GPMB_YERE8
ID GPMB_YERE8 Reviewed; 215 AA.
AC A1JJB8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=YE0592;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(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; AM286415; CAL10707.1; -; Genomic_DNA.
DR RefSeq; WP_005166949.1; NC_008800.1.
DR RefSeq; YP_001004947.1; NC_008800.1.
DR AlphaFoldDB; A1JJB8; -.
DR SMR; A1JJB8; -.
DR STRING; 393305.YE0592; -.
DR EnsemblBacteria; CAL10707; CAL10707; YE0592.
DR GeneID; 67419497; -.
DR KEGG; yen:YE0592; -.
DR PATRIC; fig|393305.7.peg.686; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_9_5_6; -.
DR OMA; TEWNVAR; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000000642; 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_1000149541"
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; 23729 MW; 23ACACF46CDA2FDB CRC64;
MLQVFLVRHG ETVWNASRQI QGQSDSPLTA VGERQAHLVA QRVRSQGITH IITSDLGRTQ
QTAKIIADAC GLKVVTDPRL RELNMGVLET RPIESLTPEE EQWRKQMING TEGGRIPEGE
SMAELGRRMR AALDSCLELP AGSKPLLVSH GMALGCLLST LLGLPPHAER RLRLRNCSLS
RVDYQESPWL ASGWVIESAG DTAHLDMPAL DELQR