ID   GPMI_TOBBP              Reviewed;          81 AA.
AC   Q8L2S1;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000250|UniProtKB:Q9X519};
DE            Short=BPG-independent PGAM {ECO:0000250|UniProtKB:Q9X519};
DE            Short=Phosphoglyceromutase {ECO:0000250|UniProtKB:Q9X519};
DE            Short=iPGM {ECO:0000250|UniProtKB:Q9X519};
DE            EC=5.4.2.12 {ECO:0000250|UniProtKB:Q9X519};
DE   Flags: Fragment;
GN   Name=gpmI;
OS   Tomato big bud phytoplasma.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=35770;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Streten C., Gibb K.S.;
RT   "Phytoplasma genomics: the Tomato big bud phytoplasma as a model.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000250|UniProtKB:Q9X519}.
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; Evidence={ECO:0000250|UniProtKB:Q9X519};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q9X519};
CC       Note=Binds 2 manganese ions per subunit.
CC       {ECO:0000250|UniProtKB:Q9X519};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000250|UniProtKB:Q9X519}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9X519}.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. {ECO:0000250|UniProtKB:Q9X519}.
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DR   EMBL; AF494526; AAM28551.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8L2S1; -.
DR   SMR; Q8L2S1; -.
DR   UniPathway; UPA00109; UER00186.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro.
DR   GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.1450.10; -; 1.
DR   InterPro; IPR011258; BPG-indep_PGM_N.
DR   InterPro; IPR036646; PGAM_B_sf.
DR   InterPro; IPR005995; Pgm_bpd_ind.
DR   PANTHER; PTHR31637; PTHR31637; 1.
DR   Pfam; PF06415; iPGM_N; 1.
DR   SUPFAM; SSF64158; SSF64158; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Isomerase; Manganese; Metal-binding.
FT   CHAIN           <1..>81
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_0000212224"
FT   ACT_SITE        14
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         14
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X519"
FT   NON_TER         1
FT   NON_TER         81
SQ   SEQUENCE   81 AA;  8858 MW;  4A767535D397F63C CRC64;
     GEAVGLPAQQ MGNSEVGHLN LGAGRVVHQS LTYINRKIKD GSFFKNKCFL KVIQHVKTNK
     SKLHLLGLVS DGGVHSHLDH F