ID   GPMB_ECOLC              Reviewed;         215 AA.
AC   B1IS24;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=EcolC_3661;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA79272.1; -; Genomic_DNA.
DR   RefSeq; WP_000942344.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IS24; -.
DR   SMR; B1IS24; -.
DR   GeneID; 66671717; -.
DR   KEGG; ecl:EcolC_3661; -.
DR   HOGENOM; CLU_033323_9_5_6; -.
DR   OMA; TEWNVAR; -.
DR   UniPathway; UPA00109; UER00186.
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_1000084335"
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