ID   MGGA_PETMO              Reviewed;         505 AA.
AC   A9BHJ0;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Mannosylglucosyl-3-phosphoglycerate synthase {ECO:0000303|PubMed:20061481};
DE            EC=2.4.1.270 {ECO:0000269|PubMed:20061481};
GN   Name=mggA {ECO:0000303|PubMed:20061481};
GN   OrderedLocusNames=Pmob_1143 {ECO:0000312|EMBL:ABX31862.1};
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, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   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 phosphorylating pathway. Catalyzes
CC       the conversion of glucosyl-3-phosphoglycerate (GPG) to
CC       mannosylglucosyl-3-phosphoglycerate (MGPG).
CC       {ECO:0000269|PubMed:20061481}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + GDP-
CC         alpha-D-mannose = (2R)-2-O-[alpha-D-mannopyranosyl-(1->2)-alpha-D-
CC         glucopyranosyl]-3-phospho-glycerate + GDP + H(+);
CC         Xref=Rhea:RHEA:31323, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527,
CC         ChEBI:CHEBI:58189, ChEBI:CHEBI:62600, ChEBI:CHEBI:62602;
CC         EC=2.4.1.270; Evidence={ECO:0000269|PubMed:20061481};
CC   -!- ACTIVITY REGULATION: Not strictly dependent on divalent cations, but
CC       the presence of Mn(2+), Ca(2+), Mg(2+) or Co(2+) stimulates activity.
CC       {ECO:0000269|PubMed:20061481}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.8 mM for glucosyl-3-phosphoglycerate (at 60 degrees Celsius)
CC         {ECO:0000269|PubMed:20061481};
CC         KM=1.0 mM for GDP-mannose (at 60 degrees Celsius)
CC         {ECO:0000269|PubMed:20061481};
CC         Vmax=30.3 umol/min/mg enzyme toward glucosyl-3-phosphoglycerate (at
CC         60 degrees Celsius) {ECO:0000269|PubMed:20061481};
CC         Vmax=37.0 umol/min/mg enzyme toward GDP-mannose (at 60 degrees
CC         Celsius) {ECO:0000269|PubMed:20061481};
CC       pH dependence:
CC         Optimum pH is 9.0 (at 60 degrees Celsius).
CC         {ECO:0000269|PubMed:20061481};
CC       Temperature dependence:
CC         Optimum temperature is 90 degrees Celsius.
CC         {ECO:0000269|PubMed:20061481};
CC   -!- SUBUNIT: Monomer in solution. {ECO:0000269|PubMed:20061481}.
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DR   EMBL; CP000879; ABX31862.1; -; Genomic_DNA.
DR   RefSeq; WP_012208963.1; NC_010003.1.
DR   AlphaFoldDB; A9BHJ0; -.
DR   STRING; 403833.Pmob_1143; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PRIDE; A9BHJ0; -.
DR   EnsemblBacteria; ABX31862; ABX31862; Pmob_1143.
DR   KEGG; pmo:Pmob_1143; -.
DR   eggNOG; COG0438; Bacteria.
DR   HOGENOM; CLU_586268_0_0_0; -.
DR   OrthoDB; 1675290at2; -.
DR   BioCyc; MetaCyc:MON-16132; -.
DR   BRENDA; 2.4.1.270; 11874.
DR   Proteomes; UP000000789; Chromosome.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..505
FT                   /note="Mannosylglucosyl-3-phosphoglycerate synthase"
FT                   /id="PRO_0000431555"
SQ   SEQUENCE   505 AA;  59124 MW;  96EF22DCBE3EB535 CRC64;
     MNNLYIFHYH YIKGGVSTVV RNIVKSLKDA YKITLFGSKK MGIDGIEEVL SYENVDFIDF
     PELGYIYYDS TDYKTFLELK ESIKNKLNNY HDERAIYWAH NYNLGKNPAF TEAFKEFITT
     KNIPTIIQIH DFPECARWEN YSFIRKFINS SLYPIRKNIQ YATINLSDYN RLIKCGIPSE
     NAFYLPNAVE FAKNKDKIDD IDKDEVINKL KKLGYNVDPT NKNILYPTRT IRRKNILEAV
     LINRLYGKSN LLVTLPANSD KERPYEKVVK ETFESEKVKG AWAISAKDPS LFPYILNISD
     LFFSSSVLEG FGMIYLESKF NEKNFLTRKL DVIEDFKNIK EISYYDRFLV SLSPKEINKV
     KEKYEEQINK IPISEENKNH LRQDLNNKFD KDLIDFSFLP VELQKKFCME EEAKLNDLKE
     INKEIFDKIE MLTSTNHIDQ GINLEDFSLK AYKSKIFLLL DKVQARGNAP KGVQGSTKEI
     EDTIIDENIL KSFLTIDNIR LLFSY