ID   ADC_STRNO               Reviewed;         244 AA.
AC   Q9EYI7;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 65.
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};
OS   Streptomyces nogalater.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=38314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27451 / DSM 40546 / JCM 4553 / NBRC 13445 / NCIMB 9489 / VKM
RC   Ac-1290;
RX   PubMed=11683270; DOI=10.1007/s004380100554;
RA   Torkkell S., Kunnari T., Palmu K., Maentsaelae P., Hakala J., Ylihonko K.;
RT   "The entire nogalamycin biosynthetic gene cluster of Streptomyces
RT   nogalater: characterization of a 20-kb DNA region and generation of hybrid
RT   structures.";
RL   Mol. Genet. Genomics 266:276-288(2001).
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; AF323753; AAG42848.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9EYI7; -.
DR   SMR; Q9EYI7; -.
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..244
FT                   /note="Acetoacetate decarboxylase"
FT                   /id="PRO_0000207109"
FT   ACT_SITE        115
FT                   /note="Schiff-base intermediate with acetoacetate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00597"
SQ   SEQUENCE   244 AA;  26988 MW;  6C6FED51F045C2F7 CRC64;
     MRAEDVVRAP STPLDAPAFP AGPYRFTDRE YLNITYRTDP EALRRVVPEP LRVAEPLVRF
     EVMRMPDVTG LGDYTEAGQL AVVEYEGEPG EYGISIHVDN FPAIASGREI GAFPKKAGRP
     RLYVDQDTLV GTLDHGTLPV ARATMGYKHR PLNTEQAREE LTRPTFMLKK LPHYDGSPRI
     CELVRTQIAD IVVKGAWSGP ARLQLFAHAL APLADLPVLE VVSAAHVLTD LTLGRARVVH
     DYLA