ID B2UFU4_RALPJ Unreviewed; 394 AA.
AC B2UFU4;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ACD27045.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:ACD27045.1};
GN OrderedLocusNames=Rpic_1910 {ECO:0000313|EMBL:ACD27045.1};
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD27045.1};
RN [1] {ECO:0000313|EMBL:ACD27045.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=12J {ECO:0000313|EMBL:ACD27045.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome1 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP001068; ACD27045.1; -; Genomic_DNA.
DR AlphaFoldDB; B2UFU4; -.
DR STRING; 402626.Rpic_1910; -.
DR KEGG; rpi:Rpic_1910; -.
DR PATRIC; fig|402626.5.peg.3062; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_4; -.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
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; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:ACD27045.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ACD27045.1}.
FT DOMAIN 5..264
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..393
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 41182 MW; 2FA9AEEAB38FE827 CRC64;
MAREVVVVSG VRTAIGTFGG SLKDVAPCEL GALVVREALA RAGVKGEDVG HVVFGHVINT
EPRDMYLSRV AAVNGGVSAE TPAFNVNRLC GSGLQAVVSA AQTVLLGDAD IAIAGGAESM
SRAPYLAPAA RWGSRMGDAK MVDMMLGALH DPFHTIHMGV TAENVAREFG ISREQQDQTA
LESHQRASRA IQAGYFKDQI VPVTIKSRKG DIQFDTDEHV RHDATIDDMT KLKPVFTKEN
GTVTAGNASG LNDAGAALVL MERSVAEKRG LKPLARLVSY GHAGVDPKIM GIGPVPATRK
ALERAGLSVK DLDVIEANEA FAAQACAVTK ELGLDPAKVN PNGSGISLGH PIGATGALIT
VKALHELQRI GGRYALVTMC IGGGQGIAAV FERI
//
