ID   KPYK_CLOPE              Reviewed;         474 AA.
AC   Q46289;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 2.
DT   16-JUN-2009, entry version 71.
DE   RecName: Full=Pyruvate kinase;
DE            Short=PK;
DE            EC=2.7.1.40;
GN   Name=pykF; OrderedLocusNames=CPE2149;
OS   Clostridium perfringens.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1502;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   MEDLINE=21664373; PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A.,
RA   Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic
RT   flesh-eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
RC   STRAIN=CPN50;
RX   MEDLINE=96032407; PubMed=7559358;
RA   Katayama S., Dupuy B., Garnier T., Cole S.T.;
RT   "Rapid expansion of the physical and genetic map of the chromosome of
RT   Clostridium perfringens CPN50.";
RL   J. Bacteriol. 177:5680-5685(1995).
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- COFACTOR: Potassium (By 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BA000016; BAB81855.1; -; Genomic_DNA.
DR   EMBL; X86495; CAA60217.1; -; Genomic_DNA.
DR   RefSeq; NP_563065.1; -.
DR   HSSP; P14178; 1E0T.
DR   GeneID; 990464; -.
DR   GenomeReviews; BA000016_GR; CPE2149.
DR   KEGG; cpe:CPE2149; -.
DR   NMPDR; fig|195102.1.peg.2212; -.
DR   HOGENOM; Q46289; -.
DR   OMA; Q46289; PLRISKF.
DR   BioCyc; CPER195102:CPE2149-MON; -.
DR   BRENDA; 2.7.1.40; 2406.
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   ATP-binding; Complete proteome; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Pyruvate; Transferase.
FT   CHAIN         1    474       Pyruvate kinase.
FT                                /FTId=PRO_0000112066.
FT   ACT_SITE    219    219       By similarity.
FT   METAL       221    221       Magnesium (By similarity).
FT   METAL       242    242       Magnesium (By similarity).
FT   METAL       243    243       Magnesium (By similarity).
FT   CONFLICT     17     17       E -> G (in Ref. 2; CAA60217).
FT   CONFLICT     45     45       E -> G (in Ref. 2; CAA60217).
FT   CONFLICT     57     57       E -> G (in Ref. 2; CAA60217).
SQ   SEQUENCE   474 AA;  52082 MW;  387970D750B2B39B CRC64;
     MQKTKMIFTI GPSSDSEEIL REFIRIGMNA ARLNFSHGDH ASHKEKIELI KRLRKEEKSA
     TAILLDIKGP KIRTYNFKNG EAELKNGDEF TFSCGDEILG DNTKCSISYK ELYEDIKPGG
     SILVDDGLLE FKVKEVRGTD IICEVIEGGT IKDHKGVNVP NVPIKLPAVT EKDRSDLIFG
     CEMEVDFVAA SFIRKPEDVL EVREILDSHG GKDIKIISKI ESQEGVDNIK EIIKVTDGVM
     VARGDMGVEI PIENVPIIQK NIIKKCNQAG KIVITATQML DSMIRNPRPT RAEASDVCNA
     IFDGTDAIML SGESASGSFP IEAAMTMSRI AKKAEANLDY NYLLRRLKDP NPNPDAFADA
     ISYSASKTAS KFPTKAIVAA TQTGSTAKIL SKYKPSCPII AITPYEKVRR SLALNFGIIS
     KKCAYFNSTD EIIEEARKVA KEFEIAETGD NIMVAAGFPT SITGGTNMLK IEKI
//