KPYC_SOLTU
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 03-AUG-2022, entry version 124.
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}.
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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.PGSC0003DMT400065094; -.
DR PRIDE; P22200; -.
DR GeneID; 102601328; -.
DR KEGG; sot:102601328; -.
DR eggNOG; KOG2323; Eukaryota.
DR OrthoDB; 933620at2759; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P22200; baseline and differential.
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 CDD; cd00288; Pyruvate_Kinase; 1.
DR Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.40.1380.20; -; 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; PTHR11817; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 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
