ADC_CHRVO
ID ADC_CHRVO Reviewed; 246 AA.
AC Q7NSA6;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Acetoacetate decarboxylase {ECO:0000255|HAMAP-Rule:MF_00597, ECO:0000303|PubMed:19458715};
DE Short=AAD {ECO:0000255|HAMAP-Rule:MF_00597};
DE Short=AADase {ECO:0000303|PubMed:19458715};
DE Short=ADC {ECO:0000255|HAMAP-Rule:MF_00597};
DE EC=4.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00597, ECO:0000269|PubMed:19458715};
GN Name=adc {ECO:0000255|HAMAP-Rule:MF_00597}; OrderedLocusNames=CV_3520;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
RN [2] {ECO:0007744|PDB:3BGT, ECO:0007744|PDB:3BH3}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH THE
RP INTERMEDIATE ANALOG 2,4-PENTANEDIONE, FUNCTION, CATALYTIC ACTIVITY,
RP REACTION MECHANISM, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE,
RP AND MUTAGENESIS OF GLU-62 AND GLU-77.
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}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 mM for acetoacetate (at pH 6) {ECO:0000269|PubMed:19458715};
CC KM=4 mM for acetoacetate (at pH 5.4) {ECO:0000269|PubMed:19458715};
CC KM=2.6 mM for acetoacetate (at pH 4.8) {ECO:0000269|PubMed:19458715};
CC Note=kcat is 350 sec(-1) at pH 6. kcat is 440 sec(-1) at pH 5.4. kcat
CC is 420 sec(-1) at pH 4.8. {ECO:0000269|PubMed:19458715};
CC -!- SUBUNIT: Homododecamer. {ECO:0000269|PubMed:19458715}.
CC -!- SIMILARITY: Belongs to the ADC family. {ECO:0000255|HAMAP-
CC Rule:MF_00597}.
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DR EMBL; AE016825; AAQ61181.1; -; Genomic_DNA.
DR RefSeq; WP_011137067.1; NC_005085.1.
DR PDB; 3BGT; X-ray; 2.10 A; A/B/C/D=1-246.
DR PDB; 3BH3; X-ray; 2.10 A; A/B/C/D=1-246.
DR PDBsum; 3BGT; -.
DR PDBsum; 3BH3; -.
DR AlphaFoldDB; Q7NSA6; -.
DR SMR; Q7NSA6; -.
DR DIP; DIP-59757N; -.
DR STRING; 243365.CV_3520; -.
DR EnsemblBacteria; AAQ61181; AAQ61181; CV_3520.
DR KEGG; cvi:CV_3520; -.
DR eggNOG; COG4689; Bacteria.
DR HOGENOM; CLU_077089_0_0_4; -.
DR OMA; FEVMRMG; -.
DR OrthoDB; 978501at2; -.
DR BRENDA; 4.1.1.4; 1370.
DR EvolutionaryTrace; Q7NSA6; -.
DR PRO; PR:Q7NSA6; -.
DR Proteomes; UP000001424; 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 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..246
FT /note="Acetoacetate decarboxylase"
FT /id="PRO_0000207104"
FT ACT_SITE 116
FT /note="Schiff-base intermediate with acetoacetate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00597,
FT ECO:0000269|PubMed:19458715"
FT SITE 117
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:19458715"
FT MUTAGEN 62
FT /note="E->Q: 20-fold decrease in kcat."
FT /evidence="ECO:0000269|PubMed:19458715"
FT MUTAGEN 77
FT /note="E->Q: 250-fold decrease in kcat."
FT /evidence="ECO:0000269|PubMed:19458715"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 25..38
FT /evidence="ECO:0007829|PDB:3BGT"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 56..69
FT /evidence="ECO:0007829|PDB:3BGT"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 73..86
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 89..100
FT /evidence="ECO:0007829|PDB:3BGT"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 139..149
FT /evidence="ECO:0007829|PDB:3BGT"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 177..187
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 189..199
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3BGT"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 220..234
FT /evidence="ECO:0007829|PDB:3BGT"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:3BGT"
SQ SEQUENCE 246 AA; 27299 MW; 3596958D9583E3E7 CRC64;
MKQQEVRQRA FAMPLTSPAF PPGPYRFVNR EYMIITYRTD PAAIEAVLPE PLQMAEPVVR
YEFIRMPDST GFGDYSESGQ VIPVTFRGER GSYTLAMFLD DQPPLAGGRE LWGFPKKAGK
PRLEVHQDTL VGSLDFGPVR IATGTMGYKY EALDRSALLA SLAEPNFLLK IIPHVDGSPR
ICELVRYHTT DVAIKGAWSA PGSLELHPHA LAPVAALPVL EVLSARHFVC DLTLDLGTVV
FDYLRQ
