ID   GPMB_ECOUT              Reviewed;         215 AA.
AC   Q1R246;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=UTI89_C5168;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE10568.1; -; Genomic_DNA.
DR   RefSeq; WP_000942350.1; NC_007946.1.
DR   AlphaFoldDB; Q1R246; -.
DR   SMR; Q1R246; -.
DR   EnsemblBacteria; ABE10568; ABE10568; UTI89_C5168.
DR   KEGG; eci:UTI89_C5168; -.
DR   HOGENOM; CLU_033323_9_5_6; -.
DR   OMA; TEWNVAR; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001952; 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.
FT   CHAIN           1..215
FT                   /note="Probable phosphoglycerate mutase GpmB"
FT                   /id="PRO_1000064124"
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;  24015 MW;  36567A1478B27016 CRC64;
     MLQVYLVRHG ETQWNAERRI QGQSDSPLTA KGEQQAMQVA TRAKELGITH IISSDLGRTR
     RTAEIIAQAC GCDIIFDSRL RELNMGVLET RNIDSLTEEE ENWRRQLVNG TVDGRIPEGE
     SMQELSDRVN AALESCRDLP QGSRPLLVSH GIALGCLVST ILGLPAWAER RLRLRNCSIS
     RVDYQESLWL ASGWVVETAG DISHLDAPAL DELQR