ID   GPGP_MYCVP              Reviewed;         225 AA.
AC   A1TC01;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Glucosyl-3-phosphoglycerate phosphatase {ECO:0000303|PubMed:22355692};
DE            EC=3.1.3.85 {ECO:0000269|PubMed:22355692};
GN   Name=gpgP {ECO:0000303|PubMed:22355692}; OrderedLocusNames=Mvan_3924;
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1;
RX   PubMed=22355692; DOI=10.1038/srep00177;
RA   Mendes V., Maranha A., Alarico S., da Costa M.S., Empadinhas N.;
RT   "Mycobacterium tuberculosis Rv2419c, the missing glucosyl-3-
RT   phosphoglycerate phosphatase for the second step in methylglucose
RT   lipopolysaccharide biosynthesis.";
RL   Sci. Rep. 1:177-177(2011).
CC   -!- FUNCTION: Involved in the biosynthesis of mycobacterial methylglucose
CC       lipopolysaccharides (MGLP). Catalyzes the dephosphorylation of
CC       glucosyl-3-phosphoglycerate (GPG) to glucosylglycerate.
CC       {ECO:0000269|PubMed:22355692}.
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:0000269|PubMed:22355692};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WIC7}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000511; ABM14701.1; -; Genomic_DNA.
DR   RefSeq; WP_011781081.1; NC_008726.1.
DR   AlphaFoldDB; A1TC01; -.
DR   SMR; A1TC01; -.
DR   STRING; 350058.Mvan_3924; -.
DR   EnsemblBacteria; ABM14701; ABM14701; Mvan_3924.
DR   KEGG; mva:Mvan_3924; -.
DR   eggNOG; COG0406; Bacteria.
DR   HOGENOM; CLU_033323_9_5_11; -.
DR   OMA; TEWNVAR; -.
DR   OrthoDB; 1122642at2; -.
DR   Proteomes; UP000009159; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..225
FT                   /note="Glucosyl-3-phosphoglycerate phosphatase"
FT                   /id="PRO_0000420160"
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         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WIC7"
SQ   SEQUENCE   225 AA;  24218 MW;  A7B2AEE573782089 CRC64;
     MRVRRLVMLR HGQTEYNAGS RMQGQLDTDL SDLGREQAVA AAEVLAKRQP LLIVSSDLRR
     ALDTAVALGD RSGQPVSIDT RLRETHLGDW QGMTHLEVDA AAPGARLAWR DDARWAPHGG
     ESRVDVADRS LPLVHELVTQ QTDWGAAGSD RPVVLVAHGG LIAALTAALL GLPVDNWPVL
     GGMGNASWVQ LAGHTRADGD PGAFADIRWR LDVWNASAQV ANDVL