ID   GPMA2_LACJO             Reviewed;         229 AA.
AC   Q74L45;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=BPG-dependent PGAM 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=PGAM 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=Phosphoglyceromutase 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=dPGM 2 {ECO:0000255|HAMAP-Rule:MF_01039};
DE            EC=5.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01039};
GN   Name=gpmA2 {ECO:0000255|HAMAP-Rule:MF_01039}; OrderedLocusNames=LJ_0380;
OS   Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=257314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNCM I-1225 / La1 / NCC 533;
RX   PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA   Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA   Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA   Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT   "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT   johnsonii NCC 533.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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}.
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DR   EMBL; AE017198; AAS08370.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q74L45; -.
DR   SMR; Q74L45; -.
DR   STRING; 257314.LJ_0380; -.
DR   EnsemblBacteria; AAS08370; AAS08370; LJ_0380.
DR   KEGG; ljo:LJ_0380; -.
DR   eggNOG; COG0588; Bacteria.
DR   HOGENOM; CLU_033323_1_5_9; -.
DR   OMA; ITESHPY; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000000581; 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; -; 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   PANTHER; PTHR11931; PTHR11931; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..229
FT                   /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT                   mutase 2"
FT                   /id="PRO_0000179884"
FT   ACT_SITE        13
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   ACT_SITE        92
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   BINDING         12..19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   BINDING         25..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   BINDING         92..95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   BINDING         119..120
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   229 AA;  26212 MW;  11E2135674109A56 CRC64;
     MKRKLAKLVL VRHGESVANR DNVYTGWNDV PLSKKGIAQA KNAGLKVEKI AEFAPTHIHT
     SVLSRAIMTA NIIADVCSFL YLPITKTWRL NERHYGALRG INKDVSKKIF GTNQVLEWRR
     GFDSVPPLLT QPVQDRRYQK YDMRLMPQGE SLHQTQERLM PYFWDHIAPE LMAGHDQLVV
     AHGSSLRALI KKIEDISNED IVKVEVPNAE PIVYTFDTDL HIVKKEILH