ID G8RUH9_MYCRN Unreviewed; 320 AA.
AC G8RUH9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000256|ARBA:ARBA00040894};
DE EC=2.4.1.266 {ECO:0000256|ARBA:ARBA00039022};
GN OrderedLocusNames=MycrhN_3678 {ECO:0000313|EMBL:AEV74196.1};
OS Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV74196.1, ECO:0000313|Proteomes:UP000005442};
RN [1] {ECO:0000313|EMBL:AEV74196.1, ECO:0000313|Proteomes:UP000005442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB3 {ECO:0000313|EMBL:AEV74196.1,
RC ECO:0000313|Proteomes:UP000005442};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL Submitted (DEC-2011) 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; CP003169; AEV74196.1; -; Genomic_DNA.
DR RefSeq; WP_014211952.1; NC_016604.1.
DR AlphaFoldDB; G8RUH9; -.
DR STRING; 710685.MycrhN_3678; -.
DR KEGG; mrh:MycrhN_3678; -.
DR PATRIC; fig|710685.3.peg.3689; -.
DR eggNOG; COG0463; Bacteria.
DR HOGENOM; CLU_053119_0_0_11; -.
DR OrthoDB; 5011697at2; -.
DR Proteomes; UP000005442; Chromosome.
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:UP000005442};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEV74196.1}.
FT DOMAIN 47..154
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
SQ SEQUENCE 320 AA; 34085 MW; BA502C74561D5C3F CRC64;
MTALIEQPTE LVSADIAGHP WLAANSWSRP MWTIAELEAA KAGRTISVVL PALNEEETVA
SVIETITPLL GGLVDELIVL DSGSTDDTEI RALAAGARVI SREVALPEVA PQPGKGEVLW
RSLAVTTGDI VVFVDSDLID PDPMFVPKLL GPLLIGEGVH LVKGFYRRPL KVSGSEDANG
GGRVTELVAR PLLAALRPEL TCLLQPLGGE YAGTRELLTS VPFAPGYGVE IGLLVDTYDR
LGLDAIAQVN LGVREHRNRP LTELAAMSRQ VIATLFSRCG VPDSGVGLTQ FFADGDDFSP
RTSEVSLVDR PPMNSLRPLG
//
