ID   F7XS04_TREPU            Unreviewed;       251 AA.
AC   F7XS04;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
DE            Short=BPG-dependent PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=dPGM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            EC=5.4.2.11 {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
GN   Name=gpmA {ECO:0000256|HAMAP-Rule:MF_01039};
GN   OrderedLocusNames=TPCCA_0168 {ECO:0000313|EMBL:AEH40123.1};
OS   Treponema paraluiscuniculi (strain Cuniculi A).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=545776 {ECO:0000313|EMBL:AEH40123.1, ECO:0000313|Proteomes:UP000008317};
RN   [1] {ECO:0000313|EMBL:AEH40123.1, ECO:0000313|Proteomes:UP000008317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cuniculi A {ECO:0000313|EMBL:AEH40123.1,
RC   ECO:0000313|Proteomes:UP000008317};
RX   PubMed=21655244; DOI=10.1371/journal.pone.0020415;
RA   Smajs D., Zobanikova M., Strouhal M., Cejkova D., Dugan-Rocha S.,
RA   Pospisilova P., Norris S.J., Albert T., Qin X., Hallsworth-Pepin K.,
RA   Buhay C., Muzny D.M., Chen L., Gibbs R.A., Weinstock G.M.;
RT   "Complete genome sequence of Treponema paraluiscuniculi, strain Cuniculi A:
RT   the loss of infectivity to humans is associated with genome decay.";
RL   PLoS ONE 6:E20415-E20415(2011).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01039,
CC       ECO:0000256|RuleBase:RU004512}.
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:0000256|ARBA:ARBA00000380,
CC         ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_01039,
CC       ECO:0000256|RuleBase:RU004512}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717,
CC       ECO:0000256|HAMAP-Rule:MF_01039}.
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DR   EMBL; CP002103; AEH40123.1; -; Genomic_DNA.
DR   RefSeq; WP_010881615.1; NC_015714.1.
DR   AlphaFoldDB; F7XS04; -.
DR   SMR; F7XS04; -.
DR   GeneID; 57878710; -.
DR   KEGG; tpl:TPCCA_0168; -.
DR   PATRIC; fig|545776.3.peg.178; -.
DR   HOGENOM; CLU_033323_1_1_12; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000008317; 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; Phosphoglycerate mutase-like; 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   NCBIfam; TIGR01258; pgm_1; 1.
DR   PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR   Pfam; PF00300; His_Phos_1; 2.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 2.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_01039};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_01039};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01039}.
FT   ACT_SITE        8
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        86
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         7..14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         20..21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         86..89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         113..114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         186..187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   SITE            185
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-3"
SQ   SEQUENCE   251 AA;  28358 MW;  8589EE625A80D60B CRC64;
     MKLVLIRHGE SEWNRLNLFT GWTDVPLTPR GESEAQEGGR VLQEAGFDFD LCYTSFLKRA
     IRTLNFVLQA LDREWLPVHK SWKLNERHYG DLQGLNKTET AQKYGEQQVR VWRRSFDVAP
     PPLTVGDARC PHTQASYRGV CASGRTPVLP FTESLKDTVA RVVPYFEEEI KPQMISGQRV
     LIVAHGNSLR ALMKHIESLD ETQIMEVNLP TGVPLVYEFE ADFTLCGKRF LGNEADVAAR
     AQAVADQGKS N
//