ID A0A1E5PU58_9ACTN Unreviewed; 316 AA.
AC A0A1E5PU58;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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=BGK67_18695 {ECO:0000313|EMBL:OEJ33079.1};
OS Streptomyces subrutilus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36818 {ECO:0000313|EMBL:OEJ33079.1, ECO:0000313|Proteomes:UP000095705};
RN [1] {ECO:0000313|EMBL:OEJ33079.1, ECO:0000313|Proteomes:UP000095705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-1-1 {ECO:0000313|EMBL:OEJ33079.1,
RC ECO:0000313|Proteomes:UP000095705};
RA Chen X.;
RT "The complete genome of Streptomyces subrutilus 10-1-1.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:OEJ33079.1}.
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DR EMBL; MEHK01000001; OEJ33079.1; -; Genomic_DNA.
DR RefSeq; WP_069921329.1; NZ_MEHK01000001.1.
DR AlphaFoldDB; A0A1E5PU58; -.
DR STRING; 36818.BGK67_18695; -.
DR OrthoDB; 5011697at2; -.
DR Proteomes; UP000095705; 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 Reference proteome {ECO:0000313|Proteomes:UP000095705};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 36..147
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT REGION 290..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 316 AA; 34614 MW; BE5FD23D002C9683 CRC64;
MLEEVERWLA ARSWSAADRP LDQLLDRKRA AGTTVSVVLP ALDEEATVGA IVEVIRRELI
EGLPVPLVDE LVVIDSGSSD ATAEVAAKAG ARVVHRDDIL PRIPALPGKG EVLWRSLLAT
TGDVVCFVDA DLRDFSAAFV HGIVGPLLTE PDVQFVKAMY DRPLDGAPGQ GGRVTELVAR
PLLNLHWPQL AGFVQPLGGE YAVRRSLLER LPFPVGYGVE LGLLVDALHT VGLDALAQVD
VGVRHHRHQD GQALGRMAAA IYRTAQLRLS RGHLVRPRLT QFERGPEGFV PRTYPVDTEE
RPPMREVEEY ARRRAA
//
