ADC2_BRADU
ID ADC2_BRADU Reviewed; 263 AA.
AC Q89EP4;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=blr7028;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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}.
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; BA000040; BAC52293.1; -; Genomic_DNA.
DR RefSeq; NP_773668.1; NC_004463.1.
DR RefSeq; WP_011089765.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89EP4; -.
DR SMR; Q89EP4; -.
DR STRING; 224911.27355309; -.
DR EnsemblBacteria; BAC52293; BAC52293; BAC52293.
DR GeneID; 64026786; -.
DR KEGG; bja:blr7028; -.
DR PATRIC; fig|224911.44.peg.7083; -.
DR eggNOG; COG4689; Bacteria.
DR HOGENOM; CLU_077089_0_0_5; -.
DR InParanoid; Q89EP4; -.
DR OMA; ITYETDM; -.
DR PhylomeDB; Q89EP4; -.
DR Proteomes; UP000002526; 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..263
FT /note="Acetoacetate decarboxylase 2"
FT /id="PRO_0000207100"
FT ACT_SITE 118
FT /note="Schiff-base intermediate with acetoacetate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00597"
SQ SEQUENCE 263 AA; 29341 MW; 22F7464454FF3AF7 CRC64;
MRENDVRKRA FAMPLTSPAY PPGPYRFVDR EYLIITYRTD PARLRAVVPE PLELDDRNPL
VKYEFIRMPD SNGFGDYTES GQVIPVSFRG HTGGYNHCMF LNDEGPIAGG RELWGFPKKL
GQPTLRTEID TLIGTLDYGP LRVATGTMGY KHREADLGQV KAALEEPNFL LKIIPHVDGS
PRICELVEYR LEQIALKGAW TGPAALSLTP HALAPVADLP VLEIVSALHI RADLTLGLGR
VAHDYLQEPA RRPFRASERS LVT