ID ACKA_BACCZ Reviewed; 397 AA. AC Q633F8; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 25-NOV-2008, entry version 30. DE RecName: Full=Acetate kinase; DE EC=2.7.2.1; DE AltName: Full=Acetokinase; GN Name=ackA; OrderedLocusNames=BCE33L4381; OS Bacillus cereus (strain ZK / E33L). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=288681; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., RA Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., RA Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). CC -!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate. CC -!- CATALYTIC ACTIVITY: ATP + propanoate = ADP + propanoyl phosphate. CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA CC biosynthesis; acetyl-CoA from acetate: step 1/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the acetokinase 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; CP000001; AAU15889.1; -; Genomic_DNA. DR RefSeq; YP_085959.1; -. DR GeneID; 3026500; -. DR GenomeReviews; CP000001_GR; BCE33L4381. DR KEGG; bcz:BCZK4381; -. DR HOGENOM; Q633F8; -. DR BioCyc; BCER288681:BCE33L4381-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0008776; F:acetate kinase activity; IEA:HAMAP. DR GO; GO:0006082; P:organic acid metabolic process; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:HAMAP. DR HAMAP; MF_00020; -; 1. DR InterPro; IPR000890; Acetate_kin. DR InterPro; IPR004372; AckA. DR PANTHER; PTHR21060; Acetate_kin; 1. DR PANTHER; PTHR21060:SF11; AckA; 1. DR Pfam; PF00871; Acetate_kinase; 1. DR PIRSF; PIRSF000722; Acetate_prop_kin; 1. DR PRINTS; PR00471; ACETATEKNASE. DR TIGRFAMs; TIGR00016; ackA; 1. DR PROSITE; PS01075; ACETATE_KINASE_1; 1. DR PROSITE; PS01076; ACETATE_KINASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Kinase; Transferase. FT CHAIN 1 397 Acetate kinase. FT /FTId=PRO_0000107528. SQ SEQUENCE 397 AA; 43232 MW; 3F8816167EBA9B99 CRC64; MSKIIAINAG SSSLKFQLFE MPSETVLTKG LVERIGLEDS IFTITVDGEK QKEITNIPDH AVAVNMLLKK LTENGIVKSL DEIGGIGHRV VHGGEKFADS VLITDEVLAD IEELSDLAPL HNPANVVGIK AFQEVLPNVP AVAVFDTAFH QTMPESAFLY SLPYEYYEKF GIRKYGFHGT SHKYVTERAA ELLGRPLESL SLLSCHLGNG ASIAAVEGGK SIDTSMGFTP LAGVTMGTRS GNIDPALIPY IMEKTGQTVE EVVNVLNKKS GMLGLTGYSS DLRDIIAKEE EGDHRAKVAL DVFVSRIHKY IGSYTARMKG VDAIIFTAGV GENSAIIRER VLEGLEYMGV YFDAKRNNVF GEEAFINFPH SPVKIIVIPT DEEVMIARDV LRLGNIG //