GPGS_METBU
ID GPGS_METBU Reviewed; 404 AA.
AC Q12XX4;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000303|PubMed:16428406};
DE Short=GpgS {ECO:0000305};
DE EC=2.4.1.266 {ECO:0000269|PubMed:16428406};
GN Name=gpgS {ECO:0000303|PubMed:16428406}; OrderedLocusNames=Mbur_0737;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=16428406; DOI=10.1128/jb.188.3.1022-1030.2006;
RA Costa J., Empadinhas N., Goncalves L., Lamosa P., Santos H., da Costa M.S.;
RT "Characterization of the biosynthetic pathway of glucosylglycerate in the
RT archaeon Methanococcoides burtonii.";
RL J. Bacteriol. 188:1022-1030(2006).
CC -!- FUNCTION: Involved in the biosynthesis of 6-O-methylglucose
CC lipopolysaccarides (MGLPs). Catalyzes the transfer of a glucose (Glc)
CC moiety from uridine diphosphate (UDP-Glc) to the position 2 of 3-
CC phospho-D-glycerate (3-PGA) to form glucosyl-3-phosphoglycerate (GPG).
CC {ECO:0000269|PubMed:16428406}.
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:16428406};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16428406};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:16428406};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16428406};
CC Note=Requires divalent cations for activity in the following order of
CC efficiency: Mn(2+), Co(2+) and Mg(2+) ions.
CC {ECO:0000269|PubMed:16428406};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.54 mM for 3-PGA (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:16428406};
CC KM=1.60 mM for 3-PGA (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:16428406};
CC KM=1.75 mM for GDP-glucose (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:16428406};
CC KM=3.70 mM for GDP-glucose (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:16428406};
CC pH dependence:
CC Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:16428406};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:16428406};
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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; CP000300; ABE51702.1; -; Genomic_DNA.
DR RefSeq; WP_011498860.1; NC_007955.1.
DR AlphaFoldDB; Q12XX4; -.
DR CAZy; GT81; Glycosyltransferase Family 81.
DR EnsemblBacteria; ABE51702; ABE51702; Mbur_0737.
DR GeneID; 3996641; -.
DR KEGG; mbu:Mbur_0737; -.
DR HOGENOM; CLU_056498_0_0_2; -.
DR OMA; GKGWAVW; -.
DR OrthoDB; 14967at2157; -.
DR BRENDA; 2.4.1.266; 9200.
DR Proteomes; UP000001979; 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; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cobalt; Glycosyltransferase; Magnesium; Manganese; Metal-binding; Nickel;
KW Reference proteome; Transferase.
FT CHAIN 1..404
FT /note="Glucosyl-3-phosphoglycerate synthase"
FT /id="PRO_0000420167"
FT BINDING 146
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 188..190
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 270
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
SQ SEQUENCE 404 AA; 46878 MW; 9C5AD32B1C1DB363 CRC64;
MDFYQEYITT IHDFCIDKEQ LVKRIEGLKV SRPASLIIPI LYKEVENPPL KKIITDLNEC
TYLSQVVIAL AAETTEQYVH VVEYFKDLKL PHIVVWCDGP RIKQIIFDMK KKGIDLTSFK
GKGKDVWIAT GIATLESYAI AYHDADIVTY SVDLPAKLLY PIVETELNFF FNKGYYARIN
LDSMTMHGRV FRLFVRPLLD TLQSESNADI LRYFLAFRYT LAGEFAMTSD LAMNIRIPAD
WGLEVGLLAE VYRNATTKKI CQIDLGYYDH KHQELGVNRS EGLCKMVSDI FTTFMRVVTE
STDNRISESY LHGIHVRYKR LGQDLIRRYH ADALCNGLYY NRHEEEIYVD MFARVIRKAG
DDYRHDPSDV LMPDWTRALS AVPDLREKLY EACIADVKEY CEKK
