ID   ADC_BORA1               Reviewed;         246 AA.
AC   Q2L048;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=BAV0264;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ47869.1; -; Genomic_DNA.
DR   RefSeq; WP_012415966.1; NC_010645.1.
DR   AlphaFoldDB; Q2L048; -.
DR   SMR; Q2L048; -.
DR   STRING; 360910.BAV0264; -.
DR   EnsemblBacteria; CAJ47869; CAJ47869; BAV0264.
DR   GeneID; 41392193; -.
DR   KEGG; bav:BAV0264; -.
DR   eggNOG; COG4689; Bacteria.
DR   HOGENOM; CLU_077089_0_0_4; -.
DR   OMA; FEVMRMG; -.
DR   OrthoDB; 978501at2; -.
DR   Proteomes; UP000001977; 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; Reference proteome; Schiff base.
FT   CHAIN           1..246
FT                   /note="Acetoacetate decarboxylase"
FT                   /id="PRO_1000025630"
FT   ACT_SITE        116
FT                   /note="Schiff-base intermediate with acetoacetate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00597"
SQ   SEQUENCE   246 AA;  27282 MW;  89E44F015E68CCDC CRC64;
     MNIDTVRANA FAMPLTSPAF PMGPYRFVKR EFFVITYRTD PEALRSVVPE PLAVTQPLVH
     YEFIRMPDST GFGDYTESGQ VIPVEYEGVA GSYTHAMYLN DHPPIAGGRE LWGFPKKLAL
     PTLKVHTDTL VGTLDYGPIR VATGTMGYKH EEVDIVEQAR HLSAPNFLLK IIPHVDCSPR
     ICELVRYYLE DIRVYGAWSG PAALELAPHA LAPVADLPVL EVVGARHFIA DLTLGLGEVV
     YDYLAK