ID B0T3Y8_CAUSK Unreviewed; 395 AA.
AC B0T3Y8;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ABZ73872.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:ABZ73872.1};
GN OrderedLocusNames=Caul_4752 {ECO:0000313|EMBL:ABZ73872.1};
OS Caulobacter sp. (strain K31).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ73872.1};
RN [1] {ECO:0000313|EMBL:ABZ73872.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31 {ECO:0000313|EMBL:ABZ73872.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-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; CP000927; ABZ73872.1; -; Genomic_DNA.
DR AlphaFoldDB; B0T3Y8; -.
DR STRING; 366602.Caul_4752; -.
DR KEGG; cak:Caul_4752; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_1_1_5; -.
DR OrthoDB; 9764638at2; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase 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; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF22; ACETYL-COA ACETYLTRANSFERASE; 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; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:ABZ73872.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ABZ73872.1}.
FT DOMAIN 5..264
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 273..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 351
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 395 AA; 41928 MW; B44F93C136D4DBF9 CRC64;
MREAVIVSYA RTGLAKSNRG GFNNTHGAAM AGHAIQHAVS RAKLEGAEVE DVALGCGGPE
GATGMNVARN AAIWAGLPVT TSGQTINRFC SSGLQAIATA ANYIRNDGAQ VAIGGGVESI
SLVQGGGHMN RFHITEEKLM REKPALWMAM IDTADIVAKR YNISREYQDE YSLRSQQRIA
AAQASGLFDD EIVPMATKMK VVNKETKEES LVDYVVTKDE CNRPETTLEG LASLKPVMGE
GNFVTAGNAS QLSDGAAALV LMDAKEAAHR NLEPLGLFKG FAVAGCEPDE MGIGPVFAVP
RLLERHGLKV DDIDLWELNE AFASQCLYSR DRLGIDPEKY NVNGGSIAIG HPFGMTGARC
AGHLLLEGKR RGAKLGVVTM CIGGGMGAAG LFEIF
//
