ID KPYK_THEAC Reviewed; 544 AA. AC P32044; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 27-MAR-2024, entry version 133. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN OrderedLocusNames=Ta0896; OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC OS 15155 / AMRC-C165). OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales; OC Thermoplasmataceae; Thermoplasma. OX NCBI_TaxID=273075; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165; RX PubMed=11029001; DOI=10.1038/35035069; RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.; RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma RT acidophilum."; RL Nature 407:508-513(2000). RN [2] RP CHARACTERIZATION. RX PubMed=1426985; DOI=10.1016/0378-1097(92)90636-3; RA Potter S., Fothergill-Gilmore L.A.; RT "Purification and properties of pyruvate kinase from Thermoplasma RT acidophilum."; RL FEMS Microbiol. Lett. 73:235-239(1992). 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 -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}. CC -!- CAUTION: PubMed:1426985 has published some partial sequence, these CC sequences do not originate from T.acidophilum, rather they seem to be CC contaminated with human samples. {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; AL445065; CAC12025.1; -; Genomic_DNA. DR RefSeq; WP_010901306.1; NC_002578.1. DR AlphaFoldDB; P32044; -. DR SMR; P32044; -. DR STRING; 273075.gene:9572111; -. DR PaxDb; 273075-Ta0896; -. DR EnsemblBacteria; CAC12025; CAC12025; CAC12025. DR GeneID; 1456432; -. DR KEGG; tac:Ta0896; -. DR eggNOG; arCOG04120; Archaea. DR HOGENOM; CLU_015439_0_2_2; -. DR InParanoid; P32044; -. DR OrthoDB; 56298at2157; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000001024; 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 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; 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. PE 1: Evidence at protein level; KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase. FT CHAIN 1..544 FT /note="Pyruvate kinase" FT /id="PRO_0000112129" FT BINDING 31 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 33..36 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 33 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 61 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 68 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 204 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 227 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 228 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 228 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 260 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 202 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" SQ SEQUENCE 544 AA; 59147 MW; 7BD8BCAF4706A5B2 CRC64; MKTKIVATIG PASSSPEIMK QMIDNGLSLV RINSAHADIK DVSKITQMVR SINRDVGIMI DLKGPELRTG EFAGGTLKIS SGKDYVMGKD IVLNNMNVLS AVQVGDRILM SDGEVSFEVE STDPFTIRAL NDGVLRDRSR VNIPGRFIEL GTITDRDRAF IREGIADGVD FFALSFVQKS ENVDSLRDFV IDSGGDQYII SKIETKSGLD NIEEIVKSSD GIMVARGDLG VELPLKEVVL AQKHIIKTAH EDGDFTIVAT QVLESMVNNS SPTRAEISDI TNAIIDNADA LMLSEESAIG KYPVQAVRTL KEVSDYVEDK VSFDSSYYFK GNTIAYSVAR AAKILSDDIK SDGIVALTHT GSTVRMISSL RPKAMVYAAT VSESLARKLN IYFGVLPLHM EGNAEDLSFS EIMEYIVRSG RFADGSKLVM TSGDPYFTFG GTNDVKVAVV GKFIGRGYSF GDSLSGTATY GTKGDILMSE DGRIPGTDFR AFIFTSDIKP SLMSSLKGKT VVTKARLVRQ IKEGERIYID GNTGIILMAS PDQK //