KPYM_XENLA
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 03-AUG-2022, entry version 123.
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}.
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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 CTD; 399448; -.
DR Xenbase; XB-GENE-485877; pkm.S.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 399448; Expressed in brain and 19 other 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 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 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
