THIK_YARLI
ID THIK_YARLI Reviewed; 414 AA.
AC Q05493;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 129.
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=POT1; OrderedLocusNames=YALI0E18568g;
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].
RX PubMed=7916689; DOI=10.1111/j.1432-1033.1993.tb18180.x;
RA Berninger G., Schmidtchen R., Casel G., Knoerr A., Rautenstrauss K.,
RA Kunau W.-H., Schweizer E.;
RT "Structure and metabolic control of the Yarrowia lipolytica peroxisomal 3-
RT oxoacyl-CoA-thiolase gene.";
RL Eur. J. Biochem. 216:607-613(1993).
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 -!- 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.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; X69988; CAA49605.1; -; Genomic_DNA.
DR EMBL; CR382131; CAG79704.1; -; Genomic_DNA.
DR PIR; S36838; S36838.
DR RefSeq; XP_504109.1; XM_504109.1.
DR AlphaFoldDB; Q05493; -.
DR SMR; Q05493; -.
DR STRING; 4952.CAG79704; -.
DR EnsemblFungi; CAG79704; CAG79704; YALI0_E18568g.
DR GeneID; 2912002; -.
DR KEGG; yli:YALI0E18568g; -.
DR VEuPathDB; FungiDB:YALI0_E18568g; -.
DR HOGENOM; CLU_031026_1_1_1; -.
DR InParanoid; Q05493; -.
DR OMA; DYYWGMG; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0010124; P:phenylacetate catabolic process; 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; 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 3: Inferred from homology;
KW Acyltransferase; Fatty acid metabolism; Lipid metabolism; Peroxisome;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Peroxisome"
FT CHAIN ?..414
FT /note="3-ketoacyl-CoA thiolase, peroxisomal"
FT /id="PRO_0000034077"
FT ACT_SITE 115
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 370
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 400
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ SEQUENCE 414 AA; 43059 MW; 29D5F83A8FC792B1 CRC64;
MDRLNNLATQ LEQNPAKGLD AITSKNPDDV VITAAYRTAH TKGGKGLFKD TSSSELLASL
LEGLVKESKI DPKLIGDVVC GNVLAAGAGA TEHRAACLVA GIPETVPFVA LNRQCSSGLM
AVNDVANKIR AGQIDIGIGC GVESMSNQYG PNSVTPFSNK FQNNEEAKKC LIPMGITSEN
VAAKYNVSRK AQDAFAAKSY EKAAAAQAAG KFDQEILPIK TTVLDDDDNE KEVTVNKDDG
IRPGVTAEKL GKLKPAFSAE GTTHAGNASQ ISDGAGAVLL MRRSVAEKLG QPILAKFVHC
KTVGVPPELM GIGPAYAIPA VLEDLGLTVN DVDVFEINEA FASQALFSIQ HCGIDESKVN
PRGGAIAIGH PLGATGARQF ATLLSELKES GKKVGVTSMC IGTGMGAASL VVAE