ID   PGK_THEKO               Reviewed;         411 AA.
AC   Q5JIG7;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00145};
DE            EC=2.7.2.3 {ECO:0000255|HAMAP-Rule:MF_00145};
GN   Name=pgk {ECO:0000255|HAMAP-Rule:MF_00145}; OrderedLocusNames=TK1146;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00145};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00145}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00145}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00145}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00145}.
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DR   EMBL; AP006878; BAD85335.1; -; Genomic_DNA.
DR   RefSeq; WP_011250097.1; NC_006624.1.
DR   AlphaFoldDB; Q5JIG7; -.
DR   SMR; Q5JIG7; -.
DR   STRING; 69014.TK1146; -.
DR   EnsemblBacteria; BAD85335; BAD85335; TK1146.
DR   GeneID; 3234551; -.
DR   KEGG; tko:TK1146; -.
DR   PATRIC; fig|69014.16.peg.1122; -.
DR   eggNOG; arCOG00496; Archaea.
DR   HOGENOM; CLU_025427_0_2_2; -.
DR   InParanoid; Q5JIG7; -.
DR   OMA; DMIFDIG; -.
DR   OrthoDB; 46017at2157; -.
DR   PhylomeDB; Q5JIG7; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1260; -; 2.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
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.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..411
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000146068"
FT   BINDING         19..21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         57..60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         332
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         358..361
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ   SEQUENCE   411 AA;  46037 MW;  4F17DDBDF63C10DE CRC64;
     MFRITDFTYE GKTVFLRADL NSPVEKGRIT SDARFRAVLP TIQHLLDNGA KLVIATHQSR
     PYKGDYITTE EHAQILSRLL GQEVEYVEDI FGKYARERIS SLKPGEAIIL ENLRFSAEEV
     FNRSIEECEK TFFVRKLAPL IDYVVNDAFA TAHRSQPSLV GFARLKPMIM GKLMETEVDA
     LSKAYESEER PRVYVLGGAK VDDSLRVAEN VLRKGKADLI LTGGLVGQIF TLAKGFDLGD
     ANIEFLHRKG LLELVDWAEK ILDEFYPYVR TPVDFAIDYK GERLEVDLLG GEKRLFDQYP
     ILDIGSRTVE KYREILIGAK IIVANGPMGV FEREEFAVGT VGVFRAIGES PAFSVVGGGH
     SIASIYRYNI TGISHISTGG GAMLSFFAGE ELPVLKALKI SYERFKDRVK E