ID KPYK_TRYBO Reviewed; 498 AA.
AC Q27788; Q27789;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 13-SEP-2023, entry version 102.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=PYK;
OS Trypanoplasma borreli.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Parabodonida; Trypanoplasma.
OX NCBI_TaxID=5710;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8003008; DOI=10.1006/bbrc.1994.1761;
RA Ernest I., Opperdoes F.R., Michels P.A.M.;
RT "Cloning and sequence analysis of the gene encoding pyruvate kinase in
RT Trypanoplasma borelli.";
RL Biochem. Biophys. Res. Commun. 201:727-732(1994).
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; X77255; CAA54472.1; -; Genomic_DNA.
DR EMBL; X77255; CAA54473.1; -; Genomic_DNA.
DR PIR; JC2456; JC2456.
DR AlphaFoldDB; Q27788; -.
DR SMR; Q27788; -.
DR UniPathway; UPA00109; UER00188.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00288; Pyruvate_Kinase; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 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 NCBIfam; TIGR01064; pyruv_kin; 1.
DR PANTHER; PTHR11817:SF3; AT14039P-RELATED; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Transferase.
FT CHAIN 1..498
FT /note="Pyruvate kinase"
FT /id="PRO_0000112105"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 55..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 55
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 238
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 498 AA; 54634 MW; 7C5882430B93DE21 CRC64;
MMRKSQLQFN TELRVHHPPA LFRSNKIICT IGPSSQSVEV LKDLMKAGLN VARMNFSHGT
YEYHQKTIDN VRKAASELGI HVGIALDTKG PEIRTGLFPA GDVVIEAHKT VILTTDETFK
EKGTAEKFYV DYMNITKVVP VGGHIFVDDG LLDLIVVKIS GKDIECVAQN THTISNRKGI
NLPNADVDLP AVSEKDLMDL QFGAKNRVDF VFASFIRNAD QVNEVRQAFG GKIAVIAKIE
NYQGIDNIDA IIDAADGIMV ARGDLGVEIP AEKVVIAQKM IMSKCNKVGK TVICATQMLD
SMTHGPRPTR AEVSDVAKSV LDGADCVMLS GETAKGKYPV ETVVYMSRIC CETQVTMWNM
AAFEAIKNLQ SFPLIPEEAI CSSAVNSIFE LHAKAILVLT NTGRSAHMVS KYRPPVPIIC
ASQELDVCRL LSITRGTIPV YYDTEKLGPD YDREKRVGLA IDVGKQMGVF KEGDVVVAVH
ADHHTKGFAN QIRAIYIK
//
