ID   MGGS_PETMO              Reviewed;         430 AA.
AC   A9BFS6;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Mannosylglucosylglycerate synthase {ECO:0000303|PubMed:20061481};
DE            EC=2.4.1.- {ECO:0000250|UniProtKB:Q9X0V7};
GN   Name=mggS {ECO:0000303|PubMed:20061481};
GN   OrderedLocusNames=Pmob_0697 {ECO:0000312|EMBL:ABX31422.1};
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   PROBABLE FUNCTION, AND GENE NAME.
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 mannosylglucosylglycerate (MGG) from
CC       glucosylglycerate (GG) and GDP-mannose. {ECO:0000303|PubMed:20061481}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + GDP-alpha-D-
CC         mannose = (2R)-2-O-[alpha-D-mannopyranosyl-(1->2)-alpha-D-
CC         glucopyranosyl]-glycerate + GDP + H(+); Xref=Rhea:RHEA:47728,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:62510, ChEBI:CHEBI:87836;
CC         Evidence={ECO:0000250|UniProtKB:Q9X0V7};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:Q9X0V7};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000305}.
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DR   EMBL; CP000879; ABX31422.1; -; Genomic_DNA.
DR   RefSeq; WP_012208525.1; NC_010003.1.
DR   AlphaFoldDB; A9BFS6; -.
DR   STRING; 403833.Pmob_0697; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   EnsemblBacteria; ABX31422; ABX31422; Pmob_0697.
DR   KEGG; pmo:Pmob_0697; -.
DR   eggNOG; COG0438; Bacteria.
DR   HOGENOM; CLU_645170_0_0_0; -.
DR   OMA; VNRYSIF; -.
DR   Proteomes; UP000000789; Chromosome.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..430
FT                   /note="Mannosylglucosylglycerate synthase"
FT                   /id="PRO_0000431557"
SQ   SEQUENCE   430 AA;  50510 MW;  8CBF7EBC54B36C5B CRC64;
     MEIGLVHYRV GETDGVSLEM VKWKQALRNM HLKTYLIAGD MGTSPGFKIP YIAYTDKRSN
     ILKQKSFVNL DEWDENYFKK EMNKYIEDIY NQLYEMMDLD VMIVNNIFSL AHNPAAAVAI
     YRFCKDNGIK MIGHHHDFYW ERDFYKNPTN DYIKEILEEY FPPKDITHVV INSLAQEELK
     NKKGLDSIVI PNVFDFNQKR WEIDDYNIKI YDKLNISQKD LIFLQATRIV RRKAIELAID
     TVAEVKKDLK KYIGKTTFNG KKITQDTNVF LVLPGLSEES DYVEVLKEYA SQKDVELKLA
     FSISDDIRHE EEEIFSLWDF YAIADFITYP SILEGFGNQF LEAIFAKTPV LMFEYPVYKK
     DIAPLGFEVV SLGSKAEYER GMYRVNQNEI IKAKEEIFQI LFDPQGLHRL SRRILNLGKN
     IFPMKLWRKS