GPMB_YERP3
ID GPMB_YERP3 Reviewed; 215 AA.
AC A7FMF8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=YpsIP31758_3480;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS49234.1; -; Genomic_DNA.
DR RefSeq; WP_002209230.1; NC_009708.1.
DR AlphaFoldDB; A7FMF8; -.
DR SMR; A7FMF8; -.
DR EnsemblBacteria; ABS49234; ABS49234; YpsIP31758_3480.
DR GeneID; 66842981; -.
DR KEGG; ypi:YpsIP31758_3480; -.
DR HOGENOM; CLU_033323_9_5_6; -.
DR OMA; TEWNVAR; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000002412; 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_1000064135"
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
