ID   GPMB_SHIDS              Reviewed;         215 AA.
AC   Q327K0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Probable phosphoglycerate mutase GpmB {ECO:0000255|HAMAP-Rule:MF_01040};
DE            EC=5.4.2.- {ECO:0000255|HAMAP-Rule:MF_01040};
DE   AltName: Full=PGAM {ECO:0000255|HAMAP-Rule:MF_01040};
DE   AltName: Full=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01040};
GN   Name=gpmB {ECO:0000255|HAMAP-Rule:MF_01040}; OrderedLocusNames=SDY_4656;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC         Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01040};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC       Rule:MF_01040}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. GpmB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01040}.
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DR   EMBL; CP000034; ABB64505.1; -; Genomic_DNA.
DR   RefSeq; WP_000942357.1; NC_007606.1.
DR   RefSeq; YP_405996.1; NC_007606.1.
DR   AlphaFoldDB; Q327K0; -.
DR   SMR; Q327K0; -.
DR   STRING; 300267.SDY_4656; -.
DR   EnsemblBacteria; ABB64505; ABB64505; SDY_4656.
DR   KEGG; sdy:SDY_4656; -.
DR   PATRIC; fig|300267.13.peg.5518; -.
DR   HOGENOM; CLU_033323_9_5_6; -.
DR   OMA; TEWNVAR; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000002716; Chromosome.
DR   GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   HAMAP; MF_01040; PGAM_GpmB; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   InterPro; IPR023086; Phosphoglycerate_mutase_GpmB.
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   Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..215
FT                   /note="Probable phosphoglycerate mutase GpmB"
FT                   /id="PRO_1000064132"
FT   ACT_SITE        9
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT   ACT_SITE        82
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT   BINDING         8..15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT   BINDING         21..22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT   BINDING         82..85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT   BINDING         104..105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT   BINDING         151..152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
FT   SITE            150
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01040"
SQ   SEQUENCE   215 AA;  24040 MW;  73F376D42F09F778 CRC64;
     MLQVYLVRHG ETQWNAERRI QGQSDSPLTA KGEQQAMQVA TRAKELGITH IISSDLGRTR
     RTVEIIAQAC GCDIIFDSRL RELNMGVLEK SHIDSLTEEE ENWRRQLVNG TVDGRIPEGE
     SMQELSDRVN AALESCRDLP QGSRPLLVSH GIALGCLVST ILGLPAWAER RLRLRNCSIS
     RVDYQESLWL SSGWVVETAG DISHLDAPAL DELQR