ID KPYK1_SALTI Reviewed; 470 AA. AC Q8Z6K2; DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 24-JAN-2024, entry version 126. DE RecName: Full=Pyruvate kinase I; DE EC=2.7.1.40; DE AltName: Full=PK-1; GN Name=pykF; OrderedLocusNames=STY1744, t1246; OS Salmonella typhi. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=90370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT18; RX PubMed=11677608; DOI=10.1038/35101607; RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T., RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., RA Barrell B.G.; RT "Complete genome sequence of a multiple drug resistant Salmonella enterica RT serovar Typhi CT18."; RL Nature 413:848-852(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700931 / Ty2; RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003; RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., RA Kodoyianni V., Schwartz D.C., Blattner F.R.; RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and RT CT18."; RL J. Bacteriol. 185:2330-2337(2003). 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; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL513382; CAD01987.1; -; Genomic_DNA. DR EMBL; AE014613; AAO68900.1; -; Genomic_DNA. DR RefSeq; NP_456147.1; NC_003198.1. DR AlphaFoldDB; Q8Z6K2; -. DR SMR; Q8Z6K2; -. DR STRING; 220341.gene:17585679; -. DR KEGG; stt:t1246; -. DR KEGG; sty:STY1744; -. DR PATRIC; fig|220341.7.peg.1755; -. DR eggNOG; COG0469; Bacteria. DR HOGENOM; CLU_015439_0_0_6; -. DR OMA; MVRVHHL; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000000541; Chromosome. DR Proteomes; UP000002670; Chromosome. 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; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd00288; 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; TIGR01064; pyruv_kin; 1. DR PANTHER; PTHR11817:SF3; AT14039P-RELATED; 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 3: Inferred from homology; KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Potassium; Pyruvate; Transferase. FT CHAIN 1..470 FT /note="Pyruvate kinase I" FT /id="PRO_0000112071" FT BINDING 32 FT /ligand="substrate" FT /evidence="ECO:0000250" 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" FT BINDING 36 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 66 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 67 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" 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 222 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 245 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 246 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 246 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 278 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 220 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT CONFLICT 370 FT /note="K -> E (in Ref. 2; AAO68900)" FT /evidence="ECO:0000305" SQ SEQUENCE 470 AA; 50656 MW; C7BF717504E38262 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 GAVETAEKLK APLIVVATQG GKSARAVRKY FPDATILALT TNEVTARQLV LSKGVVSQLV KEINSTDDFY RLGKDVALQS GLAQKGDVVV MVSGALVPSG TTNTASVHVL //