PGK_PYRWO
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-AUG-2022, entry version 66.
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 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 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