ID   PGK_THEAC               Reviewed;         408 AA.
AC   Q9HJ95;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=Ta1075;
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; AL445066; CAC12203.1; -; Genomic_DNA.
DR   RefSeq; WP_010901486.1; NC_002578.1.
DR   AlphaFoldDB; Q9HJ95; -.
DR   SMR; Q9HJ95; -.
DR   STRING; 273075.gene:9572296; -.
DR   PaxDb; 273075-Ta1075; -.
DR   EnsemblBacteria; CAC12203; CAC12203; CAC12203.
DR   GeneID; 1456589; -.
DR   KEGG; tac:Ta1075; -.
DR   eggNOG; arCOG00496; Archaea.
DR   HOGENOM; CLU_025427_0_2_2; -.
DR   InParanoid; Q9HJ95; -.
DR   OrthoDB; 6575at2157; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000001024; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..408
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000146073"
FT   BINDING         22..24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         60..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         332
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         358..361
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   408 AA;  45372 MW;  6F3C6C2357FD5849 CRC64;
     MDEFFLMNSF DLAGKTVYLR VDINAPVNPL TGEIMGIDRF RAHIDTIRNL RNSKVVIVAH
     QSRPGKDDFI SLRQHAQILS HLLNKRVQFV DQLFGSQVNR AVSEMSDGDI VMLENSRFYS
     EEVDLTTIES MESSNIVRSL SPLFDYFIID AFAAIHRAQT TLVGFHRIKP NIAGTLIERE
     VSMIERFRKI REKPKIAILG GAKIEDSIAV SENFLSRGFV DKILTGGVVA NAFLWASGFD
     IGKKNREFIM KNNGDYEKLL DKCRAILSKY GDKLVMPTDF VMNPSGQRIS INEKIPDDQI
     LADIGLDTIV EYSEIIDGAR AIFMNGPMGM YEIEDYSSGT REVFTAVAHS KAFKLAGGGH
     TLSALDKLGL TKMIDHASTG GGALISYLSG ETMPVLEALK ESKKLFEG
//