ID   KPYK_STAS1              Reviewed;         586 AA.
AC   Q49YC7;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Pyruvate kinase;
DE            Short=PK;
DE            EC=2.7.1.40;
GN   Name=pyk; OrderedLocusNames=SSP1069;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE18214.1; -; Genomic_DNA.
DR   RefSeq; YP_301159.1; -.
DR   GeneID; 3615437; -.
DR   GenomeReviews; AP008934_GR; SSP1069.
DR   KEGG; ssp:SSP1069; -.
DR   NMPDR; fig|342451.4.peg.1129; -.
DR   HOGENOM; Q49YC7; -.
DR   OMA; Q49YC7; ATESGYT.
DR   BioCyc; SSAP342451:SSP1069-MON; -.
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; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Pyruvate; Transferase.
FT   CHAIN         1    586       Pyruvate kinase.
FT                                /FTId=PRO_0000294140.
FT   ACT_SITE    220    220       By similarity.
FT   METAL       222    222       Magnesium (By similarity).
FT   METAL       243    243       Magnesium (By similarity).
FT   METAL       244    244       Magnesium (By similarity).
SQ   SEQUENCE   586 AA;  62853 MW;  FE093F0E7D948CAE CRC64;
     MRKTKIVCTI GPASESEEML EKLIKAGMNV ARLNFSHGDQ AEHKARIDTI RKVSKRLGKT
     VAILLDTKGP EIRTHNMKDG LIELEKGSEV TVSMTEVEGT PEKFSVTYEN LINDVEEGSY
     ILLDDGLIEL QVKSIDKANG EVLCDVLNTG ELKNKKGVNL PGVKVSLPGI TDKDADDINF
     GISEGVDFIA ASFVRRPSDV LDIRKLLEAK QNKNISIIPK IENQEGIDNI KEILEVSDGL
     MVARGDMGVE IPPESVPMVQ KDLIRQCNKL GKPVITATQM LDSMQRNPRA TRAEASDVAN
     AIYDGTDAVM LSGETAAGQY PEEAVKTMRN IAVSAEAAQD YKKLLSDRTK LVETSLVNAI
     GVSVAHTALN LNVKAIVAAT ESGSTARTIS KYRPQSDIIA VTPNAETARQ CALVWGIFPV
     VKEGRKTTDA LLNNAVATAV ETERVQNGDL IIITAGVPTG EKGTTNMMKL HLVGDELAKG
     QGIGRSSVVG KTLVVKDASE LEGKDLSESI IVTSSVDETL VPYIENAIGL ITEENGITSP
     SAIIGLEKGI PTVVGVENAT SEIQSDVLIT VDANQGKIFE GYANVL
//