THIL_ALLVD
ID THIL_ALLVD Reviewed; 394 AA.
AC P45369; D3RUY6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 116.
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:1396692};
GN Name=phaA {ECO:0000303|PubMed:1476773};
GN Synonyms=phbA {ECO:0000303|PubMed:1396692}; OrderedLocusNames=Alvin_0063;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=1396692; DOI=10.1111/j.1432-1033.1992.tb17270.x;
RA Liebergesell M., Steinbuechel A.;
RT "Cloning and nucleotide sequences of genes relevant for biosynthesis of
RT poly(3-hydroxybutyric acid) in Chromatium vinosum strain D.";
RL Eur. J. Biochem. 209:135-150(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
RN [3]
RP GENE NAME.
RX PubMed=1476773; DOI=10.1111/j.1574-6968.1992.tb05841.x;
RA Steinbuechel A., Hustede E., Liebergesell M., Pieper U., Timm A.,
RA Valentin H.;
RT "Molecular basis for biosynthesis and accumulation of polyhydroxyalkanoic
RT acids in bacteria.";
RL FEMS Microbiol. Rev. 9:217-230(1992).
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:1396692}.
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; L01112; AAA23322.1; -; Genomic_DNA.
DR EMBL; CP001896; ADC61035.1; -; Genomic_DNA.
DR PIR; S29276; S29276.
DR RefSeq; WP_012969311.1; NC_013851.1.
DR AlphaFoldDB; P45369; -.
DR SMR; P45369; -.
DR STRING; 572477.Alvin_0063; -.
DR PRIDE; P45369; -.
DR EnsemblBacteria; ADC61035; ADC61035; Alvin_0063.
DR KEGG; alv:Alvin_0063; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_6; -.
DR OMA; ICPSIAI; -.
DR OrthoDB; 1058688at2; -.
DR UniPathway; UPA00058; UER00101.
DR UniPathway; UPA00917; -.
DR Proteomes; UP000001441; 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..394
FT /note="Acetyl-CoA acetyltransferase"
FT /id="PRO_0000206419"
FT ACT_SITE 89
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT CONFLICT 2
FT /note="N -> S (in Ref. 1; AAA23322)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="S -> G (in Ref. 1; AAA23322)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="K -> H (in Ref. 1; AAA23322)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="R -> K (in Ref. 1; AAA23322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 41129 MW; 8AECC7EB26B29344 CRC64;
MNENIVIVDA GRSAIGTFSG SLSSLSATEI GTAVLKGLLA RTGLAPEQID EVILGQVLTA
GVGQNPARQT TLKAGLPHSV PAMTINKVCG SGLKAVHLAM QAIACGDADI VIAGGQESMS
QSSHVLPRSR DGQRMGDWSM KDTMIVDGLW DAFNNYHMGT TAENIAQKYG FTREQQDAFA
AASQQKTEAA QKAGRFQDEI IPIEIPQRKG DPKVFDADEF PRHGTTAESL GKLRPAFSRD
GSVTAGNASG INDGAAMVVV MKESKAKELG LKPMARLVAF ASAGVDPAIM GTGPIPASTK
CLEKAGWTPA DLDLIEANEA FAAQAMSVNQ DMGWDLSKVN VNGGAIAIGH PIGASGARVL
VTLLYEMQKR DAKKGLATLC IGGGQGVALA VERM
