THIL_YARLI
ID THIL_YARLI Reviewed; 397 AA.
AC Q6L8K7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Acetyl-CoA acetyltransferase;
DE EC=2.3.1.9;
DE AltName: Full=Peroxisomal acetoacetyl-CoA thiolase;
DE Short=Thiolase;
GN Name=PAT1; OrderedLocusNames=YALI0E11099g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CXAU1;
RX PubMed=11401539; DOI=10.1006/bbrc.2001.4653;
RA Yamagami S., Iida T., Nagata Y., Ohta A., Takagi M.;
RT "Isolation and characterization of acetoacetyl-CoA thiolase gene essential
RT for n-decane assimilation in yeast Yarrowia lipolytica.";
RL Biochem. Biophys. Res. Commun. 282:832-838(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Essential for n-decane utilization.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; AB120846; BAD20191.1; -; Genomic_DNA.
DR EMBL; CR382131; CAG79399.1; -; Genomic_DNA.
DR PIR; JC7675; JC7675.
DR RefSeq; XP_503808.1; XM_503808.1.
DR AlphaFoldDB; Q6L8K7; -.
DR SMR; Q6L8K7; -.
DR STRING; 4952.CAG79399; -.
DR EnsemblFungi; CAG79399; CAG79399; YALI0_E11099g.
DR GeneID; 2911520; -.
DR KEGG; yli:YALI0E11099g; -.
DR VEuPathDB; FungiDB:YALI0_E11099g; -.
DR HOGENOM; CLU_031026_0_0_1; -.
DR InParanoid; Q6L8K7; -.
DR OMA; MPEAYVI; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
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; 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.
PE 3: Inferred from homology;
KW Acyltransferase; Metal-binding; Peroxisome; Potassium; Reference proteome;
KW Transferase.
FT CHAIN 1..397
FT /note="Acetyl-CoA acetyltransferase"
FT /id="PRO_0000206415"
FT ACT_SITE 95
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 351
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
SQ SEQUENCE 397 AA; 41357 MW; 84CFBCE9D5A29EE0 CRC64;
MRLTLPRLNA AYIVGAARTP VGKFNGALKS VSAIDLGITA AKAAVQRSKV PADQIDEFLF
GQVLTANSGQ APARQVVIKG GFPESVEATT INKVCSSGLK TVALAAQAIK AGDRNVIVAG
GMESMSNTPY YSGRGLVFGN QKLEDSIVKD GLWDPYNNIH MGNCCENTNK RDGITREQQD
EYAIESYRRA NESIKNGAFK DEIVPVEIKT RKGTVTVSED EEPKGANAEK LKGLKPVFDK
QGSVTAGNAS PINDGASAVV VASGTKAKEL GTPVLAKIVS YADAATAPID FTIAPSLAIP
AALKKAGLTK DDIALWEINE AFSGVALANL MRLGIDKSKV NVKGGAVALG HPIGASGNRI
FVTLVNALKE GEYGVAAICN GGGASTAIVI KKVSSVE
