ID   GPMA_PARPJ              Reviewed;         248 AA.
AC   B2SX15;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Bphyt_0534;
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX   PubMed=21551308; DOI=10.1128/jb.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
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   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-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; CP001052; ACD14959.1; -; Genomic_DNA.
DR   RefSeq; WP_012431600.1; NC_010681.1.
DR   AlphaFoldDB; B2SX15; -.
DR   SMR; B2SX15; -.
DR   STRING; 398527.Bphyt_0534; -.
DR   EnsemblBacteria; ACD14959; ACD14959; Bphyt_0534.
DR   KEGG; bpy:Bphyt_0534; -.
DR   eggNOG; COG0588; Bacteria.
DR   HOGENOM; CLU_033323_1_1_4; -.
DR   OMA; RMLPYWY; -.
DR   OrthoDB; 1122642at2; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001739; Chromosome 1.
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; 2.
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.
FT   CHAIN           1..248
FT                   /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_1000135931"
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   248 AA;  27938 MW;  F513FA8D7B2E73E3 CRC64;
     MYKLVLIRHG ESTWNKENRF TGWVDVDLTE QGNNEAQQAG VLLKESGYTF DIAYTSVLKR
     AIRTLWHVQD KMDLMYLPVV HSWRLNERHY GALSGLNKAE TAAKFGDEQV LVWRRSYDTP
     PPALEPTDDR APYNDPRYAK VPREQLPLTE CLKDTVARVL PLWNESIAPA IKSGRKVVIA
     AHGNSIRALV KYLDNISDDD IVGLNIPNGV PLVYELDEDL KPIKHYYLGD QEAIAKAQAA
     VAKQGKAG