ID   ADC_PARXL               Reviewed;         252 AA.
AC   Q141C9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Bxeno_A1522;
GN   ORFNames=Bxe_A2916;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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; CP000270; ABE30060.1; -; Genomic_DNA.
DR   RefSeq; WP_011487770.1; NZ_CP008760.1.
DR   AlphaFoldDB; Q141C9; -.
DR   SMR; Q141C9; -.
DR   STRING; 266265.Bxe_A2916; -.
DR   EnsemblBacteria; ABE30060; ABE30060; Bxe_A2916.
DR   KEGG; bxb:DR64_598; -.
DR   KEGG; bxe:Bxe_A2916; -.
DR   PATRIC; fig|266265.5.peg.1574; -.
DR   eggNOG; COG4689; Bacteria.
DR   OMA; FEVMRMG; -.
DR   OrthoDB; 978501at2; -.
DR   Proteomes; UP000001817; 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; Reference proteome; Schiff base.
FT   CHAIN           1..252
FT                   /note="Acetoacetate decarboxylase"
FT                   /id="PRO_1000025641"
FT   ACT_SITE        116
FT                   /note="Schiff-base intermediate with acetoacetate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00597"
SQ   SEQUENCE   252 AA;  27761 MW;  1C3C812CE21E2D16 CRC64;
     MDVKSVLSNA FAMPITSPAF PMGPYRFINR EFLIITYRTD PDKLRAVVPE PLEIGEPLVH
     YEFIRMPDST GFGDYTESGQ VIPVSYKGVA GGYTLAMYLD DHPPIAGGRE LWGFPKKLAN
     PVLAVHTDTL VGTLDYGPVR IATGTMGYKH RQLDLAQQKK RLETPNFLLK VIPHVDGTPR
     ICELVRYYLQ DIDLKGAWTG PAALELAPHA LAPVAALPVL EVVEARHLIA DLTLGLGEVV
     FDYLGQPQAN AR