ID   ADC_CLOPA               Reviewed;          19 AA.
AC   P81336;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Acetoacetate decarboxylase {ECO:0000250|UniProtKB:P23670};
DE            Short=AAD {ECO:0000250|UniProtKB:P23670};
DE            Short=ADC {ECO:0000250|UniProtKB:P23670};
DE            EC=4.1.1.4 {ECO:0000250|UniProtKB:P23670};
DE   AltName: Full=CP 28/CP 29;
DE   Flags: Fragment;
GN   Name=adc;
OS   Clostridium pasteurianum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1501;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5;
RX   PubMed=9629918; DOI=10.1002/elps.1150190533;
RA   Flengsrud R., Skjeldal L.;
RT   "Two-dimensional gel electrophoresis separation and N-terminal sequence
RT   analysis of proteins from Clostridium pasteurianum W5.";
RL   Electrophoresis 19:802-806(1998).
CC   -!- FUNCTION: Catalyzes the conversion of acetoacetate to acetone and
CC       carbon dioxide. {ECO:0000250|UniProtKB:P23670}.
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;
CC         Evidence={ECO:0000250|UniProtKB:P23670};
CC   -!- SIMILARITY: Belongs to the ADC family. {ECO:0000305}.
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DR   AlphaFoldDB; P81336; -.
DR   GO; GO:0047602; F:acetoacetate decarboxylase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Decarboxylase; Direct protein sequencing; Lyase.
FT   CHAIN           1..>19
FT                   /note="Acetoacetate decarboxylase"
FT                   /id="PRO_0000207103"
FT   NON_TER         19
SQ   SEQUENCE   19 AA;  2079 MW;  6ACDAA91103AEC31 CRC64;
     MLKSEVSKQI SMPLTAPAF