ID KPYK_STAHJ Reviewed; 586 AA. AC Q4L739; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN Name=pyk; OrderedLocusNames=SH1227; OS Staphylococcus haemolyticus (strain JCSC1435). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=279808; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005; RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., RA Lee J.C., Hiramatsu K.; RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the RT extreme plasticity of its genome and the evolution of human-colonizing RT staphylococcal species."; RL J. Bacteriol. 187:7292-7308(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. 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; AP006716; BAE04536.1; -; Genomic_DNA. DR RefSeq; YP_253142.1; -. DR GeneID; 3481929; -. DR GenomeReviews; AP006716_GR; SH1227. DR KEGG; sha:SH1227; -. DR NMPDR; fig|279808.3.peg.2549; -. DR HOGENOM; Q4L739; -. DR OMA; Q4L739; ATESGYT. DR BioCyc; SHAE279808:SH1227-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 1 586 Pyruvate kinase. FT /FTId=PRO_0000294139. 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; 63019 MW; E6C0B61B47DCE8CE CRC64; MRKTKIVCTI GPASESEEML EKLMKAGMNV ARLNFSHGSH EEHKARIDTI RKVADRLGKT IGILLDTKGP EIRTHDMKDG LIMLEKGKEV IVSMSQVEGT PEKFSVTYED LINDVQVGSY ILLDDGLVEL QVKDIDKTKG EVKCDILNTG ELKNKKGVNL PGVKVNLPGI TDKDADDILF GIKEDVDYIA ASFVRRPSDV LDIREILERE NNHNITIFPK IENQEGIDNI EEILEVSDGL MVARGDMGVE IPPESVPIVQ KDLIRKCNKL GKPVITATQM LDSMQRNPRA TRAEASDVAN AIYDGTDAVM LSGETAAGLY PEEAVKTMRN IAVSAEAAQD YKKLLSDRTK LVETSLVNAI GVSVAHTALN LNVKAIVAAT ESGSTAVTIS KYRPHSDIIA VTPSEHTARQ LALVWGAYPV IKKGRKTTDD LLNNAVATAV ETGRVTNGDL IIITAGVPTG EKGTTNMMKL HLVGDEIAKG QGVGRGSVVG KTVVANSASD LEGVDLSESV IVTNSVDETL VPYIEQAVGL ITEENGITSP SAIIGLEKSI PTIIGVENAT KELKDGILVT VDAAQGKIFE GYANVL //