ID   ADC2_RHILO              Reviewed;         261 AA.
AC   Q98IH6;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Acetoacetate decarboxylase 2 {ECO:0000255|HAMAP-Rule:MF_00597};
DE            Short=AAD 2 {ECO:0000255|HAMAP-Rule:MF_00597};
DE            Short=ADC 2 {ECO:0000255|HAMAP-Rule:MF_00597};
DE            EC=4.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00597};
GN   Name=adc2 {ECO:0000255|HAMAP-Rule:MF_00597}; OrderedLocusNames=mlr2399;
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; BAB49540.1; -; Genomic_DNA.
DR   RefSeq; WP_010910892.1; NC_002678.2.
DR   AlphaFoldDB; Q98IH6; -.
DR   SMR; Q98IH6; -.
DR   STRING; 266835.14022932; -.
DR   EnsemblBacteria; BAB49540; BAB49540; BAB49540.
DR   KEGG; mlo:mlr2399; -.
DR   PATRIC; fig|266835.9.peg.1930; -.
DR   eggNOG; COG4689; Bacteria.
DR   HOGENOM; CLU_077089_0_0_5; -.
DR   OMA; ITYETDM; -.
DR   OrthoDB; 978501at2; -.
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..261
FT                   /note="Acetoacetate decarboxylase 2"
FT                   /id="PRO_0000207107"
FT   ACT_SITE        116
FT                   /note="Schiff-base intermediate with acetoacetate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00597"
SQ   SEQUENCE   261 AA;  29002 MW;  712DB9FC811DFF76 CRC64;
     MHQDTVRATA FAMPLTSPAY PVGPYRFRNR EYLIITYRTD PKKLRSLVPE PLELSEPLVK
     FEFIRMPDST GFGNYTESGQ VIPVTFRGRK GSYTHCMFLN DHPPIAGGRE LWGFPKKLAT
     PTLRTETDTL VGTLDYGPVR VATATMGYKH EAADLSAVRS SLAEPNFLLK IIPHVDGTPR
     ICELVEYHLE DVDLRGAWAG PASLNLWSHA LAPVAELPVL EVVSAMHIVA DLTLALGKVV
     HDYLPKSEPR DLKGRSHAFA E