GPMB_ERWT9
ID GPMB_ERWT9 Reviewed; 215 AA.
AC B2VH13;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, 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}; OrderedLocusNames=ETA_06930;
OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS 4357 / Et1/99).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=465817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA Geider K.;
RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT bacterium in the genus Erwinia.";
RL Environ. Microbiol. 10:2211-2222(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}.
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; CU468135; CAO95739.1; -; Genomic_DNA.
DR RefSeq; WP_012440441.1; NC_010694.1.
DR AlphaFoldDB; B2VH13; -.
DR SMR; B2VH13; -.
DR STRING; 465817.ETA_06930; -.
DR EnsemblBacteria; CAO95739; CAO95739; ETA_06930.
DR KEGG; eta:ETA_06930; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_9_5_6; -.
DR OMA; TEWNVAR; -.
DR OrthoDB; 1122642at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001726; 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; Reference proteome.
FT CHAIN 1..215
FT /note="Probable phosphoglycerate mutase GpmB"
FT /id="PRO_1000136007"
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 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; 23833 MW; 0FBFA1307B2A5B78 CRC64;
MLQVYLVRHG ETLWNAARRI QGQSDSALTE KGEQQAYQVG QRVRDLGITH VIASDLGRTR
RTAEIIADAC GCSVVLDPRL RELNMGVLEQ RKLDSLSAEE ESWRKALVDG TENGRIPQGE
SMSEMAQRMR QALDACLSLP ENSRPLIVSH GMALGVLVST ILGLPANAER RLRLRNCSIS
RVDHQQSPWL ASGWVVETAG DVSHLEDTAL DELQR