ID   KPYK_STAA3              Reviewed;         585 AA.
AC   Q2FG40;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=Pyruvate kinase;
DE            Short=PK;
DE            EC=2.7.1.40;
GN   Name=pyk; OrderedLocusNames=SAUSA300_1644;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16517273; DOI=10.1016/S0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
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   -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the PEP-
CC       utilizing enzyme family.
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DR   EMBL; CP000255; ABD22512.1; -; Genomic_DNA.
DR   RefSeq; YP_494338.1; -.
DR   GeneID; 3914281; -.
DR   GenomeReviews; CP000255_GR; SAUSA300_1644.
DR   KEGG; saa:SAUSA300_1644; -.
DR   HOGENOM; Q2FG40; -.
DR   OMA; Q2FG40; ATESGYT.
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   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   InterPro; IPR008279; PEP_mobile.
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:3.50.30.10; PEP_mobile; 1.
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; PF00391; PEP-utilizers; 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; FALSE_NEG.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Pyruvate; Transferase.
FT   CHAIN         1    585       Pyruvate kinase.
FT                                /FTId=PRO_0000294136.
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).
SQ   SEQUENCE   585 AA;  63102 MW;  4AB45FDE55BF577D CRC64;
     MRKTKIVCTI GPASESEEMI EKLINAGMNV ARLNFSHGSH EEHKGRIDTI RKVAKRLDKI
     VAILLDTKGP EIRTHNMKDG IIELERGNEV IVSMNEVEGT PEKFSVTYEN LINDVQVGSY
     ILLDDGLIEL QVKDIDHAKK EVKCDILNSG ELKNKKGVNL PGVRVSLPGI TEKDAEDIRF
     GIKENVDFIA ASFVRRPSDV LEIREILEEQ KANISVFPKI ENQEGIDNIA EILEVSDGLM
     VARGDMGVEI PPEKVPMVQK DLIRQCNKLG KPVITATQML DSMQRNPRAT RAEASDVANA
     IYDGTDAVML SGETAAGLYP EEAVKTMRNI AVSAEAAQDY KKLLSDRTKL VETSLVNAIG
     ISVAHTALNL NVKAIVAATE SGSTARTISK YRPHSDIIAV TPSEETARQC SIVWGVQPVV
     KKGRKSTDAL LNNAVATAVE TGRVSNGDLI IITAGVPTGE TGTTNMMKIH LVGDEIANGQ
     GIGRGSVVGT TLVAETVKDL EGKDLSDKVI VTNSIDETFV PYVEKALGLI TEENGITSPS
     AIVGLEKGIP TVVGVEKAVK NISNNMLVTI DAAQGKIFEG YANVL
//