GPGP_MYCTO
ID GPGP_MYCTO Reviewed; 223 AA.
AC P9WIC6; L0T9S0; P71724; Q7D764;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Glucosyl-3-phosphoglycerate phosphatase;
DE EC=3.1.3.85 {ECO:0000250|UniProtKB:P9WIC7};
DE AltName: Full=Mannosyl-3-phosphoglycerate phosphatase;
DE EC=3.1.3.70 {ECO:0000250|UniProtKB:P9WIC7};
GN Name=gpgP; OrderedLocusNames=MT2492;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Involved in the biosynthesis of mycobacterial methylglucose
CC lipopolysaccharides (MGLPs). Catalyzes the dephosphorylation of
CC glucosyl-3-phosphoglycerate (GPG) to glucosylglycerate (GG). GPG is the
CC preferred substrate, but GpgP also exhibits low dephosphorylation
CC activity on mannosyl-3-phosphoglycerate (MPG) and mannosylglucosyl-3-
CC phosphoglycerate (MGPG) in vitro. Shows only trace of phosphoglycerate
CC mutase (PGM) activity. {ECO:0000250|UniProtKB:P9WIC7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + H2O =
CC (2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + phosphate;
CC Xref=Rhea:RHEA:31343, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:62510, ChEBI:CHEBI:62600; EC=3.1.3.85;
CC Evidence={ECO:0000250|UniProtKB:P9WIC7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31344;
CC Evidence={ECO:0000250|UniProtKB:P9WIC7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O = (2R)-2-O-
CC (alpha-D-mannosyl)-glycerate + phosphate; Xref=Rhea:RHEA:19309,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57541,
CC ChEBI:CHEBI:57744; EC=3.1.3.70;
CC Evidence={ECO:0000250|UniProtKB:P9WIC7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19310;
CC Evidence={ECO:0000250|UniProtKB:P9WIC7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-O-[alpha-D-mannopyranosyl-(1->2)-alpha-D-
CC glucopyranosyl]-3-phospho-glycerate + H2O = (2R)-2-O-[alpha-D-
CC mannopyranosyl-(1->2)-alpha-D-glucopyranosyl]-glycerate + phosphate;
CC Xref=Rhea:RHEA:47696, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:62602, ChEBI:CHEBI:87836;
CC Evidence={ECO:0000250|UniProtKB:P9WIC7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47697;
CC Evidence={ECO:0000250|UniProtKB:P9WIC7};
CC -!- SUBUNIT: Homodimer. Dimerization of the enzyme is essential for its
CC dephosphorylation activity. {ECO:0000250|UniProtKB:P9WIC7}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK46789.1; -; Genomic_DNA.
DR PIR; F70685; F70685.
DR RefSeq; WP_003412388.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WIC6; -.
DR SMR; P9WIC6; -.
DR EnsemblBacteria; AAK46789; AAK46789; MT2492.
DR GeneID; 45426406; -.
DR KEGG; mtc:MT2492; -.
DR PATRIC; fig|83331.31.peg.2687; -.
DR HOGENOM; CLU_033323_9_5_11; -.
DR BRENDA; 3.1.3.85; 3445.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0050531; F:mannosyl-3-phosphoglycerate phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..223
FT /note="Glucosyl-3-phosphoglycerate phosphatase"
FT /id="PRO_0000428030"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P9WIC7"
FT ACT_SITE 84
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WIC7"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WIC7"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WIC7"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WIC7"
SQ SEQUENCE 223 AA; 24174 MW; 1B5FD5DEF80A87A0 CRC64;
MRARRLVMLR HGQTDYNVGS RMQGQLDTEL SELGRTQAVA AAEVLGKRQP LLIVSSDLRR
AYDTAVKLGE RTGLVVRVDT RLRETHLGDW QGLTHAQIDA DAPGARLAWR EDATWAPHGG
ESRVDVAARS RPLVAELVAS EPEWGGADEP DRPVVLVAHG GLIAALSAAL LKLPVANWPA
LGGMGNASWT QLSGHWAPGS DFESIRWRLD VWNASAQVSS DVL
