ADC_BURCJ
ID ADC_BURCJ Reviewed; 246 AA.
AC B4EG09;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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};
GN OrderedLocusNames=BceJ2315_34930; ORFNames=BCAM0023;
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX PubMed=18931103; DOI=10.1128/jb.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
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; AM747721; CAR53878.1; -; Genomic_DNA.
DR RefSeq; WP_006485181.1; NC_011001.1.
DR AlphaFoldDB; B4EG09; -.
DR SMR; B4EG09; -.
DR STRING; 216591.BCAM0023; -.
DR EnsemblBacteria; CAR53878; CAR53878; BCAM0023.
DR GeneID; 56560732; -.
DR KEGG; bcj:BCAM0023; -.
DR eggNOG; COG4689; Bacteria.
DR HOGENOM; CLU_077089_0_0_4; -.
DR OMA; FEVMRMG; -.
DR OrthoDB; 978501at2; -.
DR BioCyc; BCEN216591:G1G1V-3957-MON; -.
DR Proteomes; UP000001035; 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_1000129876"
FT ACT_SITE 116
FT /note="Schiff-base intermediate with acetoacetate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00597"
SQ SEQUENCE 246 AA; 27413 MW; D3287BD4D01EBB16 CRC64;
MKPSDVRSKA FAMPLTSPAF PMGPYRFVDR EFLIITYRTD PDRLREIVPE PLQVTEPLVH
YEFIRMADST GFGDYTESGQ VIPVEYNGQA GGYTLAMYLD DHPPIAGGRE LWGFPKKLAS
PTLHVNTDHI LGTLDYGKVR VATGTMGYKH KELDIDEQTK RLAGPNFLLK IIPHVDGTAR
VCELVRYYMQ DIKMKGAWTG PASLELAPHA LAPVADLPVL EIVEARHLVA DLTLGLGEVV
YDYLAQ