ID   B2HS60_MYCMM            Unreviewed;       327 AA.
AC   B2HS60;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   04-NOV-2026, entry version 70.
DE   RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000256|ARBA:ARBA00040894};
DE            EC=2.4.1.266 {ECO:0000256|ARBA:ARBA00039022};
GN   OrderedLocusNames=MMAR_4230 {ECO:0000313|EMBL:ACC42638.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC42638.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC42638.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + UDP-alpha-D-glucose = (2R)-2-O-
CC         (alpha-D-glucopyranosyl)-3-phospho-glycerate + UDP + H(+);
CC         Xref=Rhea:RHEA:31319, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58272, ChEBI:CHEBI:58885, ChEBI:CHEBI:62600;
CC         EC=2.4.1.266; Evidence={ECO:0000256|ARBA:ARBA00048689};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31320;
CC         Evidence={ECO:0000256|ARBA:ARBA00048689};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an NDP-alpha-D-glucose + (2R)-3-phosphoglycerate = (2R)-2-O-
CC         (alpha-D-glucopyranosyl)-3-phospho-glycerate + a ribonucleoside 5'-
CC         diphosphate + H(+); Xref=Rhea:RHEA:47244, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:58272, ChEBI:CHEBI:62600,
CC         ChEBI:CHEBI:76533; EC=2.4.1.266;
CC         Evidence={ECO:0000256|ARBA:ARBA00048997};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47245;
CC         Evidence={ECO:0000256|ARBA:ARBA00048997};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC       {ECO:0000256|ARBA:ARBA00006739}.
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DR   EMBL; CP000854; ACC42638.1; -; Genomic_DNA.
DR   RefSeq; WP_012395800.1; NC_010612.1.
DR   AlphaFoldDB; B2HS60; -.
DR   STRING; 216594.MMAR_4230; -.
DR   GeneID; 34341232; -.
DR   KEGG; mmi:MMAR_4230; -.
DR   eggNOG; COG0463; Bacteria.
DR   HOGENOM; CLU_053119_0_0_11; -.
DR   OMA; AEHRWLT; -.
DR   OrthoDB; 5011697at2; -.
DR   Proteomes; UP000001190; Chromosome.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR050256; Glycosyltransferase_2.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   NCBIfam; NF010496; PRK13915.1; 1.
DR   PANTHER; PTHR48090:SF10; GLUCOSYL-3-PHOSPHOGLYCERATE SYNTHASE; 1.
DR   PANTHER; PTHR48090; UNDECAPRENYL-PHOSPHATE 4-DEOXY-4-FORMAMIDO-L-ARABINOSE TRANSFERASE-RELATED; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001190};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          52..159
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
SQ   SEQUENCE   327 AA;  34692 MW;  6C16A9B13B885546 CRC64;
     MTASDLVTGD LTSEGVLIPA RPGDTWLCDR SWNRPRWKID ELVEAKAGRS ISVVLPALDE
     EETIQSVIDS ISPLVDGLVD ELIVLDSGST DDTEIRAIAA GARVVSREQA LPEVPPQPGK
     GEALWRSLAA TSGDIVVFID SDLVNPNPMF VPWLVGPLLT GEGIHLVKSF YRRPLSVGDA
     SGAAGATGGG RVTELVARPL LAALRPELGC VLQPLSGEYA ASRELLTSLP FAPGYGVEIG
     LLVDTFDRLG LDAIAQVNLG VRAHRNRPLA ELGVMSRQVI ATLLSRCGIP DSGVGLTQFF
     AEGDGYTECT SPVSLADRPP MSVLRPR
//