ID A0A1B4K161_BURTH Unreviewed; 246 AA. AC A0A1B4K161; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 13-SEP-2023, entry version 36. DE RecName: Full=Acetoacetate decarboxylase {ECO:0000256|HAMAP-Rule:MF_00597}; DE Short=AAD {ECO:0000256|HAMAP-Rule:MF_00597}; DE Short=ADC {ECO:0000256|HAMAP-Rule:MF_00597}; DE EC=4.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00597}; GN Name=adc {ECO:0000256|HAMAP-Rule:MF_00597}; GN ORFNames=A8H32_31175 {ECO:0000313|EMBL:AVR29201.1}; OS Burkholderia thailandensis. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=57975 {ECO:0000313|EMBL:AVR29201.1, ECO:0000313|Proteomes:UP000241460}; RN [1] {ECO:0000313|Proteomes:UP000241460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_238 {ECO:0000313|Proteomes:UP000241460}; RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L., RA Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Vyas G., RA Aluvathingal J., Nadendla S., Geyer C., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of acetoacetate to acetone and CC carbon dioxide. {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_00597}; CC -!- SIMILARITY: Belongs to the ADC family. {ECO:0000256|HAMAP- CC Rule:MF_00597}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP020391; AVR29201.1; -; Genomic_DNA. DR RefSeq; WP_009894527.1; NZ_WVUL01000026.1. DR AlphaFoldDB; A0A1B4K161; -. DR EnsemblBacteria; AWY61294; AWY61294; A8H35_24180. DR EnsemblBacteria; PNE77493; PNE77493; A8H37_03860. DR GeneID; 66548802; -. DR KEGG; btha:DR62_4906; -. DR OrthoDB; 1633687at2; -. DR Proteomes; UP000241460; Chromosome 2. DR GO; GO:0047602; F:acetoacetate decarboxylase activity; IEA:UniProtKB-UniRule. DR Gene3D; 2.40.400.10; Acetoacetate decarboxylase-like; 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; Acetoacetate decarboxylase-like; 1. PE 3: Inferred from homology; KW Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00597}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00597, ECO:0000313|EMBL:AVR29201.1}; KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00597}. FT ACT_SITE 116 FT /note="Schiff-base intermediate with acetoacetate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00597" SQ SEQUENCE 246 AA; 27436 MW; 027F06947B06D483 CRC64; MKPSQVRSKA FAMPLTSPAF PMGPYRFVNR EFLIITYRTD MDRLREIVPE PLEVKEPLVH YEFIRMPDST GFGDYTESGQ VIPVEYKGQP GGYTLAMYLN DHPPIAGGRE LWGFPKKLAQ PTLATHIDTL LGTLDYGPVR VATGTMGYKH QELDLEEQAK RLAGANFLLK IIPHVDGSAR VCELVRYYLQ DIKMKGAWTG PASLQLAPHA LAPVADLPVL EIVEARHLLA DLTLGLGEVV YDYLAQ //