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Database: UniProt
Entry: A0A0G3GYA9_9CORY
LinkDB: A0A0G3GYA9_9CORY
Original site: A0A0G3GYA9_9CORY 
ID   A0A0G3GYA9_9CORY        Unreviewed;       252 AA.
AC   A0A0G3GYA9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000256|ARBA:ARBA00040894};
DE            EC=2.4.1.266 {ECO:0000256|ARBA:ARBA00039022};
GN   Name=gpgS {ECO:0000313|EMBL:AKK05545.1};
GN   ORFNames=CMUST_06045 {ECO:0000313|EMBL:AKK05545.1};
OS   Corynebacterium mustelae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=571915 {ECO:0000313|EMBL:AKK05545.1, ECO:0000313|Proteomes:UP000035199};
RN   [1] {ECO:0000313|EMBL:AKK05545.1, ECO:0000313|Proteomes:UP000035199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45274 {ECO:0000313|EMBL:AKK05545.1,
RC   ECO:0000313|Proteomes:UP000035199};
RX   PubMed=26358597;
RA   Ruckert C., Eimer J., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of the Type Strain Corynebacterium mustelae DSM
RT   45274, Isolated from Various Tissues of a Male Ferret with Lethal Sepsis.";
RL   Genome Announc. 3:e01012-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000035199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45274 {ECO:0000313|Proteomes:UP000035199};
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete genome sequence of Corynebacterium mustelae DSM 45274, isolated
RT   from various tissues of a male ferret with lethal sepsis.";
RL   Submitted (MAY-2015) 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; CP011542; AKK05545.1; -; Genomic_DNA.
DR   RefSeq; WP_047261734.1; NZ_CP011542.1.
DR   AlphaFoldDB; A0A0G3GYA9; -.
DR   STRING; 571915.CMUST_06045; -.
DR   KEGG; cmv:CMUST_06045; -.
DR   PATRIC; fig|571915.4.peg.1286; -.
DR   OrthoDB; 5011697at2; -.
DR   Proteomes; UP000035199; Chromosome.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd04179; DPM_DPG-synthase_like; 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   ECO:0000313|EMBL:AKK05545.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035199};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AKK05545.1}.
FT   DOMAIN          6..132
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
SQ   SEQUENCE   252 AA;  26989 MW;  6A0DD5262418AA79 CRC64;
     MNPSISVVIP ALNEEATIAK VITAIRANAP ANLIEILVID ADSHDATAQR AVEAGATVYN
     WRKILPTIDV HPGKGESLWR GVAAAKGDII VFIDADLNHV PPKIVEKLTA PYKNPEIALV
     KADYTRSFGS TPTGGGRVTE LCAKPLLRAL FPELCFINQP LGGEYAIRRS VATNLPFVGG
     YGVEIGLLID VAHTHGTQAI TQVPLGIRSH RNRPLEQLGP MAEVVATAIL TRAGCRTQSQ
     VFQRPALKSL SN
//
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