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   03-AUG-2022, entry version 68.
DE   RecName: Full=Acetylacetone-cleaving enzyme;
DE            EC=1.13.11.50 {ECO:0000269|PubMed:12379146};
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; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=40214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP   CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, CHARACTERIZATION, AND MASS
RP   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 from
RT   Acinetobacter johnsonii.";
RL   Biochem. J. 369:573-581(2003).
CC   -!- FUNCTION: Cleaves acetylacetone to equimolar amounts of methylglyoxal
CC       and acetate, consuming one equivalent of molecular oxygen.
CC       {ECO:0000269|PubMed:12379146}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetylacetone + O2 = acetate + H(+) + methylglyoxal;
CC         Xref=Rhea:RHEA:12877, ChEBI:CHEBI:14750, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17158, ChEBI:CHEBI:30089;
CC         EC=1.13.11.50; Evidence={ECO:0000269|PubMed:12379146};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000269|PubMed:12379146};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:12379146};
CC   -!- PATHWAY: Xenobiotic degradation; acetylacetone degradation.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12379146}.
CC   -!- MASS SPECTROMETRY: Mass=16607; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12379146};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) 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   AlphaFoldDB; Q8GNT2; -.
DR   SMR; Q8GNT2; -.
DR   KEGG; ag:AAN45859; -.
DR   BioCyc; MetaCyc:MON-16107; -.
DR   BRENDA; 1.13.11.50; 103.
DR   UniPathway; UPA00734; -.
DR   EvolutionaryTrace; Q8GNT2; -.
DR   GO; GO:0033752; F:acetylacetone-cleaving enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Dioxygenase; Direct protein sequencing; Iron; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN           1..153
FT                   /note="Acetylacetone-cleaving enzyme"
FT                   /id="PRO_0000079925"
FT   STRAND          12..15
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   HELIX           18..20
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   STRAND          34..41
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   TURN            42..45
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   STRAND          46..53
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   STRAND          62..66
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   STRAND          68..79
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   STRAND          87..98
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   STRAND          113..121
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   STRAND          123..126
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   STRAND          132..136
FT                   /evidence="ECO:0007829|PDB:3BAL"
FT   HELIX           138..148
FT                   /evidence="ECO:0007829|PDB:3BAL"
SQ   SEQUENCE   153 AA;  16607 MW;  F3FBCB762E8F250F CRC64;
     MDYCNKKHTA EEYVKISDNN YVPFPEAFSD GGITWQLLHS SPETSSWTAI FNCPAGSSFA
     SHIHAGPGEY FLTKGKMEVR GGEQEGGSTA YAPSYGFESS GALHGKTFFP VESQFYMTFL
     GPLNFIDDNG KVIASIGWAE AQGAWLATKN EAA