ID E3N068_CAERE Unreviewed; 482 AA.
AC E3N068;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=CRE_12191 {ECO:0000313|EMBL:EFP13313.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS268504; EFP13313.1; -; Genomic_DNA.
DR RefSeq; XP_003098209.1; XM_003098161.1.
DR AlphaFoldDB; E3N068; -.
DR STRING; 31234.E3N068; -.
DR EnsemblMetazoa; CRE12191.1; CRE12191.1; WBGene00055204.
DR GeneID; 9800420; -.
DR KEGG; crq:GCK72_009313; -.
DR CTD; 9800420; -.
DR eggNOG; KOG1392; Eukaryota.
DR HOGENOM; CLU_031026_2_0_1; -.
DR InParanoid; E3N068; -.
DR OMA; MTAFPEP; -.
DR OrthoDB; 1826604at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
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; 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 SUPFAM; SSF53901; Thiolase-like; 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 {ECO:0000256|RuleBase:RU003557};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Transferase {ECO:0000256|RuleBase:RU003557};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..332
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 340..478
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 482 AA; 52125 MW; 18722E4CA9B81162 CRC64;
MIRKFLLFYT HWYLLFVIPC FTSRLIYVIF AFQKMLRAVS SSFGTARAAS TAVKRNTPNI
VLVDAVRTPF VVSGTVFKDL MAVDLQKEAI KALVEKTKLP YEKLDHIICG TVIQECKTSN
IAREAALLAG VPDNIPAHTV TLACISSNVA ITTGMGMLAT GNANAIIAGG VELLSDVPIR
YNRKARKAML GMNKAKDVPS KLKIGGEIVK NLLSPELPAV AEFSTGETMG HSGDRLAAAF
NVSRREQDEF AIRSHTLASE AAKNGKFTDV VPVFLDGKKP KTIKEDNGIR VSTIEKLSTL
KPAFVKPHGT VTAANASYLT DGASAALIMT EEYALANGFK PKAYLRDYLY VAQDPKDQLL
LSPAYVIPKL LDKAGLGLKD IDVFEIHEAF AGQVLANLNA MDSEYFCKEQ MKRSGKFGRV
PMDKLNLWGG SLSIGHPFGA TGVRLAAHSA HRLKEEKGQY AVIAACAAGG HGVGMLIEAY
GK
//
