KPYK1_SALTY
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 03-AUG-2022, entry version 138.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
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; P77983; -.
DR PRIDE; P77983; -.
DR EnsemblBacteria; AAL20302; AAL20302; STM1378.
DR GeneID; 1252896; -.
DR KEGG; stm:STM1378; -.
DR PATRIC; fig|99287.12.peg.1461; -.
DR HOGENOM; CLU_015439_0_0_6; -.
DR OMA; MVRVHHL; -.
DR PhylomeDB; P77983; -.
DR BioCyc; SENT99287:STM1378-MON; -.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR CDD; cd00288; Pyruvate_Kinase; 1.
DR Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.40.1380.20; -; 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 PANTHER; PTHR11817; PTHR11817; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 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
