ID   ADC_BURMA               Reviewed;         246 AA.
AC   Q62EK3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=BMAA0018;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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; CP000011; AAU45550.1; -; Genomic_DNA.
DR   RefSeq; WP_004194452.1; NC_006349.2.
DR   RefSeq; YP_104875.1; NC_006349.2.
DR   AlphaFoldDB; Q62EK3; -.
DR   SMR; Q62EK3; -.
DR   STRING; 243160.BMAA0018; -.
DR   DNASU; 3086006; -.
DR   EnsemblBacteria; AAU45550; AAU45550; BMAA0018.
DR   GeneID; 56596762; -.
DR   KEGG; bma:BMAA0018; -.
DR   PATRIC; fig|243160.12.peg.3511; -.
DR   eggNOG; COG4689; Bacteria.
DR   HOGENOM; CLU_077089_0_0_4; -.
DR   OMA; FEVMRMG; -.
DR   Proteomes; UP000006693; Chromosome 2.
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..246
FT                   /note="Acetoacetate decarboxylase"
FT                   /id="PRO_1000025636"
FT   ACT_SITE        116
FT                   /note="Schiff-base intermediate with acetoacetate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00597"
SQ   SEQUENCE   246 AA;  27494 MW;  17710D946B0C7483 CRC64;
     MKPSQVRSKA FAMPLTSPAF PMGPYRFVNR EFLIITYRTD MDRLREIVPE PLEVKEPLVH
     YEFIRMPDST GFGDYTESGQ VIPVEYKGQP GGYTLAMYLN DHPPIAGGRE LWGFPKKLAQ
     PTLQTHIDTL LGTLDYGPVR VATGTMGYKH QELDLEEQAK RLAGANFLLK IIPHVDGSAR
     VCELVRYYLQ DIEMKGAWTG PASLQLAPHA LAPVADLPVL EIVEARHLLA DLTLGLGEVV
     YDYLAQ