GPGS_MYCTO
ID GPGS_MYCTO Reviewed; 324 AA.
AC P9WMW8; F2GFY0; L0T8Q4; O05309; Q7D8M0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000250|UniProtKB:P9WMW9};
DE Short=GpgS {ECO:0000250|UniProtKB:P9WMW9};
DE EC=2.4.1.266 {ECO:0000250|UniProtKB:P9WMW9};
GN Name=gpgS; OrderedLocusNames=MT1246;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Involved in the biosynthesis of 6-O-methylglucose
CC lipopolysaccarides (MGLPs). Catalyzes the transfer of the glucose
CC moiety from UDP-alpha-D-glucose (UDP-Glc) to the position 2 of 3-
CC phospho-D-glycerate (3-PGA) to form glucosyl-3-phosphoglycerate (GPG).
CC {ECO:0000250|UniProtKB:P9WMW9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + an NDP-alpha-D-glucose = (2R)-2-O-
CC (alpha-D-glucopyranosyl)-3-phospho-glycerate + a ribonucleoside 5'-
CC diphosphate + H(+); Xref=Rhea:RHEA:47244, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:58272, ChEBI:CHEBI:62600,
CC ChEBI:CHEBI:76533; EC=2.4.1.266;
CC Evidence={ECO:0000250|UniProtKB:P9WMW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47245;
CC Evidence={ECO:0000250|UniProtKB:P9WMW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + UDP-alpha-D-glucose = (2R)-2-O-
CC (alpha-D-glucopyranosyl)-3-phospho-glycerate + H(+) + UDP;
CC Xref=Rhea:RHEA:31319, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58272, ChEBI:CHEBI:58885, ChEBI:CHEBI:62600;
CC EC=2.4.1.266; Evidence={ECO:0000250|UniProtKB:P9WMW9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31320;
CC Evidence={ECO:0000250|UniProtKB:P9WMW9};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WMW9};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P9WMW9};
CC Note=Requires divalent cations for activity.
CC {ECO:0000250|UniProtKB:P9WMW9};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WMW9}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000250|UniProtKB:P9WMW9}.
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; AE000516; AAK45503.1; -; Genomic_DNA.
DR PIR; F70609; F70609.
DR RefSeq; WP_003406242.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WMW8; -.
DR SMR; P9WMW8; -.
DR CAZy; GT81; Glycosyltransferase Family 81.
DR EnsemblBacteria; AAK45503; AAK45503; MT1246.
DR GeneID; 45425178; -.
DR KEGG; mtc:MT1246; -.
DR PATRIC; fig|83331.31.peg.1347; -.
DR HOGENOM; CLU_053119_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Magnesium; Manganese; Metal-binding; Transferase.
FT CHAIN 1..324
FT /note="Glucosyl-3-phosphoglycerate synthase"
FT /id="PRO_0000427229"
FT BINDING 50..54
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 81
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 114
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 134..135
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 136
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 184..187
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 229..232
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 256..261
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 260
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
SQ SEQUENCE 324 AA; 34379 MW; 7CE4AE274C1A23BA CRC64;
MTASELVAGD LAGGRAPGAL PLDTTWHRPG WTIGELEAAK AGRTISVVLP ALNEEATIES
VIDSISPLVD GLVDELIVLD SGSTDDTEIR AIASGARVVS REQALPEVPV RPGKGEALWR
SLAATSGDIV VFIDSDLINP HPLFVPWLVG PLLTGEGIQL VKSFYRRPLQ VSDVTSGVCA
TGGGRVTELV ARPLLAALRP ELGCVLQPLS GEYAASRELL TSLPFAPGYG VEIGLLIDTF
DRLGLDAIAQ VNLGVRAHRN RPLDELGAMS RQVIATLLSR CGIPDSGVGL TQFLPGGPDD
SDYTRHTWPV SLVDRPPMKV MRPR
