ID   GPMB_ECO24              Reviewed;         215 AA.
AC   A7ZVT7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
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};
GN   OrderedLocusNames=EcE24377A_4995;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV16563.1; -; Genomic_DNA.
DR   RefSeq; WP_000942344.1; NC_009801.1.
DR   AlphaFoldDB; A7ZVT7; -.
DR   SMR; A7ZVT7; -.
DR   EnsemblBacteria; ABV16563; ABV16563; EcE24377A_4995.
DR   GeneID; 66671717; -.
DR   KEGG; ecw:EcE24377A_4995; -.
DR   HOGENOM; CLU_033323_9_5_6; -.
DR   OMA; TEWNVAR; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001122; 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_1000064120"
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;  24065 MW;  3653DA0548B9E009 CRC64;
     MLQVYLVRHG ETQWNAERRI QGQSDSPLTA KGEQQAMQVA TRAKELGITH IISSDLGRTR
     RTAEIIAQAC GCDIIFDSRL RELNMGVLEK RHIDSLTEEE ENWRRQLVNG TVDGRIPEGE
     SMQELSDRVN AALESCRDLP QGSRPLLVSH GIALGCLVST ILGLPAWAER RLRLRNCSIS
     RVDYQESLWL ASGWVVETAG DISHLDAPAL DELQR