KPYM_CHICK
ID KPYM_CHICK Reviewed; 530 AA.
AC P00548;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Pyruvate kinase PKM;
DE EC=2.7.1.40 {ECO:0000250|UniProtKB:P14618};
GN Name=PKM;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6574503; DOI=10.1073/pnas.80.12.3661;
RA Lonberg N., Gilbert W.;
RT "Primary structure of chicken muscle pyruvate kinase mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3661-3665(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2981634; DOI=10.1016/0092-8674(85)90311-3;
RA Lonberg N., Gilbert W.;
RT "Intron/exon structure of the chicken pyruvate kinase gene.";
RL Cell 40:81-90(1985).
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 -!- ACTIVITY REGULATION: Allosterically activated by fructose 1,6-
CC bisphosphate. {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 -!- MISCELLANEOUS: This activity is regulated by glucose levels.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; J00903; AAA49021.1; -; mRNA.
DR EMBL; M18793; AAA49020.1; -; Genomic_DNA.
DR EMBL; M10619; AAA49020.1; JOINED; Genomic_DNA.
DR EMBL; M18788; AAA49020.1; JOINED; Genomic_DNA.
DR EMBL; M18789; AAA49020.1; JOINED; Genomic_DNA.
DR EMBL; M18790; AAA49020.1; JOINED; Genomic_DNA.
DR EMBL; M18791; AAA49020.1; JOINED; Genomic_DNA.
DR EMBL; M18792; AAA49020.1; JOINED; Genomic_DNA.
DR PIR; I50408; KICHPM.
DR RefSeq; NP_990800.1; NM_205469.1.
DR AlphaFoldDB; P00548; -.
DR SMR; P00548; -.
DR BioGRID; 676705; 2.
DR IntAct; P00548; 1.
DR STRING; 9031.ENSGALP00000034108; -.
DR PaxDb; P00548; -.
DR PRIDE; P00548; -.
DR Ensembl; ENSGALT00000003100; ENSGALP00000003096; ENSGALG00000001992.
DR GeneID; 396456; -.
DR KEGG; gga:396456; -.
DR CTD; 5313; -.
DR VEuPathDB; HostDB:geneid_396456; -.
DR eggNOG; KOG2323; Eukaryota.
DR GeneTree; ENSGT00390000008859; -.
DR InParanoid; P00548; -.
DR OrthoDB; 933620at2759; -.
DR PhylomeDB; P00548; -.
DR Reactome; R-GGA-352882; Glycolysis.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR Reactome; R-GGA-70171; Glycolysis.
DR UniPathway; UPA00109; UER00188.
DR PRO; PR:P00548; -.
DR Proteomes; UP000000539; Chromosome 10.
DR Bgee; ENSGALG00000001992; Expressed in muscle tissue and 13 other tissues.
DR ExpressionAtlas; P00548; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0032869; P:cellular response to insulin stimulus; 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; -; 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 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 Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium; Pyruvate;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P11979"
FT CHAIN 2..530
FT /note="Pyruvate kinase PKM"
FT /id="PRO_0000112097"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 74..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 74
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 76
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 112
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 113
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 431..436
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 481
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 488
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 515..520
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 269
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00549"
SQ SEQUENCE 530 AA; 58015 MW; 8B0DF09FD82EB72F CRC64;
MSKHHDAGTA FIQTQQLHAA MADTFLEHMC RLDIDSEPTI ARNTGIICTI GPASRSVDKL
KEMIKSGMNV ARLNFSHGTH EYHEGTIKNV REATESFASD PITYRPVAIA LDTKGPEIRT
GLIKGSGTAE VELKKGAALK VTLDNAFMEN CDENVLWVDY KNLIKVIDVG SKIYVDDGLI
SLLVKEKGKD FVMTEVENGG MLGSKKGVNL PGAAVDLPAV SEKDIQDLKF GVEQNVDMVF
ASFIRKAADV HAVRKVLGEK GKHIKIISKI ENHEGVRRFD EIMEASDGIM VARGDLGIEI
PAEKVFLAQK MMIGRCNRAG KPIICATQML ESMIKKPRPT RAEGSDVANA VLDGADCIML
SGETAKGDYP LEAVRMQHAI AREAEAAMFH RQQFEEILRH SVHHREPADA MAAGAVEASF
KCLAAALIVM TESGRSAHLV SRYRPRAPII AVTRNDQTAR QAHLYRGVFP VLCKQPAHDA
WAEDVDLRVN LGMNVGKARG FFKTGDLVIV LTGWRPGSGY TNTMRVVPVP
