ID   MPGS_PYRAB              Reviewed;         394 AA.
AC   Q9UZC1; G8ZKM5;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Mannosyl-3-phosphoglycerate synthase;
DE            Short=MPG synthase;
DE            Short=MPGS;
DE            EC=2.4.1.217;
GN   Name=mngA; OrderedLocusNames=PYRAB12270; ORFNames=PAB0816;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248286; CAB50138.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70668.1; -; Genomic_DNA.
DR   PIR; E75104; E75104.
DR   RefSeq; WP_010868345.1; NC_000868.1.
DR   AlphaFoldDB; Q9UZC1; -.
DR   SMR; Q9UZC1; -.
DR   STRING; 272844.PAB0816; -.
DR   CAZy; GT55; Glycosyltransferase Family 55.
DR   EnsemblBacteria; CAB50138; CAB50138; PAB0816.
DR   GeneID; 1496614; -.
DR   KEGG; pab:PAB0816; -.
DR   PATRIC; fig|272844.11.peg.1311; -.
DR   eggNOG; arCOG04158; Archaea.
DR   HOGENOM; CLU_028916_0_0_2; -.
DR   OMA; MVRLHWR; -.
DR   OrthoDB; 22332at2157; -.
DR   PhylomeDB; Q9UZC1; -.
DR   UniPathway; UPA00130; UER00192.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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; Transferase.
FT   CHAIN           1..394
FT                   /note="Mannosyl-3-phosphoglycerate synthase"
FT                   /id="PRO_0000059285"
SQ   SEQUENCE   394 AA;  45288 MW;  298B760B56B9145D CRC64;
     MLLEAPVYKE IFGAVTIHEV QKVIKMDTET EDVPVYTISN IPREKIYNLL GKMAIIVPMK
     NEKLHLVDGV LKAIPHKCPI IIVSNSKREG PNRYKLEVDL VRHFYNLTHS KVIMIHQKDP
     GLAKAFKEVG YTDILDGKGK VRSGKGEGMI IGMLLAKAIG AEYIGFVDAD NYIPGSVNEY
     VKDYAAGFLM SESDYTMVRL HWRHKPKVTK GTLYFKKWGR VSEITNHYLN LLISEHTAFE
     TTIMVTGNAG EHAMTMKLAE IMPFSTGYSV EPYEIVYLLE RFGKWENVDE FKEVFDQGIE
     IFQIETLNPH FHEDKGQEHV KEMLLLSLAT IYHSKLATNS LKKKILNDLR EHKILKENEE
     PPKPLVMRPI KEIPIKEWME IVEDNSETLL RFEL