ID KPYC_SOLTU Reviewed; 510 AA. AC P22200; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 27-MAR-2024, entry version 133. DE RecName: Full=Pyruvate kinase, cytosolic isozyme; DE Short=PK; DE EC=2.7.1.40; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum. OX NCBI_TaxID=4113; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Kennebec; TISSUE=Tuber; RX PubMed=2102383; DOI=10.1007/bf00017842; RA Blakeley S.D., Plaxton W.C., Dennis D.T.; RT "Cloning and characterization of a cDNA for the cytosolic isozyme of plant RT pyruvate kinase: the relationship between the plant and non-plant enzyme."; RL Plant Mol. Biol. 15:665-669(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1487141; DOI=10.1016/0378-1119(92)90213-9; RA Cole K.P., Blakeley S.D., Dennis D.T.; RT "Structure of the gene encoding potato cytosolic pyruvate kinase."; RL Gene 122:255-261(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 -!- SUBCELLULAR LOCATION: Cytoplasm. 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; X53688; CAA37727.1; -; mRNA. DR PIR; JC1481; JC1481. DR RefSeq; NP_001275085.1; NM_001288156.1. DR AlphaFoldDB; P22200; -. DR SMR; P22200; -. DR STRING; 4113.P22200; -. DR PaxDb; 4113-PGSC0003DMT400065094; -. DR GeneID; 102601328; -. DR KEGG; sot:102601328; -. DR eggNOG; KOG2323; Eukaryota. DR InParanoid; P22200; -. DR OrthoDB; 5483908at2759; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000011115; Unassembled WGS sequence. DR ExpressionAtlas; P22200; baseline. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. 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; PYRUVATE KINASE; 1. DR PANTHER; PTHR11817:SF131; PYRUVATE KINASE, CYTOSOLIC ISOZYME; 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; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase. FT CHAIN 1..510 FT /note="Pyruvate kinase, cytosolic isozyme" FT /id="PRO_0000112124" FT BINDING 50 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 52..55 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 52 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 54 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 84 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 85 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000250" FT BINDING 91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 176 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P14618" FT BINDING 242 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255" FT BINDING 265 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 266 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 266 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 298 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 240 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT VARIANT 133 FT /note="M -> V" FT VARIANT 169 FT /note="T -> S" FT VARIANT 227 FT /note="V -> A" FT VARIANT 309 FT /note="A -> R" SQ SEQUENCE 510 AA; 55170 MW; 1752C9ED920F2854 CRC64; MANIDIAGIM KDLPNDGRIP KTKIVCTLGP SSRTVPMLEK LLRAGMNVAR FNFSHGTHEY HQETLDNLKI AMQNTQILCA VMLDTKGPEI RTGFLTDGKP IQLKEGQEIT VSTDYTIKGN EEMISMSYKK LVMDLKPGNT ILCADGTITL TVLSCDPPSG TVRCRCENTA TLGERKNVNL PGVVVDLPTL TEKDKEDILE WGVPNNIDMI ALSFVRKGSD LVNVRKVLGP HAKRIQLMSK VENQEGVINF DEILRETDSF MVARGDLGME IPVEKIFLAQ KMMIYKCNLA GKAVVTATQM LESMIKSPAP TRAEATDVAN AVLDGTDCVM LSGESAAGAY PELAVKIMSR ICIEAESSLD NEAIFKEMIR CTPLPMSPLE SLASSAVRTA NKARAKLIVV LTRGGSTAKL VAKYRPAVPI LSVVVPVLTT DSFDWSISDE TPARHSLVYR GLIPLLGEGS AKATDSESTE VILEAALKSA VTRGLCKPGD AVVALHRIGS ASVIKICVVK //