ID   KPYK1_SALTY             Reviewed;         470 AA.
AC   P77983;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   04-NOV-2026, entry version 154.
DE   RecName: Full=Pyruvate kinase I;
DE            EC=2.7.1.40 {ECO:0000269|PubMed:3297035};
DE   AltName: Full=PK-1;
GN   Name=pykF; OrderedLocusNames=STM1378;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=9023191; DOI=10.1128/jb.179.4.1105-1111.1997;
RA   Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R.,
RA   Holden D.W.;
RT   "Analysis of the boundaries of Salmonella pathogenicity island 2 and the
RT   corresponding chromosomal region of Escherichia coli K-12.";
RL   J. Bacteriol. 179:1105-1111(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, MAGNESIUM COFACTOR, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=3297035; DOI=10.1042/bj2410573;
RA   Garcia-Olalla C., Garrido-Pertierra A.;
RT   "Purification and kinetic properties of pyruvate kinase isoenzymes of
RT   Salmonella typhimurium.";
RL   Biochem. J. 241:573-581(1987).
CC   -!- FUNCTION: Catalyzes the formation of pyruvate in the last step of
CC       glycolysis, it is irreversible under physiological conditions. The
CC       reaction is critical for the control of metabolic flux in the second
CC       part of glycolysis. {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pyruvate + ATP = phosphoenolpyruvate + ADP + H(+);
CC         Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC         EC=2.7.1.40; Evidence={ECO:0000269|PubMed:3297035};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18159;
CC         Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:3297035};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Belongs to type I PK; fructose 1,6-bisphosphate-
CC       activated. {ECO:0000269|PubMed:3297035}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.21 mM for ADP {ECO:0000269|PubMed:3297035};
CC       pH dependence:
CC         Optimum pH is 4.0-6.8. {ECO:0000269|PubMed:3297035};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:3297035}.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR   EMBL; X99945; CAA68205.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20302.1; -; Genomic_DNA.
DR   RefSeq; NP_460343.1; NC_003197.2.
DR   RefSeq; WP_000751447.1; NC_003197.2.
DR   AlphaFoldDB; P77983; -.
DR   SMR; P77983; -.
DR   STRING; 99287.STM1378; -.
DR   PaxDb; 99287-STM1378; -.
DR   GeneID; 1252896; -.
DR   KEGG; stm:STM1378; -.
DR   PATRIC; fig|99287.12.peg.1461; -.
DR   HOGENOM; CLU_015439_0_0_6; -.
DR   OMA; AACMMRS; -.
DR   PhylomeDB; P77983; -.
DR   BioCyc; SENT99287:STM1378-MONOMER; -.
DR   UniPathway; UPA00109; UER00188.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0004743; F:pyruvate kinase activity; EXP:UniProtKB.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-ARBA.
DR   CDD; cd00288; Pyruvate_Kinase; 1.
DR   FunFam; 2.40.33.10:FF:000001; Pyruvate kinase; 1.
DR   FunFam; 3.20.20.60:FF:000025; Pyruvate kinase; 1.
DR   FunFam; 3.40.1380.20:FF:000003; Pyruvate kinase; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR   Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_kinase-like_dom_sf.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   InterPro; IPR018209; Pyrv_Knase_AS.
DR   InterPro; IPR015793; Pyrv_Knase_brl.
DR   InterPro; IPR015795; Pyrv_Knase_C.
DR   InterPro; IPR036918; Pyrv_Knase_C_sf.
DR   InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR   NCBIfam; NF004491; PRK05826.1; 1.
DR   NCBIfam; NF004978; PRK06354.1; 1.
DR   NCBIfam; NF006664; pykF; 1.
DR   NCBIfam; TIGR01064; pyruv_kin; 1.
DR   PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR   SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Potassium; Pyruvate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..470
FT                   /note="Pyruvate kinase I"
FT                   /id="PRO_0000112072"
FT   BINDING         32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         34..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         34
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         36
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         66
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         67
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         156
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P14618"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         222
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   BINDING         278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P30613"
FT   SITE            220
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P00549"
FT   CONFLICT        142
FT                   /note="V -> C (in Ref. 1; CAA68205)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   470 AA;  50657 MW;  116411A30C49AAC0 CRC64;
     MKKTKIVCTI GPKTESEEML SKMLDAGMNV MRLNFSHGDY AEHGQRIQNL RNVMSKTGKK
     AAILLDTKGP EIRTIKLEGG NDVSLKAGQT FTFTTDKSVV GNNEIVAVTY EGFTSDLSVG
     NTVLVDDGLI GMEVTAIEGN KVICKVLNNG DLGENKGVNL PGVSIALPAL AEKDKQDLIF
     GCEQGVDFVA ASFIRKRSDV VEIREHLKAH GGENIQIISK IENQEGLNNF DEILEASDGI
     MVARGDLGVE IPVEEVIFAQ KMMIEKCIRA RKVVITATQM LDSMIKNPRP TRAEAGDVAN
     AILDGTDAVM LSGESAKGKY PLEAVSIMAT ICERTDRVMN SRLDYNNDSR KLRITEAVCR
     GAVETAEKLE APLIVVATQG GKSARAVRKY FPDATILALT TNEVTARQLV LSKGVVSQLV
     KEINSTDDFY RLGKDVALQS GLAQKGDVVV MVSGALVPSG TTNTASVHVL
//