ADC_BURPS
ID ADC_BURPS Reviewed; 246 AA.
AC Q63PC7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=BPSS0018;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(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; BX571966; CAH37461.1; -; Genomic_DNA.
DR RefSeq; WP_004194452.1; NZ_CP009537.1.
DR RefSeq; YP_110042.1; NC_006351.1.
DR AlphaFoldDB; Q63PC7; -.
DR SMR; Q63PC7; -.
DR STRING; 272560.BPSS0018; -.
DR EnsemblBacteria; CAH37461; CAH37461; BPSS0018.
DR GeneID; 56596762; -.
DR KEGG; bps:BPSS0018; -.
DR PATRIC; fig|272560.51.peg.6014; -.
DR eggNOG; COG4689; Bacteria.
DR OMA; FEVMRMG; -.
DR Proteomes; UP000000605; 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; Reference proteome; Schiff base.
FT CHAIN 1..246
FT /note="Acetoacetate decarboxylase"
FT /id="PRO_1000025638"
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
