MPGS_PYRHO
ID MPGS_PYRHO Reviewed; 394 AA.
AC O58689;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Mannosyl-3-phosphoglycerate synthase;
DE Short=MPG synthase;
DE Short=MPGS;
DE EC=2.4.1.217;
GN Name=mngA; OrderedLocusNames=PH0927;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=11562374; DOI=10.1074/jbc.m108054200;
RA Empadinhas N., Marugg J.D., Borges N., Santos H., da Costa M.S.;
RT "Pathway for the synthesis of mannosylglycerate in the hyperthermophilic
RT archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of
RT key enzymes.";
RL J. Biol. Chem. 276:43580-43588(2001).
CC -!- FUNCTION: Transfers a mannosyl group from GDP-mannose to
CC phosphoglycerate to form mannosyl-3-phosphoglycerate (MPG). The enzyme
CC is absolutely specific for GDP-mannose and 3-phosphoglycerate, and
CC transfers the mannosyl group with retention of configuration.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
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.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; BA000001; BAA30023.1; -; Genomic_DNA.
DR PIR; A71083; A71083.
DR RefSeq; WP_010885017.1; NC_000961.1.
DR PDB; 2ZU7; X-ray; 2.50 A; A/B=1-394.
DR PDB; 2ZU8; X-ray; 2.40 A; A/B=1-394.
DR PDB; 2ZU9; X-ray; 2.00 A; A/B=1-394.
DR PDBsum; 2ZU7; -.
DR PDBsum; 2ZU8; -.
DR PDBsum; 2ZU9; -.
DR AlphaFoldDB; O58689; -.
DR SMR; O58689; -.
DR STRING; 70601.3257340; -.
DR CAZy; GT55; Glycosyltransferase Family 55.
DR EnsemblBacteria; BAA30023; BAA30023; BAA30023.
DR GeneID; 1443252; -.
DR KEGG; pho:PH0927; -.
DR eggNOG; arCOG04158; Archaea.
DR OMA; MVRLHWR; -.
DR OrthoDB; 22332at2157; -.
DR BioCyc; MetaCyc:MON-13380; -.
DR SABIO-RK; O58689; -.
DR UniPathway; UPA00130; UER00192.
DR EvolutionaryTrace; O58689; -.
DR Proteomes; UP000000752; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycosyltransferase; Magnesium; Transferase.
FT CHAIN 1..394
FT /note="Mannosyl-3-phosphoglycerate synthase"
FT /id="PRO_0000059287"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:2ZU9"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:2ZU9"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2ZU9"
FT HELIX 93..108
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2ZU9"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2ZU9"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:2ZU9"
FT HELIX 174..190
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:2ZU9"
FT HELIX 221..237
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:2ZU9"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:2ZU9"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:2ZU9"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2ZU8"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:2ZU9"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:2ZU9"
FT HELIX 317..332
FT /evidence="ECO:0007829|PDB:2ZU9"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:2ZU8"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:2ZU9"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:2ZU9"
SQ SEQUENCE 394 AA; 45210 MW; 6C2FB4141D2CC807 CRC64;
MLLEAPVYKE IFGAVTIHEV QKVIKMDTET EEVPIYTISN IPREKIYDLL GKMAVIVPMK
NEKLHLVDGV LKAIPHKCPI IIVSNSKREG PNRYKLEVDL IRHFYNLTHS KIIMIHQKDP
GLAKAFKEVG YTDILDENGM IRSGKGEGML VGLLLAKAIG AEYVGFVDAD NYIPGAVNEY
VKDYAAGFLM SESEYTMVRL HWRHKPKVTK GTLYFKKWGR VSEITNHYLN LLVSEHTAFE
TTIMVTGNAG EHAMTMKLAE ILPFSTGYSI EPYEIVYILE RFGKWENVEE FKDVFDQGIE
IFQIETLNPH FHEDKGKEHV KEMLLLSLAT IYHSKLATDN LRKRILKDLR DHGILGENEE
PPKPLVMRPI KEIPIKEWMD IVEGNSETLL RFEL
