GGS_PETMO
ID GGS_PETMO Reviewed; 393 AA.
AC A9BEU2;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Glucosylglycerate synthase {ECO:0000303|PubMed:20061481};
DE EC=2.4.1.268 {ECO:0000269|PubMed:20061481};
GN Name=ggs {ECO:0000303|PubMed:20061481};
GN OrderedLocusNames=Pmob_0071 {ECO:0000312|EMBL:ABX30820.1};
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, 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 nonphosphorylating pathway.
CC Catalyzes the synthesis of glucosylglycerate (GG) from ADP-glucose and
CC D-glycerate. Can also use UDP-glucose, with lower efficiency.
CC {ECO:0000269|PubMed:20061481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + ADP-alpha-D-glucose = (2R)-2-O-(alpha-D-
CC glucopyranosyl)-glycerate + ADP + H(+); Xref=Rhea:RHEA:30923,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16659, ChEBI:CHEBI:57498,
CC ChEBI:CHEBI:62510, ChEBI:CHEBI:456216; EC=2.4.1.268;
CC Evidence={ECO:0000269|PubMed:20061481};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20061481};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and Zn(2+).
CC {ECO:0000269|PubMed:20061481}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.9 mM for ADP-glucose (for the native enzyme, at 60 degrees
CC Celsius) {ECO:0000269|PubMed:20061481};
CC KM=2.0 mM for ADP-glucose (for the native enzyme, at 70 degrees
CC Celsius) {ECO:0000269|PubMed:20061481};
CC KM=9.3 mM for ADP-glucose (for the recombinant enzyme, at 60 degrees
CC Celsius) {ECO:0000269|PubMed:20061481};
CC KM=0.9 mM for D-glycerate (for the native enzyme, at 60 degrees
CC Celsius) {ECO:0000269|PubMed:20061481};
CC KM=1.9 mM for D-glycerate (for the native enzyme, at 70 degrees
CC Celsius) {ECO:0000269|PubMed:20061481};
CC KM=3.4 mM for D-glycerate (for the recombinant enzyme, at 60 degrees
CC Celsius) {ECO:0000269|PubMed:20061481};
CC Vmax=5.8 umol/min/mg enzyme (for the recombinant enzyme, at 60
CC degrees 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 70-75 degrees Celsius.
CC {ECO:0000269|PubMed:20061481};
CC -!- SUBUNIT: Homotetramer in solution. {ECO:0000269|PubMed:20061481}.
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; CP000879; ABX30820.1; -; Genomic_DNA.
DR RefSeq; WP_012207927.1; NC_010003.1.
DR AlphaFoldDB; A9BEU2; -.
DR SMR; A9BEU2; -.
DR STRING; 403833.Pmob_0071; -.
DR CAZy; GT81; Glycosyltransferase Family 81.
DR EnsemblBacteria; ABX30820; ABX30820; Pmob_0071.
DR KEGG; pmo:Pmob_0071; -.
DR eggNOG; COG0463; Bacteria.
DR HOGENOM; CLU_052035_0_0_0; -.
DR OMA; IPSYNNA; -.
DR OrthoDB; 550571at2; -.
DR BioCyc; MetaCyc:MON-16142; -.
DR BRENDA; 2.4.1.268; 11874.
DR Proteomes; UP000000789; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; 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; Transferase.
FT CHAIN 1..393
FT /note="Glucosylglycerate synthase"
FT /id="PRO_0000431556"
SQ SEQUENCE 393 AA; 43684 MW; 7D3AB7575B3D2C17 CRC64;
MSIFFDDKIL QNLPKKVKVV VGIPSYNNAE TISFVSKTAA EGIVEYFDSD GIIVNADGGS
KDGTKEVFMK TDTKSVPKIA YDYIGLPGKG SAMLSVIELA KNLDAEAIVF LDSDLKSVRP
WWIERLTGPI MKGLSDYVTP YYVRHKYDGT ITNQVCYPLV SSLFGQAIRQ PIGGDFGVGK
NMIDVYLKAA SSVAKTEVAR FGIDIWMTIN AILNSNKKVY QAALGAKVHD PKDPGADLSP
MFKQVVGTLF DIIVDSASKW KDIGSIEEAP IYGEIPQIAV EPININIENL KMQLLEGLKN
EESKILANDH LGFIMEKKKV PLQIWVDILF NALIEYSKNK DKKLVESLVP LYFGRVADFA
ELTKDMNEVE AEKVIKDQIN LFANKKDELI EKL
