ID A0A1B4K161_BURTH Unreviewed; 246 AA. AC A0A1B4K161; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 25-APR-2018, entry version 11. DE RecName: Full=Probable 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=A8H37_03860 {ECO:0000313|EMBL:PNE77493.1}; OS Burkholderia thailandensis. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=57975 {ECO:0000313|EMBL:PNE77493.1, ECO:0000313|Proteomes:UP000235972}; RN [1] {ECO:0000313|EMBL:PNE77493.1, ECO:0000313|Proteomes:UP000235972} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_243 {ECO:0000313|EMBL:PNE77493.1, RC ECO:0000313|Proteomes:UP000235972}; RA Goldberg B., Campos J., Tallon L., Sadzewicz L., Sengamalay N., RA Ott S., Godinez A., Nagaraj S., Vyas G., Aluvathingal J., Nadendla S., RA Geyer C., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx RT 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: Acetoacetate = acetone + CO(2). CC {ECO:0000256|HAMAP-Rule:MF_00597}. CC -!- SIMILARITY: Belongs to the ADC family. {ECO:0000256|HAMAP- CC Rule:MF_00597}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PNE77493.1}. 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; NBSQ01000001; PNE77493.1; -; Genomic_DNA. DR RefSeq; WP_009894527.1; NZ_PDLI01000002.1. DR Proteomes; UP000235972; Unassembled WGS sequence. 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 Complete proteome {ECO:0000313|Proteomes:UP000235972}; KW Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00597}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00597, ECO:0000313|EMBL:PNE77493.1}; KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00597}. FT ACT_SITE 116 116 Schiff-base intermediate with FT acetoacetate. {ECO:0000256|HAMAP-Rule: FT 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 //