ADC_CLOAB
ID ADC_CLOAB Reviewed; 244 AA.
AC P23670; Q9S428;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Acetoacetate decarboxylase {ECO:0000255|HAMAP-Rule:MF_00597, ECO:0000303|PubMed:5946601};
DE Short=AAD {ECO:0000255|HAMAP-Rule:MF_00597, ECO:0000303|PubMed:8555196};
DE Short=AADase {ECO:0000303|PubMed:19458715};
DE Short=ADC {ECO:0000255|HAMAP-Rule:MF_00597, ECO:0000303|PubMed:2254264};
DE EC=4.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00597, ECO:0000269|PubMed:19458715, ECO:0000269|PubMed:2268159, ECO:0000269|PubMed:8555196};
GN Name=adc {ECO:0000255|HAMAP-Rule:MF_00597, ECO:0000303|PubMed:2254264};
GN OrderedLocusNames=CA_P0165;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OG Plasmid pSOL1.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-25.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=2254264; DOI=10.1128/jb.172.12.6907-6918.1990;
RA Gerischer U., Duerre P.;
RT "Cloning, sequencing, and molecular analysis of the acetoacetate
RT decarboxylase gene region from Clostridium acetobutylicum.";
RL J. Bacteriol. 172:6907-6918(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-30.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=8423010; DOI=10.1016/0378-1119(93)90545-e;
RA Petersen D.J., Cary J.W., Vanderleyden J., Bennett G.N.;
RT "Sequence and arrangement of genes encoding enzymes of the acetone-
RT production pathway of Clostridium acetobutylicum ATCC824.";
RL Gene 123:93-97(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 207-244.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=8226639; DOI=10.1128/jb.175.21.6959-6969.1993;
RA Fischer R.J., Helms J., Duerre P.;
RT "Cloning, sequencing, and molecular analysis of the sol operon of
RT Clostridium acetobutylicum, a chromosomal locus involved in
RT solventogenesis.";
RL J. Bacteriol. 175:6959-6969(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RA Sabathe F., Cornillot E., Croux C., Soucaille P.;
RT "Molecular characterization of amyP, a pSOL1 located gene coding the major
RT alpha-amylase of Clostridium acetobutylicum ATCC824, and its use as a
RT reporter system for strain degeneration.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 1-20, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=2268159; DOI=10.1128/aem.56.11.3491-3498.1990;
RA Petersen D.J., Bennett G.N.;
RT "Purification of acetoacetate decarboxylase from Clostridium acetobutylicum
RT ATCC 824 and cloning of the acetoacetate decarboxylase gene in Escherichia
RT coli.";
RL Appl. Environ. Microbiol. 56:3491-3498(1990).
RN [7]
RP ACTIVE SITE.
RX PubMed=5946601; DOI=10.1021/ja00966a044;
RA Laursen R.A., Westheimer F.H.;
RT "The active site of acetoacetate decarboxylase.";
RL J. Am. Chem. Soc. 88:3426-3430(1966).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVE SITE, AND MUTAGENESIS OF LYS-115 AND LYS-116.
RX PubMed=8555196; DOI=10.1021/bi9518306;
RA Highbarger L.A., Gerlt J.A., Kenyon G.L.;
RT "Mechanism of the reaction catalyzed by acetoacetate decarboxylase.
RT Importance of lysine 116 in determining the pKa of active-site lysine
RT 115.";
RL Biochemistry 35:41-46(1996).
RN [9] {ECO:0007744|PDB:3BH2}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP REACTION MECHANISM, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, AND
RP ACTIVE SITE.
RX PubMed=19458715; DOI=10.1038/nature07938;
RA Ho M.C., Menetret J.F., Tsuruta H., Allen K.N.;
RT "The origin of the electrostatic perturbation in acetoacetate
RT decarboxylase.";
RL Nature 459:393-397(2009).
CC -!- FUNCTION: Catalyzes the conversion of acetoacetate to acetone and
CC carbon dioxide. {ECO:0000255|HAMAP-Rule:MF_00597,
CC ECO:0000269|PubMed:19458715, ECO:0000269|PubMed:2268159,
CC ECO:0000269|PubMed:8555196}.
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, ECO:0000269|PubMed:19458715,
CC ECO:0000269|PubMed:2268159, ECO:0000269|PubMed:8555196};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.2 mM for acetoacetate (at pH 5.95) {ECO:0000269|PubMed:8555196};
CC KM=4.1 mM for acetoacetate (at pH 5.95)
CC {ECO:0000269|PubMed:19458715};
CC Note=kcat is 1560 sec(-1) (PubMed:8555196). kcat is 165 sec(-1)
CC (PubMed:19458715). {ECO:0000269|PubMed:19458715,
CC ECO:0000269|PubMed:8555196};
CC pH dependence:
CC Optimum pH is 5.95. {ECO:0000269|PubMed:8555196};
CC -!- SUBUNIT: Homododecamer. {ECO:0000269|PubMed:19458715}.
CC -!- INTERACTION:
CC P23670; P23670: adc; NbExp=4; IntAct=EBI-15782069, EBI-15782069;
CC -!- INDUCTION: By linear fatty acids (up to butyrate).
CC {ECO:0000305|PubMed:2254264}.
CC -!- DOMAIN: Lys-116 may be involved in the precise positioning of the
CC nucleophilic Lys-115. {ECO:0000269|PubMed:19458715}.
CC -!- SIMILARITY: Belongs to the ADC family. {ECO:0000255|HAMAP-
CC Rule:MF_00597, ECO:0000305}.
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DR EMBL; M55392; AAA63761.1; -; Genomic_DNA.
DR EMBL; M93363; AAB53232.1; -; Genomic_DNA.
DR EMBL; AE001438; AAK76910.1; -; Genomic_DNA.
DR EMBL; X72831; CAA51347.1; -; Genomic_DNA.
DR EMBL; AF164199; AAD47074.1; -; Genomic_DNA.
DR PIR; JN0487; JN0487.
DR RefSeq; NP_149328.1; NC_001988.2.
DR RefSeq; WP_010890849.1; NC_001988.2.
DR PDB; 3BH2; X-ray; 2.40 A; A/B/C/D=1-244.
DR PDBsum; 3BH2; -.
DR AlphaFoldDB; P23670; -.
DR SMR; P23670; -.
DR DIP; DIP-59756N; -.
DR EnsemblBacteria; AAK76910; AAK76910; CA_P0165.
DR GeneID; 45000390; -.
DR KEGG; cac:CA_P0165; -.
DR PATRIC; fig|272562.8.peg.166; -.
DR HOGENOM; CLU_077089_0_0_9; -.
DR OMA; FEVMRMG; -.
DR OrthoDB; 978501at2; -.
DR BioCyc; MetaCyc:ADCCLOS-MON; -.
DR BRENDA; 4.1.1.4; 1452.
DR EvolutionaryTrace; P23670; -.
DR Proteomes; UP000000814; Plasmid pSOL1.
DR GO; GO:0047602; F:acetoacetate decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Direct protein sequencing; Lyase; Plasmid;
KW Reference proteome; Schiff base.
FT CHAIN 1..244
FT /note="Acetoacetate decarboxylase"
FT /id="PRO_0000207101"
FT ACT_SITE 115
FT /note="Schiff-base intermediate with acetoacetate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00597,
FT ECO:0000269|PubMed:19458715, ECO:0000269|PubMed:5946601,
FT ECO:0000269|PubMed:8555196"
FT SITE 116
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:19458715"
FT MUTAGEN 115
FT /note="K->C,Q: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:8555196"
FT MUTAGEN 116
FT /note="K->C,N: Retains 2% of wild type activity."
FT /evidence="ECO:0000269|PubMed:8555196"
FT MUTAGEN 116
FT /note="K->R: Retains 20% of wild type activity."
FT /evidence="ECO:0000269|PubMed:8555196"
FT CONFLICT 85
FT /note="F -> C (in Ref. 2; AAB53232)"
FT /evidence="ECO:0000305"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 25..37
FT /evidence="ECO:0007829|PDB:3BH2"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 57..68
FT /evidence="ECO:0007829|PDB:3BH2"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 72..85
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 88..99
FT /evidence="ECO:0007829|PDB:3BH2"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:3BH2"
FT HELIX 154..161
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 176..186
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3BH2"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 219..232
FT /evidence="ECO:0007829|PDB:3BH2"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:3BH2"
SQ SEQUENCE 244 AA; 27537 MW; CA6C1157644E13B0 CRC64;
MLKDEVIKQI STPLTSPAFP RGPYKFHNRE YFNIVYRTDM DALRKVVPEP LEIDEPLVRF
EIMAMHDTSG LGCYTESGQA IPVSFNGVKG DYLHMMYLDN EPAIAVGREL SAYPKKLGYP
KLFVDSDTLV GTLDYGKLRV ATATMGYKHK ALDANEAKDQ ICRPNYMLKI IPNYDGSPRI
CELINAKITD VTVHEAWTGP TRLQLFDHAM APLNDLPVKE IVSSSHILAD IILPRAEVIY
DYLK
