ID KPYK_STAES Reviewed; 585 AA. AC Q8CS69; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 16-JUN-2009, entry version 37. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; OrderedLocusNames=SE_1373; OS Staphylococcus epidermidis (strain ATCC 12228). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=176280; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22832016; PubMed=12950922; RX DOI=10.1046/j.1365-2958.2003.03671.x; RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., RA Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., RA Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.; RT "Genome-based analysis of virulence genes in a non-biofilm-forming RT Staphylococcus epidermidis strain (ATCC 12228)."; RL Mol. Microbiol. 49:1577-1593(2003). 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. 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; AE015929; AAO04972.1; -; Genomic_DNA. DR RefSeq; NP_764928.1; -. DR HSSP; P14178; 1E0T. DR GeneID; 1058009; -. DR GenomeReviews; AE015929_GR; SE_1373. DR KEGG; sep:SE1373; -. DR HOGENOM; Q8CS69; -. DR OMA; Q8CS69; ATESGYT. DR BioCyc; SEPI176280:SE_1373-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; 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_0000294137. 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; 63033 MW; 7756EDD80D49128C CRC64; MRKTKIVCTI GPASESEEML EKLMNAGMNV ARLNFSHGSH EEHKARIDTI RKVAKRLNKT IGLLLDTKGP EIRTHNMKDG LIVLEKGKEV IVSMNEVEGT PEKFSVTYEN LINDVNIGSY ILLDDGLVEL QVKEINKDKG EVKCDILNTG ELKNKKGVNL PGVKVNLPGI TDKDADDIRF GIKENVDFIA ASFVRRPSDV LDIRQILEEE KAEITIFPKI ENQEGIDNIE EILEVSDGLM VARGDMGVEI PPESVPMVQK DLIRKCNKLG KPVITATQML DSMQRNPRAT RAEASDVANA IYDGTDAVML SGETAAGQYP EEAVKTMRNI AVSAEAAQDY KKLLSDRTKL VETSLVNAIG VSVAHTALNL NVKAIVAATE SGSTARTISK YRPHSDIIAV TPSEKTARQC AIVWGVNPVV KEGRKTTDAL LNNAVATAVE TGRVSNGDLI IITAGVPTGE KGTTNMMKIH LVGDEIAKGQ GVGRGSVVGH AIVADSASDL EGKDLSDKVI ITNSVDETLV PYVEKAIGLI TEENGITSPS AIIGLEKGIP TVVGVEQATK EIKNDMLVTL DASQGKVFEG YANVL //