GPM_THEAC
ID GPM_THEAC Reviewed; 200 AA.
AC Q9HIJ2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
DE Short=BPG-dependent PGAM;
DE Short=PGAM;
DE Short=Phosphoglyceromutase;
DE Short=dPGM;
DE EC=5.4.2.11;
GN OrderedLocusNames=Ta1347;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP FUNCTION AS A PHOSPHOGLYCERATE MUTASE, SUBUNIT, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF HIS-9.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=17576516; DOI=10.1007/s00792-007-0094-x;
RA Johnsen U., Schoenheit P.;
RT "Characterization of cofactor-dependent and cofactor-independent
RT phosphoglycerate mutases from Archaea.";
RL Extremophiles 11:647-657(2007).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000269|PubMed:17576516}.
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;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for 2,3-diphosphoglycerate {ECO:0000269|PubMed:17576516};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17576516}.
CC -!- INDUCTION: Inhibited by vanadate. Inhibition can partially be relieved
CC by EDTA.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC {ECO:0000305}.
CC -!- CAUTION: The original start site is 14 aa downstream of the start site
CC shown here. Experiments from PubMed:17576516 were carried out with the
CC original sequence. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC12468.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL445067; CAC12468.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048162417.1; NC_002578.1.
DR AlphaFoldDB; Q9HIJ2; -.
DR SMR; Q9HIJ2; -.
DR STRING; 273075.Ta1347; -.
DR PRIDE; Q9HIJ2; -.
DR EnsemblBacteria; CAC12468; CAC12468; CAC12468.
DR GeneID; 1456820; -.
DR KEGG; tac:Ta1347; -.
DR eggNOG; arCOG01991; Archaea.
DR HOGENOM; CLU_033323_9_3_2; -.
DR OMA; RHGESDI; -.
DR OrthoDB; 61359at2157; -.
DR SABIO-RK; Q9HIJ2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:RHEA.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..200
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase"
FT /id="PRO_0000303675"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 142
FT /evidence="ECO:0000250"
FT MUTAGEN 9
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17576516"
SQ SEQUENCE 200 AA; 22322 MW; 3256FA2B51534D72 CRC64;
MKIAILIRHG ESDINVKGIL SDTIDNNMLT EKGMRQAEHA AAELKGIDIK NFYSSPIKRA
FDTAQIIADS FNKDVVTDQR LIEIGLGKAR GRKANEFTNG LYSGHITGKI REDLEMEKWD
SLQKRVVEAI ASREGINVYV THSDPIRAAI SYFLEMGEEE TYGLSIKNAS MTVIDVEIGR
ILTLGAISMT DSVRKYLNIQ