GPGS_PETMO
ID GPGS_PETMO Reviewed; 325 AA.
AC A9BHI9;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000303|PubMed:20061481};
DE Short=GpgS {ECO:0000305};
DE EC=2.4.1.266 {ECO:0000269|PubMed:20061481};
GN Name=gpgS {ECO:0000303|PubMed:20061481};
GN OrderedLocusNames=Pmob_1142 {ECO:0000312|EMBL:ABX31861.1};
OS Petrotoga mobilis (strain DSM 10674 / SJ95).
OC Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Petrotoga.
OX NCBI_TaxID=403833;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10674 / SJ95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Noll K., Richardson P.;
RT "Complete sequence of Petroga mobilis SJ95.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=DSM 10674 / SJ95;
RX PubMed=20061481; DOI=10.1128/jb.01424-09;
RA Fernandes C., Mendes V., Costa J., Empadinhas N., Jorge C., Lamosa P.,
RA Santos H., da Costa M.S.;
RT "Two alternative pathways for the synthesis of the rare compatible solute
RT mannosylglucosylglycerate in Petrotoga mobilis.";
RL J. Bacteriol. 192:1624-1633(2010).
CC -!- FUNCTION: Involved in the biosynthesis of the compatible solute
CC mannosylglucosylglycerate through a phosphorylating pathway. Catalyzes
CC the transfer of the glucose moiety from a nuleotide sugar such as UDP-
CC alpha-D-glucose to the position 2 of 3-phospho-D-glycerate (3-PGA) to
CC form glucosyl-3-phosphoglycerate (GPG). UDP-glucose is the preferred
CC substrate, but it can be partially replaced by ADP-glucose.
CC {ECO:0000269|PubMed:20061481}.
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:20061481};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47245;
CC Evidence={ECO:0000305|PubMed:20061481};
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:20061481};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31320;
CC Evidence={ECO:0000305|PubMed:20061481};
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:20061481};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31312;
CC Evidence={ECO:0000305|PubMed:20061481};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:20061481};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20061481};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20061481};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:20061481};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:20061481};
CC Note=Requires divalent cations for activity.
CC {ECO:0000269|PubMed:20061481};
CC -!- ACTIVITY REGULATION: Inhibited by ADP and EDTA.
CC {ECO:0000269|PubMed:20061481}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for 3-PGA (at 60 degrees Celsius)
CC {ECO:0000269|PubMed:20061481};
CC KM=0.5 mM for 3-PGA (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:20061481};
CC KM=1.0 mM for UDP-glucose (at 60 degrees Celsius)
CC {ECO:0000269|PubMed:20061481};
CC KM=0.9 mM for UDP-glucose (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:20061481};
CC Vmax=43.9 umol/min/mg enzyme toward 3-PGA (at 60 degrees Celsius)
CC {ECO:0000269|PubMed:20061481};
CC Vmax=65.0 umol/min/mg enzyme toward 3-PGA (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:20061481};
CC Vmax=44.0 umol/min/mg enzyme toward UDP-glucose (at 60 degrees
CC Celsius) {ECO:0000269|PubMed:20061481};
CC Vmax=49.5 umol/min/mg enzyme toward UDP-glucose (at 70 degrees
CC Celsius) {ECO:0000269|PubMed:20061481};
CC pH dependence:
CC Optimum pH is 7.0 (at 60 degrees Celsius).
CC {ECO:0000269|PubMed:20061481};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:20061481};
CC -!- SUBUNIT: Homodimer in solution. {ECO:0000269|PubMed:20061481}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; CP000879; ABX31861.1; -; Genomic_DNA.
DR RefSeq; WP_012208962.1; NC_010003.1.
DR AlphaFoldDB; A9BHI9; -.
DR SMR; A9BHI9; -.
DR STRING; 403833.Pmob_1142; -.
DR CAZy; GT81; Glycosyltransferase Family 81.
DR EnsemblBacteria; ABX31861; ABX31861; Pmob_1142.
DR KEGG; pmo:Pmob_1142; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_053119_0_0_0; -.
DR OMA; HLVKSFY; -.
DR OrthoDB; 1064289at2; -.
DR BioCyc; MetaCyc:MON-16143; -.
DR BRENDA; 2.4.1.266; 11874.
DR Proteomes; UP000000789; 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 Cobalt; Glycosyltransferase; Magnesium; Manganese; Metal-binding; Nickel;
KW Transferase; Zinc.
FT CHAIN 1..325
FT /note="Glucosyl-3-phosphoglycerate synthase"
FT /id="PRO_0000431554"
FT BINDING 37..41
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 71
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 104
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 124..125
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 171..174
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 216..219
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 243..248
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 245
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 247
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
SQ SEQUENCE 325 AA; 37133 MW; 5EF167CEFF7E709C CRC64;
MKDNILKRSF HHSKFENIKE LVKLKEKQDV KISLAFPSLN EEKTIGKEII IMKSELMEKY
PLLDEIAVID SGSEDETVSI AKEYGAKVFY SSDILPEYGF YKGKGENLWK SLYALDGDII
VWVDSDIENI HPKFVYGLVG ALLNYPEIGY VKAFYDRPIV GKSAMQPTGG GRVTELVARP
LFSLFYPELS TIIQPLSGEY AGRREILEKL PFFVGYGVEI AHLIDIAEKF GSEIIAQVDL
ELRIHDNQPL HSLSKMAFEL TKVVLKRLEK YGKLDLNTEL TDKHIMIQKK ENEKVLVPTE
ILSVERPPMI TIPEYKEKFS KEEKV
