ID GPMA_BRUSU Reviewed; 206 AA. AC P59160; G0KE58; DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 13-DEC-2002, sequence version 1. DT 27-MAR-2024, entry version 115. 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=gpm; GN OrderedLocusNames=BRA1052, BS1330_II1044; OS Brucella suis biovar 1 (strain 1330). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=204722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=12271122; DOI=10.1073/pnas.192319099; RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E., RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.; RT "The Brucella suis genome reveals fundamental similarities between animal RT and plant pathogens and symbionts."; RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=22038969; DOI=10.1128/jb.06181-11; RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.; RT "Revised genome sequence of Brucella suis 1330."; RL J. Bacteriol. 193:6410-6410(2011). 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; AE014292; AAN34219.1; -; Genomic_DNA. DR EMBL; CP002998; AEM20496.1; -; Genomic_DNA. DR RefSeq; WP_002965600.1; NZ_KN046805.1. DR AlphaFoldDB; P59160; -. DR SMR; P59160; -. DR GeneID; 58777136; -. DR KEGG; bms:BRA1052; -. DR KEGG; bsi:BS1330_II1044; -. DR PATRIC; fig|204722.21.peg.1068; -. DR HOGENOM; CLU_033323_1_4_5; -. DR PhylomeDB; P59160; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000007104; Chromosome II. 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; Phosphoglycerate mutase-like; 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 NCBIfam; TIGR01258; pgm_1; 1. DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1. DR PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1. DR Pfam; PF00300; His_Phos_1; 1. DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 1. DR SMART; SM00855; PGAM; 1. DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1. DR PROSITE; PS00175; PG_MUTASE; 1. PE 3: Inferred from homology; KW Gluconeogenesis; Glycolysis; Isomerase. FT CHAIN 1..206 FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate FT mutase" FT /id="PRO_0000179857" FT ACT_SITE 10 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT ACT_SITE 88 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 9..16 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 22..23 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 61 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 88..91 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 99 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 115..116 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT BINDING 159..160 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT SITE 158 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" SQ SEQUENCE 206 AA; 22886 MW; 4287DDAA47754E9B CRC64; MSRTLVLVRH GQSEWNLKNL FTGWRDPGLT EQGHAEAKAA GQRLKAAGLK FDIAYTSALS RAQVTCQHIL DELGQPGLET IRDQALNERD YGDLSGLNKD DARAKWGEEQ VHIWRRSYDV PPPGGESLKD TGARVWPYYL HTIQPHVLRE ETVLVAAHGN SLRALIMALD GLTPEQILKQ ELNTGVPIIY RLNADSTVAS KEILSA //