ID KPYK_MYCPN Reviewed; 508 AA. AC P78031; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 134. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; OrderedLocusNames=MPN_303; ORFNames=MP533; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) OS (Mycoplasmoides pneumoniae). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 / Subtype 1; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC -!- ACTIVITY REGULATION: Regulated by phosphoenolpyruvate substrate and is CC allosterically activated by ribose-5-phosphate, AMP and other CC nucleoside monophosphates but not by fructose-1,6-bisphosphate. CC {ECO:0000250}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- INTERACTION: CC P78031; P02788: LTF; Xeno; NbExp=3; IntAct=EBI-2259473, EBI-1058602; CC P78031; P04004: VTN; Xeno; NbExp=3; IntAct=EBI-2259473, EBI-1036653; 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; U00089; AAB96181.1; -; Genomic_DNA. DR PIR; S73859; S73859. DR RefSeq; NP_109991.1; NC_000912.1. DR RefSeq; WP_010874660.1; NZ_OU342337.1. DR AlphaFoldDB; P78031; -. DR SMR; P78031; -. DR IntAct; P78031; 5. DR STRING; 272634.MPN_303; -. DR EnsemblBacteria; AAB96181; AAB96181; MPN_303. DR GeneID; 66609050; -. DR KEGG; mpn:MPN_303; -. DR PATRIC; fig|272634.6.peg.327; -. DR HOGENOM; CLU_015439_0_2_14; -. DR OrthoDB; 9812123at2; -. DR BioCyc; MPNE272634:G1GJ3-473-MONOMER; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016020; C:membrane; IDA:AgBase. 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 GO; GO:0031639; P:plasminogen activation; IDA:AgBase. 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; IPR036918; Pyrv_Knase_C_sf. DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf. DR NCBIfam; TIGR01064; pyruv_kin; 1. DR PANTHER; PTHR11817; PYRUVATE KINASE; 1. DR PANTHER; PTHR11817:SF132; PYRUVATE KINASE 1; 1. DR Pfam; PF00224; PK; 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..508 FT /note="Pyruvate kinase" FT /id="PRO_0000112081" FT BINDING 56 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 58..61 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 58 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 60 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 90 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 91 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 97 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 185 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 251 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 274 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 275 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 275 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 307 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 249 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" SQ SEQUENCE 508 AA; 57268 MW; 011D97377F8BB527 CRC64; MIHHLKRTKI IATCGPALTK KLWTLAMLDD PAYAAMKAEA YANIENIIKN GVTVIRLNFS HGNHEEQAVR IKIVRDVAKK LNLPVSIMLD TNGPEIRVFE TAPEGLKILK DSEVVINTTT KEVAKNNQFS VSDASGTYNM VNDVKVGQKI LVDDGKLSLV VKRIDTKNNQ VICVAQNDHT IFTKKRLNLP NADYSIPFLS AKDLRDIDFG LTHQIDYIAA SFVNTTENIK QLRDYLASKN AKHVKLIAKI ESNHALNNID GIIKASDGIM VARGDLGLEI PYYKVPYWQR YMIKACRFFN KRVITATQML DSLEKNIQPT RAEVTDVYFA VDRGNDATML SGETANGAFP LNAVYVMKMI DKQSETFFDY QYNLNYYMAN SKARHSEFWK QVVLPLAQKT APKRKLINSD FKYDFVVHAT NNLNEIYALS NARLAAAVII LTNDPQVYTG HGVDYGIFPY LIDQKPQSLS KAEFKSLANV AIKHYQQHGE ISQLKQCLGV FHNKIISL //