ID KPYK_BUCBP Reviewed; 479 AA. AC Q89AI8; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 04-NOV-2026, entry version 131. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pykA; OrderedLocusNames=bbp_297; OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Erwiniaceae; Buchnera. OX NCBI_TaxID=224915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bp; RX PubMed=12522265; DOI=10.1073/pnas.0235981100; RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.; RT "Reductive genome evolution in Buchnera aphidicola."; RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003). 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; 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 -!- ACTIVITY REGULATION: Allosterically activated by AMP and by several CC sugar phosphates. Belongs to type II PK (By similarity). {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; AE016826; AAO27022.1; -; Genomic_DNA. DR RefSeq; WP_011091423.1; NC_004545.1. DR SMR; Q89AI8; -. DR STRING; 224915.bbp_297; -. DR KEGG; bab:bbp_297; -. DR eggNOG; COG0469; Bacteria. DR HOGENOM; CLU_015439_0_2_6; -. DR OMA; AAALXEI; -. DR OrthoDB; 9812123at2; -. DR UniPathway; UPA00109; UER00188. DR FunFam; 3.40.1380.20:FF:000004; 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 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 NCBIfam; NF004491; PRK05826.1; 1. DR NCBIfam; TIGR01064; pyruv_kin; 1. DR PROSITE; PS00110; PYRUVATE_KINASE; 1. 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 Proteomes; UP000000601; Chromosome. DR AlphaFoldDB; Q89AI8; -. PE 3: Inferred from homology; KW Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Potassium; Pyruvate; Reference proteome; KW Transferase. FT CHAIN 1..479 FT /note="Pyruvate kinase" FT /id="PRO_0000112060" FT BINDING 36 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 38..41 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 38 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 40 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 70 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 77 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 160 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 225 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 251 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 252 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 252 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 284 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 223 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" SQ SEQUENCE 479 AA; 52698 MW; 674367EACE323020 CRC64; MIRRFRRTKI VATLGPSTDN HIILENMIKS GVNVFRLNFS HGTREEHIYR AKLVTSIAKR LNCHIALLGD LQGPKIRICK FQDKKVFLKV NNYFILDANL NENLGTSERV GIDYKNLPKD VKKCDILLLD DGKIQLKVIN IVDQEIFTKI IIGGVLSNNK GINKLGGGLS ARILTKKDKR DIITSIDIGV DYLAVSFPRY GSDLDHARKC AVKFGSKAKI IAKIERAEAV KDLKIIDEII LASDAIMVAR GDLGVEIGES ELAGIQKTLI RRARQLNRVV ITATQMMESM INNPMPTRAE VMDVANAVLD GSDAVMLSAE TASGKYPIET IKVMSKVCMG AEKMPSINVS QHRIHDKFHD IEEAIAMSAM YAANHLSGIT AIITMTESGK TSLMTSRITS GLPIFALSSH IQTLKLTALY RGVTPIFFNS SKEGVSAANE VINLLVKRGF LEPGNLVIIT QGDIMGKVGK TNTSRILKV //