KPYK_LEIME
ID KPYK_LEIME Reviewed; 499 AA.
AC Q27686;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=PYK;
OS Leishmania mexicana.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5665;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8078522; DOI=10.1016/0166-6851(94)90133-3;
RA Ernest I., Callens M., Opperdoes F.R., Michels P.A.M.;
RT "Pyruvate kinase of Leishmania mexicana mexicana. Cloning and analysis of
RT the gene, overexpression in Escherichia coli and characterization of the
RT enzyme.";
RL Mol. Biochem. Parasitol. 64:43-54(1994).
RN [2]
RP SEQUENCE REVISION TO SER-383; TYR-390; ARG-405 AND SER-406.
RA Michels P.A.M.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RC STRAIN=MHOM/BZ/84/BEL46;
RX PubMed=10448041; DOI=10.1006/jmbi.1999.2918;
RA Rigden D.J., Phillips S.E.V., Michels P.A.M., Fothergill-Gilmore L.A.;
RT "The structure of pyruvate kinase from Leishmania mexicana reveals details
RT of the allosteric transition and unusual effector specificity.";
RL J. Mol. Biol. 291:615-635(1999).
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 -!- ACTIVITY REGULATION: Activated by fructose 2,6-bisphosphate, activated
CC by the effector in a non cooperative manner.
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}.
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DR EMBL; X74944; CAA52898.2; -; Genomic_DNA.
DR PDB; 1PKL; X-ray; 2.35 A; A/B/C/D/E/F/G/H=1-499.
DR PDB; 3E0V; X-ray; 3.30 A; A/B/C/D/E/F=1-499.
DR PDB; 3E0W; X-ray; 3.10 A; A=1-499.
DR PDB; 3HQN; X-ray; 2.00 A; A/D=1-499.
DR PDB; 3HQO; X-ray; 3.40 A; A/B/C/K=1-499.
DR PDB; 3HQP; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-499.
DR PDB; 3HQQ; X-ray; 5.07 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-499.
DR PDB; 3IS4; X-ray; 2.10 A; A/B=1-499.
DR PDB; 3KTX; X-ray; 2.10 A; A/B=1-499.
DR PDB; 3PP7; X-ray; 2.35 A; A/B=2-499.
DR PDB; 3QV6; X-ray; 2.85 A; A/D=1-499.
DR PDB; 3QV7; X-ray; 2.70 A; A/B/C/D=1-499.
DR PDB; 3QV8; X-ray; 2.45 A; A/D=1-499.
DR PDB; 3SRK; X-ray; 2.65 A; A/B=1-499.
DR PDBsum; 1PKL; -.
DR PDBsum; 3E0V; -.
DR PDBsum; 3E0W; -.
DR PDBsum; 3HQN; -.
DR PDBsum; 3HQO; -.
DR PDBsum; 3HQP; -.
DR PDBsum; 3HQQ; -.
DR PDBsum; 3IS4; -.
DR PDBsum; 3KTX; -.
DR PDBsum; 3PP7; -.
DR PDBsum; 3QV6; -.
DR PDBsum; 3QV7; -.
DR PDBsum; 3QV8; -.
DR PDBsum; 3SRK; -.
DR AlphaFoldDB; Q27686; -.
DR SMR; Q27686; -.
DR BindingDB; Q27686; -.
DR ChEMBL; CHEMBL5149; -.
DR VEuPathDB; TriTrypDB:LmxM.34.0030; -.
DR BRENDA; 2.7.1.40; 2951.
DR UniPathway; UPA00109; UER00188.
DR EvolutionaryTrace; Q27686; -.
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; -; 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; ATP-binding; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Pyruvate; Transferase.
FT CHAIN 1..499
FT /note="Pyruvate kinase"
FT /id="PRO_0000112102"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 52..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 52
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 241
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 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 239
FT /note="Transition state stabilizer"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:3E0W"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:3HQN"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 58..75
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1PKL"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:3SRK"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:3HQN"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 249..255
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 272..289
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 311..323
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 340..357
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 360..369
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 377..392
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 405..412
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 426..431
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 438..442
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 445..448
FT /evidence="ECO:0007829|PDB:3HQN"
FT HELIX 455..467
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 476..482
FT /evidence="ECO:0007829|PDB:3HQN"
FT STRAND 485..489
FT /evidence="ECO:0007829|PDB:1PKL"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:3HQN"
SQ SEQUENCE 499 AA; 54405 MW; 7B8CB0F9D3EDEBA9 CRC64;
MSQLAHNLTL SIFDPVANYR AARIICTIGP STQSVEALKG LIQSGMSVAR MNFSHGSHEY
HQTTINNVRQ AAAELGVNIA IALDTKGPEI RTGQFVGGDA VMERGATCYV TTDPAFADKG
TKDKFYIDYQ NLSKVVRPGN YIYIDDGILI LQVQSHEDEQ TLECTVTNSH TISDRRGVNL
PGCDVDLPAV SAKDRVDLQF GVEQGVDMIF ASFIRSAEQV GDVRKALGPK GRDIMIICKI
ENHQGVQNID SIIEESDGIM VARGDLGVEI PAEKVVVAQK ILISKCNVAG KPVICATQML
ESMTYNPRPT RAEVSDVANA VFNGADCVML SGETAKGKYP NEVVQYMARI CLEAQSALNE
YVFFNSIKKL QHIPMSADEA VCSSAVNSVY ETKAKAMVVL SNTGRSARLV AKYRPNCPIV
CVTTRLQTCR QLNITQGVES VFFDADKLGH DEGKEHRVAA GVEFAKSKGY VQTGDYCVVI
HADHKVKGYA NQTRILLVE
