GPMA_RHIEC
ID GPMA_RHIEC Reviewed; 209 AA.
AC Q8KL44;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=BPG-dependent PGAM {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=PGAM {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01039};
DE Short=dPGM {ECO:0000255|HAMAP-Rule:MF_01039};
DE EC=5.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01039};
GN Name=gpmA {ECO:0000255|HAMAP-Rule:MF_01039}; Synonyms=pgmY;
GN OrderedLocusNames=RHE_PD00127;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OG Plasmid sym p42d.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9274036; DOI=10.1099/00221287-143-8-2825;
RA Ramirez-Romero M.A., Bustos P., Girard L., Rodriguez O., Cevallos M.A.,
RA Davila G.;
RT "Sequence, localization and characteristics of the replicator region of the
RT symbiotic plasmid of Rhizobium etli.";
RL Microbiology 143:2825-2831(1997).
RN [2]
RP SEQUENCE REVISION.
RA Quintero V., Cevallos M.A., Davila G.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=12801410; DOI=10.1186/gb-2003-4-6-r36;
RA Gonzalez V., Bustos P., Ramirez-Romero M.A., Medrano-Soto A., Salgado H.,
RA Hernandez-Gonzalez I., Hernandez-Celis J.C., Quintero V.,
RA Moreno-Hagelsieb G., Girard L., Rodriguez O., Flores M., Cevallos M.A.,
RA Collado-Vides J., Romero D., Davila G.;
RT "The mosaic structure of the symbiotic plasmid of Rhizobium etli CFN42 and
RT its relation to other symbiotic genome compartments.";
RL Genome Biol. 4:R36.1-R36.13(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01039}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000255|HAMAP-Rule:MF_01039};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01039}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01039}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01039}.
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; U80928; AAM54923.1; -; Genomic_DNA.
DR RefSeq; WP_008534389.1; NC_004041.2.
DR AlphaFoldDB; Q8KL44; -.
DR SMR; Q8KL44; -.
DR EnsemblBacteria; AAM54923; AAM54923; RHE_PD00127.
DR GeneID; 45960471; -.
DR GeneID; 58692114; -.
DR KEGG; ret:RHE_PD00127; -.
DR HOGENOM; CLU_033323_1_4_5; -.
DR OMA; EYMYIRR; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001936; Plasmid sym p42d.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; 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_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis; Glycolysis; Isomerase; Plasmid; Reference proteome.
FT CHAIN 1..209
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase"
FT /id="PRO_0000179904"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT ACT_SITE 87
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 114..115
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 158..159
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT SITE 157
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
SQ SEQUENCE 209 AA; 22885 MW; 85762898661E858E CRC64;
MSTLVIVRHG QSEGNARGEF TGTSDVPLTQ EGWSESRRAG SLLANLGISF DIAFSSALLR
TVDTCRAILN ETNGDLLEPI RRTELNERDY GQLTGINKNV ARERWGQDVV QVWRRSYSTP
PPGGESIRDI SARVLPFLIS EVFPPLLRGK SVLVVAHGNT IRSLKQGIER LTIQDTLAIE
SPTAAPTVYR IASDLSIIEK TNVLVGTVC
