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   16-JUN-2009, entry version 70.
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 (Streptococcus lactis).
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LM0230;
RX   MEDLINE=93239679; PubMed=8478320;
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
RT   kinase, and lactate dehydrogenase.";
RL   J. Bacteriol. 175:2541-2551(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   MEDLINE=21235186; PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K.,
RA   Weissenbach J., 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: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC   -!- COFACTOR: Magnesium.
CC   -!- COFACTOR: Potassium.
CC   -!- ENZYME REGULATION: Regulated by phosphoenolpyruvate substrate and
CC       is allosterically activated by ribose-5-phosphate, AMP and other
CC       nucleoside monophosphates but not by fructose-1,6-bisphosphate (By
CC       similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family.
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DR   EMBL; L07920; AAA99895.1; -; Genomic_DNA.
DR   EMBL; AE006365; AAK05430.1; -; Genomic_DNA.
DR   PIR; B40620; B40620.
DR   PIR; D86791; D86791.
DR   RefSeq; NP_267488.1; -.
DR   HSSP; P14178; 1E0T.
DR   GeneID; 1114982; -.
DR   GenomeReviews; AE005176_GR; LL1332.
DR   KEGG; lla:L0003; -.
DR   NMPDR; fig|272623.1.peg.1367; -.
DR   HOGENOM; Q07637; -.
DR   OMA; Q07637; WVSKSQR.
DR   BioCyc; LLAC272623:L0003-MON; -.
DR   BioCyc; MetaCyc:MON-13043; -.
DR   BRENDA; 2.7.1.40; 278870.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0004743; F:pyruvate kinase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase_cat.
DR   InterPro; IPR015794; Pyrv_Knase_a/b.
DR   InterPro; IPR018209; Pyrv_Knase_AS.
DR   InterPro; IPR015793; Pyrv_Knase_brl.
DR   Gene3D; G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
DR   Gene3D; G3DSA:3.40.1380.20; Pyrv_Knase_a/b; 1.
DR   PANTHER; PTHR11817; Pyruvate_kinase; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   ProDom; PD001009; Pyruvate_kinase; 2.
DR   TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; ATP-binding; Complete proteome; Glycolysis; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Pyruvate; Transferase.
FT   CHAIN         1    502       Pyruvate kinase.
FT                                /FTId=PRO_0000112077.
FT   ACT_SITE    250    250       By similarity.
FT   METAL       252    252       Magnesium (By similarity).
FT   METAL       273    273       Magnesium (By similarity).
FT   METAL       274    274       Magnesium (By similarity).
FT   CONFLICT    100    100       A -> T (in Ref. 1; AAA99895).
FT   CONFLICT    105    105       A -> S (in Ref. 1; AAA99895).
FT   CONFLICT    402    402       I -> V (in Ref. 1; AAA99895).
FT   CONFLICT    424    424       N -> D (in Ref. 1; AAA99895).
FT   CONFLICT    449    449       T -> M (in Ref. 1; AAA99895).
FT   CONFLICT    455    455       S -> A (in Ref. 1; AAA99895).
FT   CONFLICT    476    476       S -> A (in Ref. 1; AAA99895).
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
//