THIL_RHIME
ID THIL_RHIME Reviewed; 393 AA.
AC P50174;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Acetyl-CoA acetyltransferase;
DE EC=2.3.1.9;
DE AltName: Full=Acetoacetyl-CoA thiolase;
DE AltName: Full=Beta-ketothiolase {ECO:0000303|PubMed:7582015};
GN Name=phaA {ECO:0000303|PubMed:7582015}; OrderedLocusNames=R03262;
GN ORFNames=SMc03879;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=41;
RX PubMed=7582015; DOI=10.1099/13500872-141-10-2553;
RA Tombolini R., Povolo S., Buson A., Squartini A., Nuti M.P.;
RT "Poly-beta-hydroxybutyrate (PHB) biosynthetic genes in Rhizobium meliloti
RT 41.";
RL Microbiology 141:2553-2559(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate
CC biosynthesis. {ECO:0000269|PubMed:7582015}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P14611}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; U17226; AAA90982.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC47841.1; -; Genomic_DNA.
DR RefSeq; NP_387368.1; NC_003047.1.
DR RefSeq; WP_010970528.1; NC_003047.1.
DR AlphaFoldDB; P50174; -.
DR SMR; P50174; -.
DR STRING; 266834.SMc03879; -.
DR EnsemblBacteria; CAC47841; CAC47841; SMc03879.
DR GeneID; 61604721; -.
DR KEGG; sme:SMc03879; -.
DR PATRIC; fig|266834.11.peg.4817; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_5; -.
DR OMA; MPEAYVI; -.
DR UniPathway; UPA00058; UER00101.
DR UniPathway; UPA00917; -.
DR Proteomes; UP000001976; 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:0042619; P:poly-hydroxybutyrate 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; PHB biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..393
FT /note="Acetyl-CoA acetyltransferase"
FT /id="PRO_0000206461"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ SEQUENCE 393 AA; 40851 MW; B3162E72A9DB2A0D CRC64;
MSNPSIVIAS AARTAVGSFN GAFGNTLAHE LGAAAIKAVL ERAGVEAGEV DEVILGQVLP
AGEGQNPARQ AAMKAGLPQE KTAWGMNQLC GSGLRAVALG MQQIATGDAK VIVAGGMESM
SMAPHCAHLR GGVKMGDYKM IDTMIKDGLT DAFYGYHMGI TAENVARKWQ LTREEQDEFA
LASQNKAEAA QKAGRFADEI VPFVVKTRKG DVNVDQDEYI RHGATLDSIA KLRPAFDKEG
TVTAGNASGL NDGAAAALLM TEAEAARRGI QPLARIVSWA TAGVDPQIMG TGPIPASRKA
LEKAGWSVAD IELVEANEAF AAQACAVNKD LGWDPSIVNV NGGAIAIGHP IGASGARVLN
TLLFEMKRRG VSKGLATLCI GGGMGVAMCV ERL
