ID   ADC3_RHILO              Reviewed;         256 AA.
AC   Q98FS9;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Acetoacetate decarboxylase 3 {ECO:0000255|HAMAP-Rule:MF_00597};
DE            Short=AAD 3 {ECO:0000255|HAMAP-Rule:MF_00597};
DE            Short=ADC 3 {ECO:0000255|HAMAP-Rule:MF_00597};
DE            EC=4.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00597};
GN   Name=adc3 {ECO:0000255|HAMAP-Rule:MF_00597}; OrderedLocusNames=mlr3634;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB50488.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q98FS9; -.
DR   SMR; Q98FS9; -.
DR   STRING; 266835.14023883; -.
DR   DNASU; 1227363; -.
DR   EnsemblBacteria; BAB50488; BAB50488; BAB50488.
DR   KEGG; mlo:mlr3634; -.
DR   eggNOG; COG4689; Bacteria.
DR   HOGENOM; CLU_077089_0_0_5; -.
DR   OMA; YEWIKMP; -.
DR   Proteomes; UP000000552; 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; Schiff base.
FT   CHAIN           1..256
FT                   /note="Acetoacetate decarboxylase 3"
FT                   /id="PRO_0000207108"
FT   ACT_SITE        110
FT                   /note="Schiff-base intermediate with acetoacetate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00597"
SQ   SEQUENCE   256 AA;  28472 MW;  DABAF96FC47ABCD7 CRC64;
     MKRAYAMPLT NPSFPPGPYR FFDREYIIIT YRTTREALEA VVPAPLEIDE PLVKYEFIRM
     PDSTGFGDYT ETGQVIPVKY KGQHGGYVHS MYLDDDAPIA GGRELWGFPK KLANPKIVHE
     GEVIVGTLHY GSVLCATGTM GYKHREADHD SVLASLAAPN FLIKIIPHVD GGPRICELVR
     YYLTDITLKE AWTAPAALDL RPHVMADVAK LPVLDIISAV HFKADLTLGL GEVVHDYLSD
     HNRLATSTTQ PEKIRA