PGK_THEAC
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 03-AUG-2022, entry version 102.
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.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 OMA; DMIFDIG; -.
DR OrthoDB; 46017at2157; -.
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 Gene3D; 3.40.50.1260; -; 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; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 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
