ID KPYM_XENLA Reviewed; 527 AA. AC Q92122; Q68FC1; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 129. DE RecName: Full=Pyruvate kinase PKM; DE EC=2.7.1.40; DE AltName: Full=Cytosolic thyroid hormone-binding protein; DE Short=CTHBP; GN Name=pkm; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Intestine; RX PubMed=7957964; DOI=10.1016/0014-5793(94)01173-7; RA Shi Y.-B., Liang V.C.-T., Parkison C., Cheng S.-Y.; RT "Tissue-dependent developmental expression of a cytosolic thyroid hormone RT protein gene in Xenopus: its role in the regulation of amphibian RT metamorphosis."; RL FEBS Lett. 355:61-64(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Heart; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Glycolytic enzyme that catalyzes the transfer of a phosphoryl CC group from phosphoenolpyruvate (PEP) to ADP, generating ATP. CC {ECO:0000250|UniProtKB:P14618}. 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:0000250|UniProtKB:P14618}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P14618}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000250|UniProtKB:P14618}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P14618}. CC -!- DEVELOPMENTAL STAGE: Expressed in all stages of tadpole development. In CC the tail, high levels found in the premetamorphic stage (levels 54-60). CC Levels decrease with tail resorption. In the hindlimb, low expression CC during limb morphogenesis (stages 54-56), increased levels with limb CC growth (stages 58-66). Levels increase only slightly during intestine CC remodeling. {ECO:0000269|PubMed:7957964}. 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; U03878; AAA63581.1; -; mRNA. DR EMBL; BC079921; AAH79921.1; -; mRNA. DR RefSeq; NP_001084341.1; NM_001090872.1. DR AlphaFoldDB; Q92122; -. DR SMR; Q92122; -. DR BioGRID; 100773; 2. DR DNASU; 399448; -. DR GeneID; 399448; -. DR KEGG; xla:399448; -. DR AGR; Xenbase:XB-GENE-485877; -. DR CTD; 399448; -. DR Xenbase; XB-GENE-485877; pkm.S. DR OrthoDB; 312683at2759; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000186698; Chromosome 3S. DR Bgee; 399448; Expressed in brain and 19 other cell types or tissues. 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; 2. 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; PYRUVATE KINASE; 1. DR PANTHER; PTHR11817:SF101; PYRUVATE KINASE PKM; 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 2: Evidence at transcript level; KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase. FT CHAIN 1..527 FT /note="Pyruvate kinase PKM" FT /id="PRO_0000112098" FT BINDING 69 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 71..74 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 71 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 73 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 109 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 110 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 203 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 266 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 268 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 291 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 292 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 292 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 324 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P30613" FT BINDING 428..433 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 478 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 485 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 512..517 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000250|UniProtKB:P14618" FT SITE 266 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P00549" SQ SEQUENCE 527 AA; 57525 MW; A8379F0E65325A66 CRC64; MSEAGSAFIQ TQQLHAAMAD TFLEHMCRLD IDSEPIVARN TGIICTIGPA SRSVEMLKEM IKSGMNIARL NFSHGTHEYH AGTIKNVREA TESLASNPIH YRPVAVALDT KGPEIRTGLI KGSGTAEVEL KKGATMRITL DDAFQENCDE NVLWVDYKNL TKVVKPGSKI YVDDGLISLL VKEIGPDFCV TEIENGGMLG SKKGVNLPGA AVDLPAVSSK DIQDLQFGVE QDVDMVFASF IRKAADVHEV REVLGEKGKN IKIISKIENH EGVRRFDEIL EASDGIMVAR GDLGIEIPAE KVFLAQKMMI GRCNRAGKPV ICATQMLESM IKKPRPTRAE GSDVANAVLD GADCIMLSGE TAKGDYPLEA VRMQHAIARE AEAAIFHRQL FEELRRVSPL TRDPTEATAV GAVEASFKCS SGAIIVLTKS GRSAHLLSRY RPRAPIISVT RNGQTARQAH LYRGIFPVLY REAVHEAWAE DVDSRVNFAM DIGKARGFFK SGDVVIVLTG WRPGSGFTNT MRVVPVP //