GPGS_MYCS2
ID GPGS_MYCS2 Reviewed; 303 AA.
AC A0R2E6; I7G6T6;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=MSMEG_5084, MSMEI_4958;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND SUBUNIT.
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=19421329; DOI=10.1371/journal.pone.0005447;
RA Kaur D., Pham H., Larrouy-Maumus G., Riviere M., Vissa V., Guerin M.E.,
RA Puzo G., Brennan P.J., Jackson M.;
RT "Initiation of methylglucose lipopolysaccharide biosynthesis in
RT mycobacteria.";
RL PLoS ONE 4:E5447-E5447(2009).
CC -!- FUNCTION: Involved in the biosynthesis of 6-O-methylglucose
CC lipopolysaccarides (MGLPs) (PubMed:18221489, PubMed:19421329).
CC Catalyzes the transfer of the glucose moiety from a nuleotide sugar
CC such as UDP-alpha-D-glucose to the position 2 of 3-phospho-D-glycerate
CC (3-PGA) to form glucosyl-3-phosphoglycerate (GPG). It can use UDP-
CC glucose, ADP-glucose and GDP-glucose as sugar donor substrates with
CC decreasing affinity and with 3-PGA as an acceptor. D-glycerate can only
CC be an acceptor with ADP-glucose and at a very low rate
CC (PubMed:18221489). {ECO:0000269|PubMed:18221489,
CC ECO:0000269|PubMed:19421329}.
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 at 20 mM of MgCl(2). {ECO:0000269|PubMed:18221489};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.24 mM for 3-PGA (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18221489};
CC KM=1.28 mM for UDP-glucose (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18221489};
CC KM=6.08 mM for ADP-glucose (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18221489};
CC KM=32.04 mM for GDP-glucose (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18221489};
CC Vmax=2.45 umol/min/mg enzyme towards GDP-glucose
CC {ECO:0000269|PubMed:18221489};
CC Vmax=25.91 umol/min/mg enzyme towards 3-PGA
CC {ECO:0000269|PubMed:18221489};
CC Vmax=26.23 umol/min/mg enzyme towards ADP-glucose
CC {ECO:0000269|PubMed:18221489};
CC Vmax=27.51 umol/min/mg enzyme towards UDP-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 -!- DISRUPTION PHENOTYPE: Disruption reduces growth rate and results in an
CC 80% decrease in the production of methylglucose lipopolysaccharides
CC (MGLPs) directly attributable to a drastic if not complete loss of GPG
CC synthesis. {ECO:0000269|PubMed:19421329}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP41402.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK73566.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41402.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003896491.1; NC_018289.1.
DR RefSeq; YP_889334.1; NC_008596.1.
DR AlphaFoldDB; A0R2E6; -.
DR SMR; A0R2E6; -.
DR STRING; 246196.MSMEI_4958; -.
DR CAZy; GT81; Glycosyltransferase Family 81.
DR EnsemblBacteria; ABK73566; ABK73566; MSMEG_5084.
DR EnsemblBacteria; AFP41402; AFP41402; MSMEI_4958.
DR GeneID; 66736404; -.
DR KEGG; msg:MSMEI_4958; -.
DR KEGG; msm:MSMEG_5084; -.
DR PATRIC; fig|246196.19.peg.4962; -.
DR eggNOG; COG0463; Bacteria.
DR OMA; HLVKSFY; -.
DR BRENDA; 2.4.1.266; 3512.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 Glycosyltransferase; Magnesium; Manganese; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..303
FT /note="Glucosyl-3-phosphoglycerate synthase"
FT /id="PRO_0000420165"
FT BINDING 35..39
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 66
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 99
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 119..120
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 121
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 166..169
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 211..214
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 238..243
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 240
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 242
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
SQ SEQUENCE 303 AA; 32304 MW; 405C56639EF26854 CRC64;
MGHRWLTDHS WNRPSWTVAD LEAAKAGRTV SVVLPALNEE ETVGSVVETI KPLLGGLVDE
LIVLDSGSTD ETEIRAVAAG AKVVSREAAL PEVPPQPGKG EVLWRSLAAT TGDIIAFVDS
DLIDPDPMFV PKLLGPLLTC DGVHLVKGFY RRPLKVSGAE DANGGGRVTE LVARPLLASL
RPELNCVLQP LGGEYAGTRE LLTSVPFAPG YGVEIGLLVD TYDRLGLDGI AQVNLGVRAH
RNRPLTELAS MSRQVIATLL SRCGISDSGV GLTQFFADGD DFTPRVSSVS LADRPPMTTL
RPR
