THIL_CHRVO
ID THIL_CHRVO Reviewed; 392 AA.
AC Q9ZHI1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Acetyl-CoA acetyltransferase;
DE EC=2.3.1.9;
DE AltName: Full=Acetoacetyl-CoA thiolase;
GN Name=phaA; OrderedLocusNames=CV_2790;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-143.
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=10427049; DOI=10.1128/aem.65.8.3561-3565.1999;
RA Kolibachuk D., Miller A., Dennis D.;
RT "Cloning, molecular analysis, and expression of the polyhydroxyalkanoic
RT acid synthase (phaC) gene from Chromobacterium violaceum.";
RL Appl. Environ. Microbiol. 65:3561-3565(1999).
CC -!- FUNCTION: Involved in the production of polyhydroxyalkonic acids
CC (PHAs), composed primarily of 3-hydroxybutyric acid (3HB) and 3-
CC hydroxyvaleric acid (3HV).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10020};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; AE016825; AAQ60458.1; -; Genomic_DNA.
DR EMBL; AF061446; AAC69616.1; -; Genomic_DNA.
DR RefSeq; WP_011136337.1; NC_005085.1.
DR AlphaFoldDB; Q9ZHI1; -.
DR SMR; Q9ZHI1; -.
DR STRING; 243365.CV_2790; -.
DR PRIDE; Q9ZHI1; -.
DR EnsemblBacteria; AAQ60458; AAQ60458; CV_2790.
DR KEGG; cvi:CV_2790; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_4; -.
DR OMA; ICPSIAI; -.
DR OrthoDB; 1058688at2; -.
DR UniPathway; UPA00058; UER00101.
DR Proteomes; UP000001424; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042621; P:poly(3-hydroxyalkanoate) biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; PHA biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..392
FT /note="Acetyl-CoA acetyltransferase"
FT /id="PRO_0000206420"
FT ACT_SITE 87
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT CONFLICT 9..11
FT /note="QRT -> HAP (in Ref. 2; AAC69616)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="H -> Y (in Ref. 2; AAC69616)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 40119 MW; CCE21993747EF8DB CRC64;
MEVAIVAAQR TAIGSFGGGL AKIPAPELGA TVIKALLEKT GVKPEDVSEV ILGQVLTAGS
GQNPARQALI KAGLPVTTPA TTLNVVCGSG LRAVHLAAQA ILAGDADIVI AGGQESMSLS
PHILPGSRDG FRMGNAQLVD TMVNDGLTDA YNAYHMGITA ENVAAKYGIG REEQDAFSLQ
SQQRAAAAQK AGKFRDEIVP VLVPQRKGDP LAFDADEFIK HDASADGLAK LRPAFKKDGT
VTAGNASGIN DGAAAVLLMS TQKADQLGLK PLAIIKGYAL TGCEPEIMGI GPVSATRKAL
SKAGWTVEDL DLVEANEAFA AQALGVAKEL GWGSDKVNVN GGAIALGHPI GASGCRVLVT
LLHEMQRRGA KKGLATLCIG GGMGVALAVE RP
