KPYK_LACLA
ID KPYK_LACLA Reviewed; 502 AA.
AC Q07637;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Pyruvate kinase;
DE Short=PK;
DE EC=2.7.1.40;
GN Name=pyk; OrderedLocusNames=LL1332; ORFNames=L0003;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LM0230;
RX PubMed=8478320; DOI=10.1128/jb.175.9.2541-2551.1993;
RA Llanos R.M., Harris C.J., Hillier A.J., Davidson B.E.;
RT "Identification of a novel operon in Lactococcus lactis encoding three
RT enzymes for lactic acid synthesis: phosphofructokinase, pyruvate kinase,
RT and lactate dehydrogenase.";
RL J. Bacteriol. 175:2541-2551(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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: Regulated by phosphoenolpyruvate substrate and is
CC allosterically activated by ribose-5-phosphate, AMP and other
CC nucleoside monophosphates but not by fructose-1,6-bisphosphate.
CC {ECO:0000250}.
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; L07920; AAA99895.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05430.1; -; Genomic_DNA.
DR PIR; B40620; B40620.
DR PIR; D86791; D86791.
DR RefSeq; NP_267488.1; NC_002662.1.
DR RefSeq; WP_003131076.1; NC_002662.1.
DR AlphaFoldDB; Q07637; -.
DR SMR; Q07637; -.
DR STRING; 272623.L0003; -.
DR MoonProt; Q07637; -.
DR PaxDb; Q07637; -.
DR PRIDE; Q07637; -.
DR EnsemblBacteria; AAK05430; AAK05430; L0003.
DR GeneID; 66442315; -.
DR KEGG; lla:L0003; -.
DR PATRIC; fig|272623.7.peg.1439; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_9; -.
DR OMA; QVPIVQK; -.
DR BioCyc; MetaCyc:MON-13043; -.
DR SABIO-RK; Q07637; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0009986; C:cell surface; IDA:CAFA.
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:2001065; F:mannan binding; IDA:CAFA.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004743; F:pyruvate kinase activity; IDA:CAFA.
DR GO; GO:0006116; P:NADH oxidation; IDA:CAFA.
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 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Potassium; Pyruvate; Reference proteome;
KW Transferase.
FT CHAIN 1..502
FT /note="Pyruvate kinase"
FT /id="PRO_0000112077"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 56..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 56
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 58
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 89
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 250
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 100
FT /note="A -> T (in Ref. 1; AAA99895)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="A -> S (in Ref. 1; AAA99895)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="I -> V (in Ref. 1; AAA99895)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="N -> D (in Ref. 1; AAA99895)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="T -> M (in Ref. 1; AAA99895)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="S -> A (in Ref. 1; AAA99895)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="S -> A (in Ref. 1; AAA99895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 54255 MW; 5A63C790B27E6B73 CRC64;
MNKRVKIVST LGPAVEIRGG KKFGESGYWG ESLDVEASAK NIAALIEEGA NVFRFNFSHG
DHPEQGARMA TVHRAEEIAG HKVGFLLDTK GPEMRTELFA DGADAISVVT GDKFRVATKQ
GLKSTPELIA LNVAGGLDIF DDVEIGQTIL IDDGKLGLSL TGKDAATREF EVEAQNDGVI
GKQKGVNIPN TKIPFPALAE RDDADIRFGL SQPGGINFIA ISFVRTANDV KEVRRICEET
GNPHVQLLAK IENQQGIENL DEIIEAADGI MIARGDMGIE VPFEMVPVYQ KLIISKVNKA
GKIVVTATNM LESMTYNPRA TRSEISDVFN AVIDGTDATM LSGESANGKY PRESVRTMAT
VNKNAQTMLK EYGRLHPERY DKSTVTEVVA ASVKNAAEAM DIKLIVALTE SGNTARLISK
HRPNADILAI TFDEKVERGL MINWGVIPTM TEKPSSTDDM FEVAEKVALA SGLVESGDNI
IIVAGVPVGT GRTNTMRIRT VK
