ID   GPMA_CHLPM              Reviewed;         247 AA.
AC   A4SDM0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Cvib_0557;
OS   Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris
OS   vibrioformis (strain DSM 265)).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 265 / 1930;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J.,
RA   Schuster S.C., Bryant D.A., Richardson P.;
RT   "Complete sequence of Prosthecochloris vibrioformis DSM 265.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000607; ABP36579.1; -; Genomic_DNA.
DR   RefSeq; WP_011889807.1; NC_009337.1.
DR   AlphaFoldDB; A4SDM0; -.
DR   SMR; A4SDM0; -.
DR   STRING; 290318.Cvib_0557; -.
DR   EnsemblBacteria; ABP36579; ABP36579; Cvib_0557.
DR   KEGG; pvi:Cvib_0557; -.
DR   eggNOG; COG0588; Bacteria.
DR   HOGENOM; CLU_033323_1_1_10; -.
DR   OMA; RMLPYWY; -.
DR   OrthoDB; 1122642at2; -.
DR   UniPathway; UPA00109; UER00186.
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..247
FT                   /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_1000084328"
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   247 AA;  28213 MW;  C94DCF83D2F94903 CRC64;
     MIKLVLLRHG ESQWNLDNRF TGWHDIDLTD KGRREASNAG KLLCEAGFEF DVAYVSVLKR
     AIRTLWNVLD EMNLMWIPVI RNWRLNERHY GALQGLNKAE TAQKYGDEQV LVWRRSYDTP
     PPPLERTDER WPGSDRRYAA LDADEVPLTE CLKDTVARFL PFWHETIAPE ISKGRNVLIV
     AHGNSLRALV KYLDGISEED IVGLNIPTGI PLVYELDDNL KPLKSYYLGD QEELKKAVDA
     VAGQGKA