ID   THIK_ENCCU              Reviewed;         391 AA.
AC   Q8SVA6;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=3-ketoacyl-CoA thiolase, peroxisomal;
DE            EC=2.3.1.16;
DE   AltName: Full=Acetyl-CoA acyltransferase;
DE   AltName: Full=Beta-ketothiolase;
DE   AltName: Full=Peroxisomal 3-oxoacyl-CoA thiolase;
DE   Flags: Precursor;
GN   Name=FOX3; OrderedLocusNames=ECU06_0940;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC         Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; AL590446; CAD25454.1; -; Genomic_DNA.
DR   RefSeq; NP_585850.1; NM_001041472.1.
DR   AlphaFoldDB; Q8SVA6; -.
DR   SMR; Q8SVA6; -.
DR   STRING; 284813.Q8SVA6; -.
DR   GeneID; 859275; -.
DR   KEGG; ecu:ECU06_0940; -.
DR   VEuPathDB; MicrosporidiaDB:ECU06_0940; -.
DR   HOGENOM; CLU_031026_1_1_1; -.
DR   InParanoid; Q8SVA6; -.
DR   OMA; GIWEINE; -.
DR   OrthoDB; 1129049at2759; -.
DR   UniPathway; UPA00199; -.
DR   Proteomes; UP000000819; Chromosome VI.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
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   1: Evidence at protein level;
KW   Acyltransferase; Fatty acid metabolism; Lipid metabolism; Peroxisome;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Peroxisome"
FT   CHAIN           ?..391
FT                   /note="3-ketoacyl-CoA thiolase, peroxisomal"
FT                   /id="PRO_0000381750"
FT   ACT_SITE        92
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        335
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT   ACT_SITE        366
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ   SEQUENCE   391 AA;  41775 MW;  53A83C24FD04B71B CRC64;
     MISHEDVVVV GALRTPIGRA TRGKLRSLRN DELVTAAIRG IIEKTGIDPR LIEEVILGHC
     LSSMEGNVAA RMGVLRAGVP VETPVMIINR LCGSGLESVG LIAEKIRSGR IEIGLAGGFE
     SMTSYGLPKE YTLSRGGACE DAEDCMLTLG EVSEMLGKTH GVTRSEADEY AVTSQKRALE
     ATKKGHFLAE IIPMRVGDET VERDEGIRET SLGTIESLKP VFRQDGVCTS ANSSQLSDGA
     SAVLLMKRRR ADELGLPVVA EFIDFIAVGL KPRDMGLGPV VAIEKLLKRN GLEKDQISYF
     EINEAFASQV LCCLRKLQIG EDRVNRYGGS IALGHPIGAS GARIVCTLLS VMKNEALEGY
     GVASLCVGAG HGVAALFRRA AGSKPQDIKN T