GPGS_PERMH
ID GPGS_PERMH Reviewed; 403 AA.
AC C0QRQ2;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000303|PubMed:17189358};
DE Short=GpgS {ECO:0000303|PubMed:17189358};
DE EC=2.4.1.266 {ECO:0000269|PubMed:17189358};
GN Name=gpgS {ECO:0000303|PubMed:17189358}; OrderedLocusNames=PERMA_1582;
OS Persephonella marina (strain DSM 14350 / EX-H1).
OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; Persephonella.
OX NCBI_TaxID=123214;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14350 / EX-H1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=17189358; DOI=10.1128/jb.00841-06;
RA Costa J., Empadinhas N., da Costa M.S.;
RT "Glucosylglycerate biosynthesis in the deepest lineage of the Bacteria:
RT characterization of the thermophilic proteins GpgS and GpgP from
RT Persephonella marina.";
RL J. Bacteriol. 189:1648-1654(2007).
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 GpgS is most active with UDP-glucose, followed by GDP-glucose, ADP-
CC glucose, and to a lesser extent, TDP-glucose. 3-PGA is the only
CC acceptor for these glucosyl donors. {ECO:0000269|PubMed:17189358}.
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:17189358};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17189358};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:17189358};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17189358};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:17189358};
CC Note=Requires divalent cations for activity in the following order of
CC efficiency: Mn(2+), Co(2+), Mg(2+) and Ni(2+) ions.
CC {ECO:0000269|PubMed:17189358};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.09 mM for 3-PGA (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17189358};
CC KM=0.25 mM for 3-PGA (at 85 degrees Celsius)
CC {ECO:0000269|PubMed:17189358};
CC KM=0.3 mM for 3-PGA (at 90 degrees Celsius)
CC {ECO:0000269|PubMed:17189358};
CC KM=1.47 mM for UDP-glucose (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17189358};
CC KM=1.55 mM for UDP-glucose (at 85 degrees Celsius)
CC {ECO:0000269|PubMed:17189358};
CC KM=1.58 mM for UDP-glucose (at 90 degrees Celsius)
CC {ECO:0000269|PubMed:17189358};
CC Vmax=51.5 umol/min/mg enzyme with 3-PGA as substrate (at 70 degrees
CC Celsius) {ECO:0000269|PubMed:17189358};
CC Vmax=110 umol/min/mg enzyme with 3-PGA as substrate (at 85 degrees
CC Celsius) {ECO:0000269|PubMed:17189358};
CC Vmax=128 umol/min/mg enzyme with 3-PGA as substrate (at 90 degrees
CC Celsius) {ECO:0000269|PubMed:17189358};
CC Vmax=66 umol/min/mg enzyme with UDP-glucose as substrate (at 70
CC degrees Celsius) {ECO:0000269|PubMed:17189358};
CC Vmax=98 umol/min/mg enzyme with UDP-glucose as substrate (at 85
CC degrees Celsius) {ECO:0000269|PubMed:17189358};
CC Vmax=106 umol/min/mg enzyme with UDP-glucose as substrate (at 90
CC degrees Celsius) {ECO:0000269|PubMed:17189358};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:17189358};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius. GpgS is inactive at 40
CC degrees Celsius, but the activity increases dramatically above 50
CC degrees Celsius. At 100 degrees Celsius, GpgS retains 33% of the
CC total activity. {ECO:0000269|PubMed:17189358};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17189358}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; CP001230; ACO04915.1; -; Genomic_DNA.
DR RefSeq; WP_015899019.1; NC_012440.1.
DR AlphaFoldDB; C0QRQ2; -.
DR SMR; C0QRQ2; -.
DR STRING; 123214.PERMA_1582; -.
DR EnsemblBacteria; ACO04915; ACO04915; PERMA_1582.
DR KEGG; pmx:PERMA_1582; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_056498_0_0_0; -.
DR OMA; GKGWAVW; -.
DR OrthoDB; 1064289at2; -.
DR Proteomes; UP000001366; 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..403
FT /note="Glucosyl-3-phosphoglycerate synthase"
FT /id="PRO_0000420168"
FT BINDING 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 189..192
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT BINDING 273
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
SQ SEQUENCE 403 AA; 46704 MW; 2F98AB0559DAC0A2 CRC64;
MADFFQNGVI TTLQNFRNRS LEELEYELEL FSKRRNMVLL LPALYSEFEG PAMPKIIQEL
KDIRYLYKIV LSLDRATEEE FKKVKKIMSE INTEVKVIWH DGPRMQRLYR ELEEAGFNVS
IPGKGRSVWM SLGYILSDAD AYAIALHDCD IVNYSRELPA RLLYPVVHPA LDFEFSKGYY
ARVTHKLYGR VTRIFYTPLI RALIRILGCN RFLVYLDSFR YALSGEFAFI RTLARGIRIS
PTWGLEVSML SEVYQNTSFN RICQVEVMDT YEHKHQKLVK STSEGLVKMA SDIAKTLFRV
LAHDGFVFSE AFFRTLLTTY LQEARYAIEK YNALSLINGL TYDRHAEIEA IEVFVDALKK
AEKEFIEDPI GVPLMSAWVR VRAALPEISD KLIRAVEEDN SDD
