ID J1Z2P0_9NOCA Unreviewed; 316 AA.
AC J1Z2P0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000256|ARBA:ARBA00040894};
DE EC=2.4.1.266 {ECO:0000256|ARBA:ARBA00039022};
GN ORFNames=JVH1_7610 {ECO:0000313|EMBL:EJI95025.1};
OS Rhodococcus sp. JVH1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=745408 {ECO:0000313|EMBL:EJI95025.1, ECO:0000313|Proteomes:UP000009024};
RN [1] {ECO:0000313|EMBL:EJI95025.1, ECO:0000313|Proteomes:UP000009024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JVH1 {ECO:0000313|EMBL:EJI95025.1,
RC ECO:0000313|Proteomes:UP000009024};
RX PubMed=22965106; DOI=10.1128/JB.01066-12;
RA Brooks S.L., Van Hamme J.D.;
RT "Whole-Genome Shotgun Sequence of Rhodococcus Species Strain JVH1.";
RL J. Bacteriol. 194:5492-5493(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + UDP-alpha-D-glucose = (2R)-2-O-
CC (alpha-D-glucopyranosyl)-3-phospho-glycerate + H(+) + UDP;
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:ARBA00036914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31320;
CC Evidence={ECO:0000256|ARBA:ARBA00036914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + an NDP-alpha-D-glucose = (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:ARBA00035799};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47245;
CC Evidence={ECO:0000256|ARBA:ARBA00035799};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJI95025.1}.
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DR EMBL; AKKP01000108; EJI95025.1; -; Genomic_DNA.
DR AlphaFoldDB; J1Z2P0; -.
DR PATRIC; fig|745408.3.peg.7220; -.
DR Proteomes; UP000009024; Unassembled WGS sequence.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR48090:SF9; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJI95025.1}.
FT DOMAIN 45..153
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
SQ SEQUENCE 316 AA; 33496 MW; E62D020667485802 CRC64;
MGARAARTMV AEERTPRSWA EANSWDQPSW SIAELERAKA GRTVSVVLPA LNEEETVAAV
VDTIHPLLGG LVDELIVLDS GSTDLTAERA RAAGATVISR EEAVPAFPPV AGKGEVLWRS
VAASTGDLIA FVDSDLINPD PAFVPKLLGP LLTADGIHLV KGYYRRPLRL SGTEDANGGG
RVTELVARPM LASLRPELTC VLQPLGGEYA GTRELLSAVP FAPGYGVEIG LLLDTYDRLG
LGAIGQVNLG VRKHRNRPLS ELGVMSRQII GTMMRRCGVP DSGAGLTQFL VDGDSFVPTT
TDVALADRPP MNTVCP
//
