ID   MPGS_PYRFU              Reviewed;         394 AA.
AC   Q8U380;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Mannosyl-3-phosphoglycerate synthase;
DE            Short=MPG synthase;
DE            Short=MPGS;
DE            EC=2.4.1.217;
GN   Name=mngA; OrderedLocusNames=PF0591;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
CC   -!- FUNCTION: Transfers a mannosyl group from GDP-mannose to
CC       phosphoglycerate to form mannosyl-3-phosphoglycerate (MPG).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + GDP-alpha-D-mannose = 2-O-(alpha-D-
CC         mannosyl)-3-phosphoglycerate + GDP + H(+); Xref=Rhea:RHEA:13537,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:57744,
CC         ChEBI:CHEBI:58189, ChEBI:CHEBI:58272; EC=2.4.1.217;
CC   -!- PATHWAY: Carbohydrate biosynthesis; 2-(alpha-D-mannosyl)-D-glycerate
CC       biosynthesis; 2-(alpha-D-mannosyl)-D-glycerate from GDP-alpha-D-mannose
CC       (MPG route): step 1/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; AE009950; AAL80715.1; -; Genomic_DNA.
DR   RefSeq; WP_011011710.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U380; -.
DR   SMR; Q8U380; -.
DR   STRING; 186497.PF0591; -.
DR   CAZy; GT55; Glycosyltransferase Family 55.
DR   EnsemblBacteria; AAL80715; AAL80715; PF0591.
DR   GeneID; 41712396; -.
DR   KEGG; pfu:PF0591; -.
DR   PATRIC; fig|186497.12.peg.620; -.
DR   eggNOG; arCOG04158; Archaea.
DR   HOGENOM; CLU_028916_0_0_2; -.
DR   OMA; MVRLHWR; -.
DR   OrthoDB; 22332at2157; -.
DR   PhylomeDB; Q8U380; -.
DR   UniPathway; UPA00130; UER00192.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050504; F:mannosyl-3-phosphoglycerate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051479; P:mannosylglycerate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR012812; Osmo_MPG_synth.
DR   Pfam; PF09488; Osmo_MPGsynth; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR02460; osmo_MPGsynth; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..394
FT                   /note="Mannosyl-3-phosphoglycerate synthase"
FT                   /id="PRO_0000059286"
SQ   SEQUENCE   394 AA;  45426 MW;  259598FEE665ED25 CRC64;
     MLLEAPVYKE IFGAVKIYEL QKVIKLDTET EDVPVYTITN IPREKIYDTL GKMAVIVPMK
     NEKLHLVDGV LKAIPHKCPI IIVSNSKREG PNRYRLEVDL VRHFYNLTNS KIIMVHQRDP
     GLAKAFQKVG YTDILDEKGN IRSGKGEGML IGILLAKAIG AEYVGFVDAD NYIPGAVNEY
     VKDYAAGFLM SESDYTMVRL HWRHKPKVTK GTLYFKKWGR VSEITNHYLN MLISEQTSFE
     TTIMVTGNAG EHAMTMKLAE IMPFSTNYSI EPYEIVYLLE RFGKWENVEE FKDVFDQGIE
     IFQIETLNPH FHEDKGQEHV REMILLSLAT IYHSKMASKN LKRRILNDLI EHGILKEGEE
     PPKLRIMRPI NEIDIEEWMK VVENNSETLL RFGL