ID DKE1_ACIJO Reviewed; 153 AA. AC Q8GNT2; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 20-JAN-2009, entry version 29. DE RecName: Full=Acetylacetone-cleaving enzyme; DE EC=1.13.11.50; DE AltName: Full=Acetylacetone dioxygenase; DE AltName: Full=Diketone cleaving dioxygenase; DE AltName: Full=Diketone cleaving enzyme; GN Name=dke1; OS Acinetobacter johnsonii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=40214; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, RP CHARACTERIZATION, AND MASS SPECTROMETRY. RC STRAIN=DSMZ 98-849; RX PubMed=12379146; DOI=10.1042/BJ20021047; RA Straganz G.D., Glieder A., Brecker L., Ribbons D.W., Steiner W.; RT "Acetylacetone-cleaving enzyme Dke1: a novel C-C-bond-cleaving enzyme RT from Acinetobacter johnsonii."; RL Biochem. J. 369:573-581(2003). CC -!- FUNCTION: Cleaves acetylacetone to equimolar amounts of CC methylglyoxal and acetate, consuming one equivalent of molecular CC oxygen. CC -!- CATALYTIC ACTIVITY: Pentane-2,4-dione + O(2) = acetate + 2- CC oxopropanal. CC -!- COFACTOR: Binds 1 iron ion per subunit. CC -!- PATHWAY: Xenobiotic degradation; acetylacetone degradation. CC -!- SUBUNIT: Homotetramer. CC -!- MASS SPECTROMETRY: Mass=16607; Method=MALDI; Range=1-153; CC Source=PubMed:12379146; 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; AF489107; AAN45859.1; -; Genomic_DNA. DR PDB; 3BAL; X-ray; 1.95 A; A/B/C/D=1-153. DR PDBsum; 3BAL; -. DR BRENDA; 1.13.11.50; 74504. DR GO; GO:0033752; F:acetylacetone-cleaving enzyme activity; IEA:EC. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW 3D-structure; Dioxygenase; Direct protein sequencing; Iron; KW Metal-binding; Oxidoreductase. FT CHAIN 1 153 Acetylacetone-cleaving enzyme. FT /FTId=PRO_0000079925. FT STRAND 12 15 FT HELIX 18 20 FT HELIX 26 28 FT STRAND 29 31 FT STRAND 34 41 FT TURN 42 45 FT STRAND 46 53 FT STRAND 57 59 FT STRAND 62 66 FT STRAND 68 79 FT HELIX 83 85 FT STRAND 87 98 FT STRAND 103 105 FT STRAND 108 111 FT STRAND 113 121 FT STRAND 123 126 FT STRAND 132 136 FT HELIX 138 148 SQ SEQUENCE 153 AA; 16607 MW; F3FBCB762E8F250F CRC64; MDYCNKKHTA EEYVKISDNN YVPFPEAFSD GGITWQLLHS SPETSSWTAI FNCPAGSSFA SHIHAGPGEY FLTKGKMEVR GGEQEGGSTA YAPSYGFESS GALHGKTFFP VESQFYMTFL GPLNFIDDNG KVIASIGWAE AQGAWLATKN EAA //