KPYR_RAT
ID KPYR_RAT Reviewed; 574 AA.
AC P12928; P04763; Q64618;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Pyruvate kinase PKLR;
DE EC=2.7.1.40 {ECO:0000250|UniProtKB:P30613};
DE AltName: Full=L-PK;
DE AltName: Full=Pyruvate kinase isozymes L/R;
GN Name=Pklr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3654663; DOI=10.1016/s0021-9258(18)47947-1;
RA Noguchi T., Yamada K., Inoue H., Matsuda T., Tanaka T.;
RT "The L- and R-type isozymes of rat pyruvate kinase are produced from a
RT single gene by use of different promoters.";
RL J. Biol. Chem. 262:14366-14371(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3002799; DOI=10.1111/j.1432-1033.1986.tb09420.x;
RA Inoue H., Noguchi T., Tanaka T.;
RT "Complete amino acid sequence of rat L-type pyruvate kinase deduced from
RT the cDNA sequence.";
RL Eur. J. Biochem. 154:465-469(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3080337; DOI=10.1016/0014-5793(86)80138-7;
RA Lone Y.-C., Simon M.-P., Kahn A., Marie J.;
RT "Complete nucleotide and deduced amino acid sequences of rat L-type
RT pyruvate kinase.";
RL FEBS Lett. 195:97-100(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3309348; DOI=10.1016/0022-2836(87)90507-9;
RA Cognet M., Lone Y.C., Vaulont S., Kahn A., Marie J.;
RT "Structure of the rat L-type pyruvate kinase gene.";
RL J. Mol. Biol. 196:11-25(1987).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Pyruvate kinase that catalyzes the conversion of
CC phosphoenolpyruvate to pyruvate with the synthesis of ATP, and which
CC plays a key role in glycolysis. {ECO:0000250|UniProtKB:P30613}.
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:P30613};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18159;
CC Evidence={ECO:0000250|UniProtKB:P30613};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P30613};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P30613};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:P30613};
CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 1,6-
CC bisphosphate. {ECO:0000250|UniProtKB:P30613}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000250|UniProtKB:P30613}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P30613}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=R-type; Synonyms=PKR;
CC IsoId=P12928-1; Sequence=Displayed;
CC Name=L-type; Synonyms=PKL;
CC IsoId=P12928-2; Sequence=VSP_002884;
CC -!- MISCELLANEOUS: There are 4 isozymes of pyruvate kinase in mammals: L,
CC R, M1 and M2. L type is major isozyme in the liver, R is found in red
CC cells, M1 is the main form in muscle, heart and brain, and M2 is found
CC in early fetal tissues. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; M17091; AAA41882.1; -; Genomic_DNA.
DR EMBL; M17088; AAA41882.1; JOINED; Genomic_DNA.
DR EMBL; M17089; AAA41882.1; JOINED; Genomic_DNA.
DR EMBL; M17090; AAA41882.1; JOINED; Genomic_DNA.
DR EMBL; M17091; AAA41883.1; -; Genomic_DNA.
DR EMBL; M17088; AAA41883.1; JOINED; Genomic_DNA.
DR EMBL; M17089; AAA41883.1; JOINED; Genomic_DNA.
DR EMBL; M17090; AAA41883.1; JOINED; Genomic_DNA.
DR EMBL; M17685; AAA41881.1; -; mRNA.
DR EMBL; X05684; CAA29169.1; -; Genomic_DNA.
DR EMBL; M11709; AAA41880.1; -; mRNA.
DR PIR; A27427; KIRTPR.
DR PIR; A92940; KIRTPL.
DR RefSeq; NP_036756.3; NM_012624.3. [P12928-2]
DR RefSeq; XP_006232655.1; XM_006232593.3. [P12928-1]
DR PDB; 6ECH; X-ray; 2.19 A; A/B/C/D=34-574.
DR PDB; 6ECK; X-ray; 2.36 A; A/B=34-574.
DR PDBsum; 6ECH; -.
DR PDBsum; 6ECK; -.
DR AlphaFoldDB; P12928; -.
DR SMR; P12928; -.
DR IntAct; P12928; 1.
DR MINT; P12928; -.
DR STRING; 10116.ENSRNOP00000027700; -.
DR BindingDB; P12928; -.
DR ChEMBL; CHEMBL3089; -.
DR iPTMnet; P12928; -.
DR PhosphoSitePlus; P12928; -.
DR jPOST; P12928; -.
DR PaxDb; P12928; -.
DR PRIDE; P12928; -.
DR Ensembl; ENSRNOT00000027700; ENSRNOP00000027700; ENSRNOG00000020420. [P12928-1]
DR Ensembl; ENSRNOT00000103387; ENSRNOP00000093132; ENSRNOG00000020420. [P12928-2]
DR GeneID; 24651; -.
DR KEGG; rno:24651; -.
DR UCSC; RGD:3336; rat. [P12928-1]
DR CTD; 5313; -.
DR RGD; 3336; Pklr.
DR eggNOG; KOG2323; Eukaryota.
DR GeneTree; ENSGT00390000008859; -.
DR HOGENOM; CLU_015439_0_1_1; -.
DR InParanoid; P12928; -.
DR OMA; MVRVHHL; -.
DR OrthoDB; 933620at2759; -.
DR PhylomeDB; P12928; -.
DR TreeFam; TF300390; -.
DR Reactome; R-RNO-70171; Glycolysis.
DR SABIO-RK; P12928; -.
DR UniPathway; UPA00109; UER00188.
DR PRO; PR:P12928; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000020420; Expressed in duodenum and 14 other tissues.
DR ExpressionAtlas; P12928; baseline and differential.
DR Genevisible; P12928; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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; IDA:RGD.
DR GO; GO:0006754; P:ATP biosynthetic process; IDA:RGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:RGD.
DR GO; GO:0071872; P:cellular response to epinephrine stimulus; IEP:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:RGD.
DR GO; GO:0006096; P:glycolytic process; IDA:RGD.
DR GO; GO:0042866; P:pyruvate biosynthetic process; IDA:RGD.
DR GO; GO:0033198; P:response to ATP; IDA:RGD.
DR GO; GO:0051591; P:response to cAMP; IDA:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IDA:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0010226; P:response to lithium ion; IDA:RGD.
DR GO; GO:0010038; P:response to metal ion; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0051707; P:response to other organism; ISO:RGD.
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 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Alternative splicing; ATP-binding;
KW Glycolysis; Kinase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Potassium; Pyruvate;
KW Reference proteome; Transferase.
FT CHAIN 1..574
FT /note="Pyruvate kinase PKLR"
FT /id="PRO_0000112096"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 118..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 118
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 120
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 156
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 157
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 315
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 339
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 475..480
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 525
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 532
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 559..564
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT SITE 313
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00549"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT VAR_SEQ 1..33
FT /note="MSVQENTLPQQLWPWIFRSQKDLAKSALSGAPG -> ME (in isoform
FT L-type)"
FT /evidence="ECO:0000305"
FT /id="VSP_002884"
FT CONFLICT 130
FT /note="S -> Y (in Ref. 1; AAA41882/AAA41883)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="K -> R (in Ref. 1; AAA41882/AAA41883)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="R -> G (in Ref. 3; AAA41880)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="Q -> K (in Ref. 3; AAA41880)"
FT /evidence="ECO:0000305"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:6ECK"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 124..139
FT /evidence="ECO:0007829|PDB:6ECH"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:6ECH"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:6ECK"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:6ECH"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 224..232
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 266..277
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 291..301
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 317..321
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 323..329
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 337..343
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 349..363
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 385..397
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 414..431
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 434..444
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 451..465
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 479..485
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 490..498
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 500..505
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:6ECH"
FT HELIX 525..542
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 551..561
FT /evidence="ECO:0007829|PDB:6ECH"
FT STRAND 565..572
FT /evidence="ECO:0007829|PDB:6ECH"
SQ SEQUENCE 574 AA; 62200 MW; 6BBC544653C51380 CRC64;
MSVQENTLPQ QLWPWIFRSQ KDLAKSALSG APGGPAGYLR RASVAQLTQE LGTAFFQQQQ
LPAAMADTFL EHLCLLDIDS QPVAARSTSI IATIGPASRS VDRLKEMIKA GMNIARLNFS
HGSHEYHAES IANIREATES FATSPLSYRP VAIALDTKGP EIRTGVLQGG PESEVEIVKG
SQVLVTVDPK FQTRGDAKTV WVDYHNITRV VAVGGRIYID DGLISLVVQK IGPEGLVTEV
EHGGILGSRK GVNLPNTEVD LPGLSEQDLL DLRFGVQHNV DIIFASFVRK ASDVLAVRDA
LGPEGQNIKI ISKIENHEGV KKFDEILEVS DGIMVARGDL GIEIPAEKVF LAQKMMIGRC
NLAGKPVVCA TQMLESMITK ARPTRAETSD VANAVLDGAD CIMLSGETAK GSFPVEAVMM
QHAIAREAEA AVYHRQLFEE LRRAAPLSRD PTEVTAIGAV EASFKCCAAA IIVLTKTGRS
AQLLSQYRPR AAVIAVTRSA QAARQVHLSR GVFPLLYREP PEAIWADDVD RRVQFGIESG
KLRGFLRVGD LVIVVTGWRP GSGYTNIMRV LSVS
