GPMA_TREPA
ID GPMA_TREPA Reviewed; 251 AA.
AC P96121;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
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}; Synonyms=gpm, pgm;
GN OrderedLocusNames=TP_0168;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9332349; DOI=10.1016/s0378-1119(97)00234-5;
RA Hardham J.M., Stamm L.V., Porcella S.F., Frye J.G., Barnes N.Y.,
RA Howell J.K., Mueller S.L., Radolf J.D., Weinstock G.M., Norris S.J.;
RT "Identification and transcriptional analysis of a Treponema pallidum operon
RT encoding a putative ABC transport system, an iron-activated repressor
RT protein homolog, and a glycolytic pathway enzyme homolog.";
RL Gene 197:47-64(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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; U55214; AAC45730.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC65158.1; -; Genomic_DNA.
DR PIR; E71357; E71357.
DR RefSeq; WP_010881615.1; NC_021490.2.
DR AlphaFoldDB; P96121; -.
DR SMR; P96121; -.
DR IntAct; P96121; 1.
DR STRING; 243276.TPANIC_0168; -.
DR EnsemblBacteria; AAC65158; AAC65158; TP_0168.
DR GeneID; 57878710; -.
DR KEGG; tpa:TP_0168; -.
DR eggNOG; COG0588; Bacteria.
DR HOGENOM; CLU_033323_1_1_12; -.
DR OMA; RMLPYWY; -.
DR OrthoDB; 1122642at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000000811; 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; 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; Reference proteome.
FT CHAIN 1..251
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase"
FT /id="PRO_0000179934"
FT ACT_SITE 8
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT ACT_SITE 86
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 7..14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 20..21
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 86..89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 113..114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 186..187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT SITE 185
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
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
