ID   ADC_PARPJ               Reviewed;         252 AA.
AC   B2T319;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Bphyt_1567;
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX   PubMed=21551308; DOI=10.1128/jb.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
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; CP001052; ACD15980.1; -; Genomic_DNA.
DR   RefSeq; WP_012432594.1; NC_010681.1.
DR   AlphaFoldDB; B2T319; -.
DR   SMR; B2T319; -.
DR   STRING; 398527.Bphyt_1567; -.
DR   EnsemblBacteria; ACD15980; ACD15980; Bphyt_1567.
DR   KEGG; bpy:Bphyt_1567; -.
DR   eggNOG; COG4689; Bacteria.
DR   HOGENOM; CLU_077089_0_0_4; -.
DR   OMA; FEVMRMG; -.
DR   OrthoDB; 978501at2; -.
DR   Proteomes; UP000001739; Chromosome 1.
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..252
FT                   /note="Acetoacetate decarboxylase"
FT                   /id="PRO_1000129878"
FT   ACT_SITE        116
FT                   /note="Schiff-base intermediate with acetoacetate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00597"
SQ   SEQUENCE   252 AA;  27932 MW;  C8F9812CE6EC20DB CRC64;
     MDVKSVLSNA FAMPITSPAF PMGPYRFINR EFLIITYRTD PDKLRAVVPE PLEIGEPLVH
     YEFIRMPDST GFGDYTESGQ VIPVSYKGVA GGYTLAMYLD DHPPIAGGRE LWGFPKKLAN
     PVLAVHTDTL VGTLDYGPVR IATGTMGYKH RQLDLAQQKK RLETPNFLLK VIPHVDGTPR
     ICELVRYYLQ DIDLKGAWTG PAALELAHHA LAPVAELPVL EIVEARHLLA DLTLGLGEVV
     FDYLDQPEAN AR