHDWQ AALVPLYLRT CFKDTNVGRA SAVLTIHNLK FQGIYDRKMI
QYWSGLPDYV FNKDCMIQNW LDANMLKGGI AYANKVTTVS NTYAWEIQTE EYGEGLAEHL
RYHSDKIRGI VNGIDTDNWN PATDKLLAAN YDAETAIANK KINKKTLQES LGLDVDDHKI
VIGLISRLTN QKGLDLVNDI IPSIMDEHTQ VVVLGTGDSW YENTFRYYED KYKGNFCAYI
AYDENVAHNI YSGCDALLVP SRFEPCGLTQ LIAMRYGTIP IVRETGGLKD TVQPYNMFDN
TGNGFTFDRY ERGLLYDAIN RAKTLYFENR KYWDDMVIRD MKKDVSWEKS ARQYKDMYVE
LTPRY
//