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Database: UniProt
Entry: A0A1I5WI74_9PSEU
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ID   A0A1I5WI74_9PSEU        Unreviewed;       312 AA.
AC   A0A1I5WI74;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000256|ARBA:ARBA00040894};
DE            EC=2.4.1.266 {ECO:0000256|ARBA:ARBA00039022};
GN   ORFNames=SAMN05421810_105119 {ECO:0000313|EMBL:SFQ19331.1};
OS   Amycolatopsis arida.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=587909 {ECO:0000313|EMBL:SFQ19331.1, ECO:0000313|Proteomes:UP000198727};
RN   [1] {ECO:0000313|Proteomes:UP000198727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5579 {ECO:0000313|Proteomes:UP000198727};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOWW01000005; SFQ19331.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5WI74; -.
DR   STRING; 587909.SAMN05421810_105119; -.
DR   Proteomes; UP000198727; Unassembled WGS sequence.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd00761; Glyco_tranf_GTA_type; 1.
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:UP000198727};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          34..144
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
SQ   SEQUENCE   312 AA;  33210 MW;  63D5B342DC580E9C CRC64;
     MTPEISDWFA RRTWQAPRWT AGELCAAKRG RTVSVVLPAL DEEHTVAGVV GSVRPLLGSL
     VDELVVMDSG STDGTVAAAT TAGARVVRRE DVLPDLAPRP GKGEVLWRSL AATRGDLVVF
     LDSDLVDPDP AFVPTLLGPL LTEPGVHLVK GFYRRPLRLE TAEQGTGGGR VTELLARPVL
     GALRPELAGL VQPLGGEYAA SRELLESVPF APGYGVEIGL LLDTERRFGL AALAQVNLGV
     RKHRNRSLLQ LGVMARQILG TALARCGVDT PGPAALTQFV QVAGEWLPDT TDVEVADRPP
     MHEVLAARGP GR
//
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