ID GPMA_STAHJ Reviewed; 228 AA. AC Q4L8T0; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 24-JAN-2024, entry version 123. 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}; OrderedLocusNames=SH0636; OS Staphylococcus haemolyticus (strain JCSC1435). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=279808; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCSC1435; RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005; RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., RA Hiramatsu K.; RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the RT extreme plasticity of its genome and the evolution of human-colonizing RT staphylococcal species."; RL J. Bacteriol. 187:7292-7308(2005). 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 -!- 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; AP006716; BAE03945.1; -; Genomic_DNA. DR RefSeq; WP_011274961.1; NC_007168.1. DR AlphaFoldDB; Q4L8T0; -. DR SMR; Q4L8T0; -. DR GeneID; 74185215; -. DR KEGG; sha:SH0636; -. DR eggNOG; COG0588; Bacteria. DR HOGENOM; CLU_033323_1_5_9; -. DR OMA; RMLPYWY; -. DR OrthoDB; 9781415at2; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000000543; Chromosome. 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 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..228 FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate FT mutase" FT /id="PRO_0000179918" 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 183..184 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" FT SITE 182 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039" SQ SEQUENCE 228 AA; 26735 MW; 0C65EFA7A78A02F4 CRC64; MPKLILCRHG QSEWNAKNLF TGWEDVQLSE QGRNEAITSG RKLKENGIEI DVAFTSLLTR ALETTQFLLA ESDQEWIPVH KSWRLNERHY GKLQGLNKDE ARKEFGEEQV HQWRRSYDVK PPAQTEEQRE SYLKDRRYRH LDHRMMPYSE SLKTTLERVV PIWTDKISQH LLDGETVLVA AHGNSIRALI KYLDNVSDED IIGYEIKTGA PLIYELDDNL NVIDHYYL //