ID Q11CY0_CHESB Unreviewed; 393 AA.
AC Q11CY0;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ABG64745.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:ABG64745.1};
DE Flags: Precursor;
GN OrderedLocusNames=Meso_3374 {ECO:0000313|EMBL:ABG64745.1};
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans.
OX NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG64745.1};
RN [1] {ECO:0000313|EMBL:ABG64745.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BNC1 {ECO:0000313|EMBL:ABG64745.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL Submitted (JUN-2006) 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; CP000390; ABG64745.1; -; Genomic_DNA.
DR AlphaFoldDB; Q11CY0; -.
DR STRING; 266779.Meso_3374; -.
DR KEGG; mes:Meso_3374; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_5; -.
DR OrthoDB; 9764638at2; -.
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; 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; 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; 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:ABG64745.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ABG64745.1}.
FT DOMAIN 7..264
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 272..393
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
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 393 AA; 41052 MW; 2CB56E22E867BC41 CRC64;
MASSNSVVIA SAARTPVGSF NGSFAQIPAH QLGASVIRAV LERAKVAADE VNEVILGQVL
TAGQGQNPAR QAAVAAGLLA ETTAWGVNQV CGSGLRAAAL GMQQIACGDA KIVIAGGQES
MSLSPHCAHL RSGVKMGDYA MIDTMIRDGL WDAFNGYHMG ITAENVARAF QITRDEQDRF
ALASQNKAEA AQKAGRFRDE IAAVTVKTRK GDEVVENDEY IRIGATLEAM QKLRPAFDRE
GTVTAGNASG INDGAAALLL ISEEEASRRG IEPMARIASW ATAGVDPAVM GTGPIPASRK
ALEKAGWRAA DLDLVEANEA FAAQACAVNK EMGWNPDIVN VNGGAIAIGH PIGASGARIL
NTLLYEMRRR NAKRGLATLC IGGGMGVAMC VER
//
