ADC_ACICJ
ID ADC_ACICJ Reviewed; 245 AA.
AC A5FVT7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Acry_0495;
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000697; ABQ29719.1; -; Genomic_DNA.
DR RefSeq; WP_007422113.1; NC_009484.1.
DR AlphaFoldDB; A5FVT7; -.
DR SMR; A5FVT7; -.
DR STRING; 349163.Acry_0495; -.
DR EnsemblBacteria; ABQ29719; ABQ29719; Acry_0495.
DR KEGG; acr:Acry_0495; -.
DR eggNOG; COG4689; Bacteria.
DR HOGENOM; CLU_077089_0_0_5; -.
DR OMA; FEVMRMG; -.
DR OrthoDB; 978501at2; -.
DR Proteomes; UP000000245; Chromosome.
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..245
FT /note="Acetoacetate decarboxylase"
FT /id="PRO_1000025629"
FT ACT_SITE 116
FT /note="Schiff-base intermediate with acetoacetate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00597"
SQ SEQUENCE 245 AA; 27261 MW; 9C3136B76E632E6B CRC64;
MDAATIRETA FAMPLTSPGF PKGPYRFVNR EYMIITYRTD RAALEKIVPE PLELADDVVK
YEFIRMPDST GFGDYTESGQ VIPVRYKGKP GVYVHSMFLN DHPPIAGGRE IWGFPKKLAR
PVLEVEIDTL VGTLDYGRIR VATGTMGYKH HTLDHDPVLS SMHEPNFLLK IIPHVDGSPR
ICELVRYHMS DIVLKGAWTG PAALALYPHA LAPVADLPVR EVVAASHILA DMTLDLGEVV
HDYLA