ID   PGK_PYRWO               Reviewed;         410 AA.
AC   P61884; P50316;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-MAY-2023, entry version 69.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk;
OS   Pyrococcus woesei.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=2262;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 49860 / DSM 3773 / JCM 8421 / Vul4;
RX   PubMed=7588750; DOI=10.1111/j.1432-1033.1995.227_1.x;
RA   Hess D., Krueger K., Knappik A., Palm P., Hensel R.;
RT   "Dimeric 3-phosphoglycerate kinases from hyperthermophilic Archaea.
RT   Cloning, sequencing and expression of the 3-phosphoglycerate kinase gene of
RT   Pyrococcus woesei in Escherichia coli and characterization of the protein.
RT   Structural and functional comparison with the 3-phosphoglycerate kinase of
RT   Methanothermus fervidus.";
RL   Eur. J. Biochem. 233:227-237(1995).
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: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; X73527; CAA51930.1; -; Genomic_DNA.
DR   PIR; S68188; S68188.
DR   AlphaFoldDB; P61884; -.
DR   SMR; P61884; -.
DR   BRENDA; 2.7.2.3; 5249.
DR   SABIO-RK; P61884; -.
DR   UniPathway; UPA00109; UER00185.
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; IPR015911; Phosphoglycerate_kinase_CS.
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.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..410
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000146069"
FT   BINDING         19..21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         57..60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
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   410 AA;  46224 MW;  D90D4172A06707E0 CRC64;
     MFRLRDFEYY NRTVFLRVDL NSPMSNGKII SDARFRAVLP TIKYLIESGA KVVVGTHQGK
     PYSEEYSTTE EHARILSELL NMHVEYVEDI FGKYARERIK AMKPGEVIVL ENLRFSAEEV
     KNATIEECEK TFFVRKLSQV IDLVVNDAFA AAHRSQPSLV GFARIKPMIM GFLMEKEVDA
     LTKAYESEEK PRVYVLGGAK VDDSLKVAEN VLRKEKADLI LTGGLVGQLF TLAKGFDLGR
     ENIKFLEKKG ILKYVDWAEK ILDEFYPYVR TPVDFAIDFK GERVEIDLLS DEKRLFDEYP
     ILDIGSRTVE KYREILLKAR IIVANGPMGV FEREEFAVGT IGVFKAIGES PAFSVIGGGH
     SIASIYKYNI TGISHISTGG GAMLTFFAGE KLPVLEALKI SYEKFSNLLS
//