GPGS_MYCBO
ID GPGS_MYCBO Reviewed; 324 AA.
AC Q7U0E1; A0A1R3XXP0; X2BGZ8;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000303|PubMed:18221489};
DE Short=GpgS {ECO:0000305};
DE EC=2.4.1.266 {ECO:0000269|PubMed:18221489};
GN Name=gpgS; OrderedLocusNames=BQ2027_MB1240;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=18221489; DOI=10.1111/j.1574-6968.2007.01064.x;
RA Empadinhas N., Albuquerque L., Mendes V., Macedo-Ribeiro S., da Costa M.S.;
RT "Identification of the mycobacterial glucosyl-3-phosphoglycerate
RT synthase.";
RL FEMS Microbiol. Lett. 280:195-202(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) IN COMPLEX WITH UDP.
RX PubMed=28625787; DOI=10.1016/j.str.2017.05.009;
RA Albesa-Jove D., Romero-Garcia J., Sancho-Vaello E., Contreras F.X.,
RA Rodrigo-Unzueta A., Comino N., Carreras-Gonzalez A., Arrasate P.,
RA Urresti S., Biarnes X., Planas A., Guerin M.E.;
RT "Structural snapshots and loop dynamics along the catalytic cycle of
RT glycosyltransferase GpgS.";
RL Structure 25:1034-1044(2017).
CC -!- FUNCTION: Involved in the biosynthesis of 6-O-methylglucose
CC lipopolysaccarides (MGLPs). Catalyzes the transfer of the glucose
CC moiety from a nuleotide sugar such as UDP-alpha-D-glucose to the
CC position 2 of 3-phospho-D-glycerate (3-PGA) to form glucosyl-3-
CC phosphoglycerate (GPG). It can use UDP-glucose, ADP-glucose and GDP-
CC glucose as sugar donor substrates with decreasing affinity and with 3-
CC PGA as an acceptor. D-glycerate can only be an acceptor with ADP-
CC glucose and at a very low rate. {ECO:0000269|PubMed:18221489}.
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:0000269|PubMed:18221489};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47245;
CC Evidence={ECO:0000305|PubMed:18221489};
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:0000269|PubMed:18221489};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31320;
CC Evidence={ECO:0000305|PubMed:18221489};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ADP-alpha-D-glucose = (2R)-2-O-
CC (alpha-D-glucopyranosyl)-3-phospho-glycerate + ADP + H(+);
CC Xref=Rhea:RHEA:31311, ChEBI:CHEBI:15378, ChEBI:CHEBI:57498,
CC ChEBI:CHEBI:58272, ChEBI:CHEBI:62600, ChEBI:CHEBI:456216;
CC EC=2.4.1.266; Evidence={ECO:0000269|PubMed:18221489};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31312;
CC Evidence={ECO:0000305|PubMed:18221489};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + GDP-D-glucose = (2R)-2-O-(alpha-D-
CC glucopyranosyl)-3-phospho-glycerate + GDP + H(+);
CC Xref=Rhea:RHEA:31315, ChEBI:CHEBI:15378, ChEBI:CHEBI:58127,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:58272, ChEBI:CHEBI:62600;
CC EC=2.4.1.266; Evidence={ECO:0000269|PubMed:18221489};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31316;
CC Evidence={ECO:0000305|PubMed:18221489};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18221489};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P9WMW9};
CC Note=Requires divalent cations for activity. The maximum activity is
CC observed between 20 and 75 mM of MgCl(2).
CC {ECO:0000269|PubMed:18221489};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.04 mM for 3-PGA (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18221489};
CC KM=2.43 mM for UDP-glucose (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18221489};
CC KM=6.63 mM for ADP-glucose (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18221489};
CC KM=27.7 mM for GDP-glucose (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18221489};
CC Vmax=1.42 umol/min/mg enzyme towards 3-PGA
CC {ECO:0000269|PubMed:18221489};
CC Vmax=1.56 umol/min/mg enzyme towards UDP-glucose
CC {ECO:0000269|PubMed:18221489};
CC Vmax=1.69 umol/min/mg enzyme towards GDP-glucose
CC {ECO:0000269|PubMed:18221489};
CC Vmax=3.56 umol/min/mg enzyme towards ADP-glucose
CC {ECO:0000269|PubMed:18221489};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:18221489};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. The activity is
CC undetectable below 20 and above 55 degrees Celsius.
CC {ECO:0000269|PubMed:18221489};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:18221489}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; LT708304; SIT99841.1; -; Genomic_DNA.
DR RefSeq; NP_854894.1; NC_002945.3.
DR RefSeq; WP_003406242.1; NC_002945.4.
DR PDB; 5JUD; X-ray; 2.59 A; A=1-324.
DR PDBsum; 5JUD; -.
DR AlphaFoldDB; Q7U0E1; -.
DR SMR; Q7U0E1; -.
DR CAZy; GT81; Glycosyltransferase Family 81.
DR EnsemblBacteria; SIT99841; SIT99841; BQ2027_MB1240.
DR GeneID; 45425178; -.
DR PATRIC; fig|233413.5.peg.1360; -.
DR OMA; HLVKSFY; -.
DR Proteomes; UP000001419; 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 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Magnesium; Manganese; Metal-binding;
KW Transferase.
FT CHAIN 1..324
FT /note="Glucosyl-3-phosphoglycerate synthase"
FT /id="PRO_0000420166"
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"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:5JUD"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:5JUD"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:5JUD"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:5JUD"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:5JUD"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:5JUD"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:5JUD"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:5JUD"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:5JUD"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:5JUD"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:5JUD"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 263..280
FT /evidence="ECO:0007829|PDB:5JUD"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:5JUD"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:5JUD"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:5JUD"
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
