AC MF_01038; DC Protein; auto TR HAMAP; MF_01038; -; 1; level=0 XX Names: GpmI XX ID GPMI DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase; DE Short=BPG-independent PGAM; DE Short=Phosphoglyceromutase; DE Short=iPGM; DE EC=5.4.2.12; GN Name=gpmI; XX case CC -!- FUNCTION: Essential for rapid growth and for sporulation. Catalyzes the CC interconversion of 2-phosphoglycerate and 3-phosphoglycerate. else CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- CC phosphoglycerate. end case CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289; CC EC=5.4.2.12; case CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 2 manganese ions per subunit.; end case CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. case CC -!- SUBUNIT: Monomer. end case case CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. end case CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase CC family. XX DR Pfam; PF06415; iPGM_N; 1; trigger=no DR Pfam; PF01676; Metalloenzyme; 1; trigger=no DR NCBIfam; TIGR01307; Pgm_bpd_ind; 1; trigger=no XX KW Isomerase KW Glycolysis case KW Metal-binding KW Manganese end case case and KW Phosphoprotein end case case KW Sporulation end case XX GO GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity case GO GO:0030145; F:manganese ion binding end case GO GO:0006096; P:glycolytic process case GO GO:0009507; C:chloroplast end case XX FT From: GPMI_GEOSE (Q9X519) FT BINDING 153..154 FT /ligand="substrate" FT Condition: R-D FT BINDING 261..264 FT /ligand="substrate" FT Condition: R-x-x-R FT ACT_SITE 62 FT /note="Phosphoserine intermediate" FT Condition: S FT BINDING 12 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT Group: 1; Condition: D FT BINDING 62 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT Group: 1; Condition: S FT BINDING 403 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT Group: 1; Condition: D FT BINDING 407 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT Group: 1; Condition: H FT BINDING 444 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT Group: 1; Condition: D FT BINDING 445 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT Group: 1; Condition: H FT BINDING 462 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT Group: 1; Condition: H FT BINDING 123 FT /ligand="substrate" FT Condition: H FT BINDING 185 FT /ligand="substrate" FT Condition: R FT BINDING 191 FT /ligand="substrate" FT Condition: [RK] FT BINDING 336 FT /ligand="substrate" FT Condition: K FT From: GPMI_BACSU (P39773) case FT MOD_RES 36 FT /note="Phosphotyrosine" FT Condition: Y end case XX Size: 490-552; Related: MF_01402; Template: Q9X519; P39773; P37689; Scope: Bacteria Archaea Plastid Fusion: Nter: None Cter: None Duplicate: in METAC Plasmid: None Comments: Possible wrong start in METMA and in the second copy of gpmI in METAC. LEPIC and LEPIN seem to be more closely related to protozoan and plant gpmI than to bacterial orthologs; not shown in alignment. XX # Revision 1.42 2023/06/01 //