ID   ADC_CLOBB               Reviewed;         246 AA.
AC   B2TLN8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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}; OrderedLocusNames=CLL_A2135;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001056; ACD22518.1; -; Genomic_DNA.
DR   RefSeq; WP_012423368.1; NC_018648.1.
DR   AlphaFoldDB; B2TLN8; -.
DR   SMR; B2TLN8; -.
DR   PRIDE; B2TLN8; -.
DR   EnsemblBacteria; ACD22518; ACD22518; CLL_A2135.
DR   KEGG; cbk:CLL_A2135; -.
DR   PATRIC; fig|935198.13.peg.2090; -.
DR   HOGENOM; CLU_077089_0_0_9; -.
DR   OMA; FEVMRMG; -.
DR   OrthoDB; 978501at2; -.
DR   Proteomes; UP000001195; Chromosome.
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_1000129879"
FT   ACT_SITE        116
FT                   /note="Schiff-base intermediate with acetoacetate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00597"
SQ   SEQUENCE   246 AA;  27800 MW;  A56D0A1C4F85FC96 CRC64;
     MLKSEVSKQI TTPLTAPAFP RGPYRFHNRE YFNIIYRTDA DALRKIVPEP LELGEDPLVR
     FEMMAMPDTS GLGSYTECGQ AIPVSYNGKK GDYLHMMYLD NQPAIAVGRE LSAYPKKLGY
     PKLFVDSDTL VGTLDYGKLR VAIATMGYKH KQLDLNEAKE QICRPNFMLK IIPNYDGTPR
     ICELISAQIK DITVHEAWTG PARLQLFDHA MAPFNDLPVK EIVSSSHILT DLTLPSPEVI
     YDYLKK