ID A0A2U3PKV7_LEUCA Unreviewed; 221 AA. AC A0A2U3PKV7; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 24-JAN-2024, entry version 22. DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512}; DE Short=BPG-dependent PGAM {ECO:0000256|HAMAP-Rule:MF_01039}; DE Short=PGAM {ECO:0000256|HAMAP-Rule:MF_01039}; DE Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01039}; DE Short=dPGM {ECO:0000256|HAMAP-Rule:MF_01039}; DE EC=5.4.2.11 {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512}; GN Name=gpmA {ECO:0000256|HAMAP-Rule:MF_01039, GN ECO:0000313|EMBL:SPJ43240.1}; GN ORFNames=LCAC16_150345 {ECO:0000313|EMBL:SPJ43240.1}; OS Leuconostoc carnosum. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Leuconostoc. OX NCBI_TaxID=1252 {ECO:0000313|EMBL:SPJ43240.1, ECO:0000313|Proteomes:UP000295336}; RN [1] {ECO:0000313|Proteomes:UP000295336} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MFPC16A2803 {ECO:0000313|Proteomes:UP000295336}; RA Chaillou S.; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- CC phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01039, CC ECO:0000256|RuleBase:RU004512}. 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:0000256|HAMAP-Rule:MF_01039, CC ECO:0000256|RuleBase:RU004512}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_01039, CC ECO:0000256|RuleBase:RU004512}. CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717, CC ECO:0000256|HAMAP-Rule:MF_01039}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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; ONZM01000007; SPJ43240.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2U3PKV7; -. DR OrthoDB; 9781415at2; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000295336; Unassembled WGS sequence. 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; 2. 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 {ECO:0000256|HAMAP-Rule:MF_01039}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_01039}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01039}. FT ACT_SITE 10 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-1" FT ACT_SITE 88 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-1" FT BINDING 9..16 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 22..23 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 61 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 88..91 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 99 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 115..116 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-2" FT SITE 175 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039, FT ECO:0000256|PIRSR:PIRSR613078-3" SQ SEQUENCE 221 AA; 25442 MW; 975E10DD93E5A596 CRC64; MVAQLVLVRH GESTANRNNE FTGWTDVPLT PKGRQQAKQV GQKLAERQIL FNQVHTSYLQ RAIITANIIL FEMNQSWLPM TKTWRLNERH YGALRGLNKD LARKEYGFEA VALWRRSYTA VPPLLTKVTP DRRYPNGLEP YGESLKMASD RLLPYWTQVI EPALKAGKNQ LIVAHGSSLR ALVKYLEHIS DEDIDGLEIG NGEPIYYTFD DEFNISQRHY L //