GPGS_MYCPA
ID GPGS_MYCPA Reviewed; 329 AA.
AC Q73WU1;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000303|PubMed:18667419};
DE Short=GpgS {ECO:0000305};
DE EC=2.4.1.266 {ECO:0000269|PubMed:18667419};
GN OrderedLocusNames=MAP_2569c;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
RN [2] {ECO:0007744|PDB:3CKJ, ECO:0007744|PDB:3CKN, ECO:0007744|PDB:3CKO, ECO:0007744|PDB:3CKQ, ECO:0007744|PDB:3CKV}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEXES WITH UDP AND
RP UDP-ALPHA-D-GLUCOSE AND MANGANESE ION, FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, COFACTOR, AND SUBUNIT.
RX PubMed=18667419; DOI=10.1074/jbc.m801853200;
RA Fulton Z., McAlister A., Wilce M.C., Brammananth R., Zaker-Tabrizi L.,
RA Perugini M.A., Bottomley S.P., Coppel R.L., Crellin P.K., Rossjohn J.,
RA Beddoe T.;
RT "Crystal structure of a UDP-glucose-specific glycosyltransferase from a
RT Mycobacterium species.";
RL J. Biol. Chem. 283:27881-27890(2008).
CC -!- FUNCTION: Involved in the biosynthesis of 6-O-methylglucose
CC lipopolysaccarides (MGLPs). Catalyzes the transfer of the glucose
CC moiety from UDP-alpha-D-glucose (UDP-Glc) to the position 2 of 3-
CC phospho-D-glycerate (3-PGA) to form glucosyl-3-phosphoglycerate (GPG).
CC To a lesser extent can also use GDP-Glc but not UDP-Gal or UDP-GlcNAc
CC as the sugar donor. {ECO:0000269|PubMed:18667419}.
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:0000269|PubMed:18667419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47245;
CC Evidence={ECO:0000305|PubMed:18667419};
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:0000269|PubMed:18667419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31320;
CC Evidence={ECO:0000305|PubMed:18667419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + GDP-D-glucose = (2R)-2-O-(alpha-D-
CC glucopyranosyl)-3-phospho-glycerate + GDP + H(+);
CC Xref=Rhea:RHEA:31315, ChEBI:CHEBI:15378, ChEBI:CHEBI:58127,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:58272, ChEBI:CHEBI:62600;
CC EC=2.4.1.266; Evidence={ECO:0000269|PubMed:18667419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31316;
CC Evidence={ECO:0000305|PubMed:18667419};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:18667419};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:18667419};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18667419}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016958; AAS04886.1; -; Genomic_DNA.
DR RefSeq; WP_003878473.1; NC_002944.2.
DR PDB; 3CKJ; X-ray; 1.80 A; A=1-329.
DR PDB; 3CKN; X-ray; 2.20 A; A=1-329.
DR PDB; 3CKO; X-ray; 2.50 A; A=1-329.
DR PDB; 3CKQ; X-ray; 3.00 A; A=1-329.
DR PDB; 3CKV; X-ray; 2.00 A; A=1-329.
DR PDBsum; 3CKJ; -.
DR PDBsum; 3CKN; -.
DR PDBsum; 3CKO; -.
DR PDBsum; 3CKQ; -.
DR PDBsum; 3CKV; -.
DR AlphaFoldDB; Q73WU1; -.
DR SMR; Q73WU1; -.
DR STRING; 262316.MAP_2569c; -.
DR CAZy; GT81; Glycosyltransferase Family 81.
DR EnsemblBacteria; AAS04886; AAS04886; MAP_2569c.
DR GeneID; 66693074; -.
DR KEGG; mpa:MAP_2569c; -.
DR eggNOG; COG0463; Bacteria.
DR HOGENOM; CLU_053119_0_0_11; -.
DR OMA; HLVKSFY; -.
DR EvolutionaryTrace; Q73WU1; -.
DR Proteomes; UP000000580; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Magnesium; Manganese; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..329
FT /note="Glucosyl-3-phosphoglycerate synthase"
FT /id="PRO_0000420164"
FT BINDING 55..59
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:18667419,
FT ECO:0007744|PDB:3CKQ"
FT BINDING 86
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:18667419,
FT ECO:0007744|PDB:3CKQ"
FT BINDING 119
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:18667419,
FT ECO:0007744|PDB:3CKQ"
FT BINDING 139..141
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:18667419,
FT ECO:0007744|PDB:3CKQ"
FT BINDING 141
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:18667419,
FT ECO:0007744|PDB:3CKN, ECO:0007744|PDB:3CKQ"
FT BINDING 189..192
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0000305|PubMed:18667419,
FT ECO:0007744|PDB:3CKJ"
FT BINDING 234..237
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:18667419,
FT ECO:0007744|PDB:3CKQ"
FT BINDING 263
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:18667419,
FT ECO:0007744|PDB:3CKN, ECO:0007744|PDB:3CKQ"
FT BINDING 265
FT /ligand="(2R)-3-phosphoglycerate"
FT /ligand_id="ChEBI:CHEBI:58272"
FT /evidence="ECO:0000250|UniProtKB:P9WMW9"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:3CKQ"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:3CKQ"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3CKQ"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:3CKJ"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:3CKJ"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:3CKJ"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3CKJ"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:3CKJ"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:3CKJ"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:3CKJ"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:3CKJ"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:3CKJ"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:3CKQ"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:3CKJ"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 236..248
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:3CKJ"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:3CKJ"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:3CKJ"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:3CKJ"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:3CKJ"
SQ SEQUENCE 329 AA; 34795 MW; 06493E07C809B6E7 CRC64;
MTTSDLVAGE LAGDGLRDTR PGDTWLADRS WNRPGWTVAE LEAAKAGRTI SVVLPALDEE
DTIGSVIDSI SPLVDGLVDE LIVLDSGSTD DTEIRAVAAG ARVVSREQAL PEVPIRPGKG
EALWRSLAAS RGDIVVFVDS DLINPHPMFV PWLVGPLLTG DGVHLVKSFY RRPLNVGDAG
GGAGATGGGR VTELVARPLL AALRPELGCI LQPLGGEYAA TRELLTSVPF APGYGVEIGL
LVDTFDRLGL DAIAQVNLGV REHRNRPLAE LGAMSRQVIA TLLSRCGIPD SGVGLTQFVA
DGPEGQSYTQ HTWPVSLADR PPMQAIRPR
