ID   ADC_BURM9               Reviewed;         246 AA.
AC   A2RZY1; A2RZY0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Acetoacetate decarboxylase {ECO:0000255|HAMAP-Rule:MF_00597};
DE            Short=AAD {ECO:0000255|HAMAP-Rule:MF_00597};
DE            Short=ADC {ECO:0000255|HAMAP-Rule:MF_00597};
DE            EC=4.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00597};
GN   Name=adc {ECO:0000255|HAMAP-Rule:MF_00597};
GN   OrderedLocusNames=BMA10229_1447;
OS   Burkholderia mallei (strain NCTC 10229).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=412022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10229;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
CC   -!- FUNCTION: Catalyzes the conversion of acetoacetate to acetone and
CC       carbon dioxide. {ECO:0000255|HAMAP-Rule:MF_00597}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetoacetate + H(+) = acetone + CO2; Xref=Rhea:RHEA:19729,
CC         ChEBI:CHEBI:13705, ChEBI:CHEBI:15347, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526; EC=4.1.1.4; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00597};
CC   -!- SIMILARITY: Belongs to the ADC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00597}.
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DR   EMBL; CP000545; ABM99027.2; -; Genomic_DNA.
DR   RefSeq; WP_004194452.1; NC_008835.1.
DR   AlphaFoldDB; A2RZY1; -.
DR   SMR; A2RZY1; -.
DR   EnsemblBacteria; ABM99027; ABM99027; BMA10229_1447.
DR   GeneID; 56596762; -.
DR   KEGG; bml:BMA10229_1447; -.
DR   HOGENOM; CLU_077089_0_0_4; -.
DR   OMA; FEVMRMG; -.
DR   Proteomes; UP000002283; Chromosome II.
DR   GO; GO:0047602; F:acetoacetate decarboxylase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.400.10; -; 1.
DR   HAMAP; MF_00597; ADC; 1.
DR   InterPro; IPR010451; Acetoacetate_decarboxylase.
DR   InterPro; IPR023653; Acetoacetate_decarboxylase_bac.
DR   InterPro; IPR023375; ADC_dom_sf.
DR   Pfam; PF06314; ADC; 1.
DR   SUPFAM; SSF160104; SSF160104; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Schiff base.
FT   CHAIN           1..246
FT                   /note="Acetoacetate decarboxylase"
FT                   /id="PRO_1000025635"
FT   ACT_SITE        116
FT                   /note="Schiff-base intermediate with acetoacetate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00597"
SQ   SEQUENCE   246 AA;  27494 MW;  17710D946B0C7483 CRC64;
     MKPSQVRSKA FAMPLTSPAF PMGPYRFVNR EFLIITYRTD MDRLREIVPE PLEVKEPLVH
     YEFIRMPDST GFGDYTESGQ VIPVEYKGQP GGYTLAMYLN DHPPIAGGRE LWGFPKKLAQ
     PTLQTHIDTL LGTLDYGPVR VATGTMGYKH QELDLEEQAK RLAGANFLLK IIPHVDGSAR
     VCELVRYYLQ DIEMKGAWTG PASLQLAPHA LAPVADLPVL EIVEARHLLA DLTLGLGEVV
     YDYLAQ