GPMB_YERPP
ID GPMB_YERPP Reviewed; 215 AA.
AC A4TQH5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=YPDSF_3179;
OS Yersinia pestis (strain Pestoides F).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=386656;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pestoides F;
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 Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E.,
RA Richardson P.;
RT "Complete sequence of chromosome of Yersinia pestis Pestoides F.";
RL Submitted (FEB-2007) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000668; ABP41537.1; -; Genomic_DNA.
DR RefSeq; WP_002209230.1; NZ_CP009715.1.
DR AlphaFoldDB; A4TQH5; -.
DR SMR; A4TQH5; -.
DR GeneID; 66842981; -.
DR KEGG; ypp:YPDSF_3179; -.
DR PATRIC; fig|386656.14.peg.1168; -.
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_1000064138"
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 82..85
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; 23829 MW; B59BC554434E47FB CRC64;
MLQVYLVRHG ETLWNAARRI QGQSDSPLTE IGIRQAHLVA QRVRNQGITH IISSDLGRTQ
QTAKIIADAC GLTMVTDPRL RELNMGVLEN RPIDSLTPEE EQWRKQMVNG TEGARIPEGE
SMTELGRRMH AALDSCLELP AGSKPLLVSH GMALGCLLST LLGLPAHAER RLRLRNCSLS
RVDYQESPWL ASGWVIESAG DTAHLDMPAL DELQR
