ADC1_RHILO
ID ADC1_RHILO Reviewed; 247 AA.
AC Q98AN6; Q8KJA4;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Acetoacetate decarboxylase 1 {ECO:0000255|HAMAP-Rule:MF_00597};
DE Short=AAD 1 {ECO:0000255|HAMAP-Rule:MF_00597};
DE Short=ADC 1 {ECO:0000255|HAMAP-Rule:MF_00597};
DE EC=4.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00597};
GN Name=adc1 {ECO:0000255|HAMAP-Rule:MF_00597}; OrderedLocusNames=mll5917;
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 [GENOMIC DNA].
RC STRAIN=R7A;
RX PubMed=12003951; DOI=10.1128/jb.184.11.3086-3095.2002;
RA Sullivan J.T., Trzebiatowski J.R., Cruickshank R.W., Gouzy J., Brown S.D.,
RA Elliot R.M., Fleetwood D.J., McCallum N.G., Rossbach U., Stuart G.S.,
RA Weaver J.E., Webby R.J., de Bruijn F.J., Ronson C.W.;
RT "Comparative sequence analysis of the symbiosis island of Mesorhizobium
RT loti strain R7A.";
RL J. Bacteriol. 184:3086-3095(2002).
RN [2]
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; AL672114; CAD31314.1; -; Genomic_DNA.
DR EMBL; BA000012; BAB52286.1; -; Genomic_DNA.
DR RefSeq; WP_010913619.1; NC_002678.2.
DR AlphaFoldDB; Q98AN6; -.
DR SMR; Q98AN6; -.
DR STRING; 266835.14025686; -.
DR EnsemblBacteria; BAB52286; BAB52286; BAB52286.
DR KEGG; mlo:mll5917; -.
DR PATRIC; fig|266835.9.peg.4710; -.
DR eggNOG; COG4689; Bacteria.
DR HOGENOM; CLU_077089_0_0_5; -.
DR OMA; FEVMRMG; -.
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..247
FT /note="Acetoacetate decarboxylase 1"
FT /id="PRO_0000207106"
FT ACT_SITE 116
FT /note="Schiff-base intermediate with acetoacetate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00597"
FT CONFLICT 16
FT /note="I -> T (in Ref. 1; CAD31314)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="Y -> C (in Ref. 1; CAD31314)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="V -> A (in Ref. 1; CAD31314)"
FT /evidence="ECO:0000305"
FT CONFLICT 245..246
FT /note="AK -> PE (in Ref. 1; CAD31314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 27390 MW; C36298F3EA4DCC1C CRC64;
MHQDTVRGKA FAMPLISPAY PAGPYRFRNR EYLIITYRTD PQKLRDLVPE PLQVCEPMVK
FEFIRMPDST GFGDYTEGGQ VIPVSFYGRR GSYTHCMFLD DHPPIAGGRE LWGFPKKLAS
PTLRTETDTL VGTLDYGPVR VATGTMGYKH RAADLASVRA SLAEPNFLLK IIPHVDGTPR
ICELVEYHLE DVHLRGAWTG PAALNLWSHA LAPVAELPVL EVVSAVHLVA DLTLALGKVV
HDYLAKA