KPYK_THEAC
ID KPYK_THEAC Reviewed; 544 AA.
AC P32044;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN OrderedLocusNames=Ta0896;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP CHARACTERIZATION.
RX PubMed=1426985; DOI=10.1016/0378-1097(92)90636-3;
RA Potter S., Fothergill-Gilmore L.A.;
RT "Purification and properties of pyruvate kinase from Thermoplasma
RT acidophilum.";
RL FEMS Microbiol. Lett. 73:235-239(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 -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
CC -!- CAUTION: PubMed:1426985 has published some partial sequence, these
CC sequences do not originate from T.acidophilum, rather they seem to be
CC contaminated with human samples. {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; AL445065; CAC12025.1; -; Genomic_DNA.
DR RefSeq; WP_010901306.1; NC_002578.1.
DR AlphaFoldDB; P32044; -.
DR SMR; P32044; -.
DR STRING; 273075.Ta0896; -.
DR EnsemblBacteria; CAC12025; CAC12025; CAC12025.
DR GeneID; 1456432; -.
DR KEGG; tac:Ta0896; -.
DR eggNOG; arCOG04120; Archaea.
DR HOGENOM; CLU_015439_0_2_2; -.
DR OMA; QVPIVQK; -.
DR OrthoDB; 40634at2157; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000001024; Chromosome.
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 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; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Reference proteome; Transferase.
FT CHAIN 1..544
FT /note="Pyruvate kinase"
FT /id="PRO_0000112129"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 33..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 33
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 202
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 544 AA; 59147 MW; 7BD8BCAF4706A5B2 CRC64;
MKTKIVATIG PASSSPEIMK QMIDNGLSLV RINSAHADIK DVSKITQMVR SINRDVGIMI
DLKGPELRTG EFAGGTLKIS SGKDYVMGKD IVLNNMNVLS AVQVGDRILM SDGEVSFEVE
STDPFTIRAL NDGVLRDRSR VNIPGRFIEL GTITDRDRAF IREGIADGVD FFALSFVQKS
ENVDSLRDFV IDSGGDQYII SKIETKSGLD NIEEIVKSSD GIMVARGDLG VELPLKEVVL
AQKHIIKTAH EDGDFTIVAT QVLESMVNNS SPTRAEISDI TNAIIDNADA LMLSEESAIG
KYPVQAVRTL KEVSDYVEDK VSFDSSYYFK GNTIAYSVAR AAKILSDDIK SDGIVALTHT
GSTVRMISSL RPKAMVYAAT VSESLARKLN IYFGVLPLHM EGNAEDLSFS EIMEYIVRSG
RFADGSKLVM TSGDPYFTFG GTNDVKVAVV GKFIGRGYSF GDSLSGTATY GTKGDILMSE
DGRIPGTDFR AFIFTSDIKP SLMSSLKGKT VVTKARLVRQ IKEGERIYID GNTGIILMAS
PDQK
