ID THIK_YEAST Reviewed; 417 AA. AC P27796; D6VVC6; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 27-MAR-2024, entry version 210. 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; Synonyms=FOX3, POX3; OrderedLocusNames=YIL160C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BJ1991; RX PubMed=1715273; DOI=10.1111/j.1432-1033.1991.tb21056.x; RA Einerhand A.W.C., Voorn-Brouwer M.M., Erdmann R., Kunau W.H., Tabak H.F.; RT "Regulation of transcription of the gene coding for peroxisomal 3-oxoacyl- RT CoA thiolase of Saccharomyces cerevisiae."; RL Eur. J. Biochem. 200:113-122(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=1872029; DOI=10.1002/yea.320070408; RA Igual J.C., Matallana E., Gonzalez-Bosch C., Franco L., Perez-Ortin J.E.; RT "A new glucose-repressible gene identified from the analysis of chromatin RT structure in deletion mutants of yeast SUC2 locus."; RL Yeast 7:379-389(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169870; RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C., RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., RA Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."; RL Nature 387:84-87(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [6] RP MUTAGENESIS OF N-TERMINAL PTS REGION, SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=8125978; DOI=10.1016/s0021-9258(17)37323-4; RA Glover J.R., Andrews D.W., Subramani S., Rachubinski R.A.; RT "Mutagenesis of the amino targeting signal of Saccharomyces cerevisiae 3- RT ketoacyl-CoA thiolase reveals conserved amino acids required for import RT into peroxisomes in vivo."; RL J. Biol. Chem. 269:7558-7563(1994). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION. RX PubMed=7754706; DOI=10.1002/yea.320100905; RA Erdmann R., Kunau W.H.; RT "Purification and immunolocalization of the peroxisomal 3-oxoacyl-CoA RT thiolase from Saccharomyces cerevisiae."; RL Yeast 10:1173-1182(1994). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RX PubMed=22984289; DOI=10.1074/mcp.m112.021105; RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J., RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.; RT "Intermembrane space proteome of yeast mitochondria."; RL Mol. Cell. Proteomics 11:1840-1852(2012). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SUBUNIT. RX PubMed=7812714; DOI=10.1016/s0969-2126(94)00081-6; RA Mathieu M., Zeelen J.P., Pauptit R.A., Erdmann R., Kunau W.-H., RA Wierenga R.K.; RT "The 2.8 A crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of RT Saccharomyces cerevisiae: a five-layered alpha beta alpha beta alpha RT structure constructed from two core domains of identical topology."; RL Structure 2:797-808(1994). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND SUBUNIT. RX PubMed=9402066; DOI=10.1006/jmbi.1997.1331; RA Mathieu M., Modis Y., Zeelen J.P., Engel C.K., Abagyan R.A., Ahlberg A., RA Rasmussen B., Lamzin V.S., Kunau W.H., Wierenga R.K.; RT "The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA RT thiolase of Saccharomyces cerevisiae: implications for substrate binding RT and reaction mechanism."; RL J. Mol. Biol. 273:714-728(1997). RN [11] {ECO:0007744|PDB:3W15} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-15 IN COMPLEX WITH PEX7 AND RP PEX21. RX PubMed=23812376; DOI=10.1038/nsmb.2618; RA Pan D., Nakatsu T., Kato H.; RT "Crystal structure of peroxisomal targeting signal-2 bound to its receptor RT complex Pex7p-Pex21p."; RL Nat. Struct. Mol. Biol. 20:987-993(2013). CC -!- FUNCTION: Responsible for the thiolytic cleavage of straight chain 3- CC keto fatty acyl-CoAs (3-oxoacyl-CoAs). {ECO:0000305|PubMed:7754706}. 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 Evidence={ECO:0000305|PubMed:7754706}; CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism. CC {ECO:0000305|PubMed:7754706}. CC -!- SUBUNIT: Homodimer (PubMed:7812714, PubMed:9402066). Interacts (via CC PTS2-type peroxisomal targeting signal region) with PEX7; leading to CC its translocation into peroxisomes (PubMed:23812376). CC {ECO:0000269|PubMed:23812376, ECO:0000269|PubMed:7812714, CC ECO:0000269|PubMed:9402066}. CC -!- INTERACTION: CC P27796; P50091: PEX21; NbExp=5; IntAct=EBI-19236, EBI-23549; CC P27796; P39108: PEX7; NbExp=5; IntAct=EBI-19236, EBI-13183; CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:7754706, CC ECO:0000269|PubMed:8125978}. Mitochondrion intermembrane space CC {ECO:0000269|PubMed:22984289}. CC -!- DOMAIN: The PTS2-type peroxisomal targeting signal, which mediates CC interaction with PEX7 and localization to peroxisomes, is cleaved CC following import into peroxisomes. {ECO:0000305|PubMed:23812376, CC ECO:0000305|PubMed:8125978}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family. CC {ECO:0000305}. 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; Z38059; CAA86118.1; -; Genomic_DNA. DR EMBL; X53946; CAA37893.1; -; Genomic_DNA. DR EMBL; X53395; CAA37472.1; -; Genomic_DNA. DR EMBL; AY693184; AAT93203.1; -; Genomic_DNA. DR EMBL; BK006942; DAA08392.1; -; Genomic_DNA. DR PIR; S22784; S22784. DR RefSeq; NP_012106.1; NM_001179508.1. DR PDB; 1AFW; X-ray; 1.80 A; A/B=25-417. DR PDB; 1PXT; X-ray; 2.80 A; A/B=28-417. DR PDB; 3W15; X-ray; 1.80 A; C=1-15. DR PDBsum; 1AFW; -. DR PDBsum; 1PXT; -. DR PDBsum; 3W15; -. DR AlphaFoldDB; P27796; -. DR SMR; P27796; -. DR BioGRID; 34832; 278. DR DIP; DIP-1504N; -. DR IntAct; P27796; 4. DR MINT; P27796; -. DR STRING; 4932.YIL160C; -. DR SwissLipids; SLP:000001408; -. DR PaxDb; 4932-YIL160C; -. DR PeptideAtlas; P27796; -. DR EnsemblFungi; YIL160C_mRNA; YIL160C; YIL160C. DR GeneID; 854646; -. DR KEGG; sce:YIL160C; -. DR AGR; SGD:S000001422; -. DR SGD; S000001422; POT1. DR VEuPathDB; FungiDB:YIL160C; -. DR eggNOG; KOG1389; Eukaryota. DR GeneTree; ENSGT01030000234626; -. DR HOGENOM; CLU_031026_1_1_1; -. DR InParanoid; P27796; -. DR OMA; MTAFPEP; -. DR OrthoDB; 5481312at2759; -. DR BioCyc; MetaCyc:YIL160C-MONOMER; -. DR BioCyc; YEAST:YIL160C-MONOMER; -. DR BRENDA; 2.3.1.16; 984. DR Reactome; R-SCE-2046106; alpha-linolenic acid (ALA) metabolism. DR Reactome; R-SCE-390247; Beta-oxidation of very long chain fatty acids. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR Reactome; R-SCE-9033241; Peroxisomal protein import. DR UniPathway; UPA00199; -. DR BioGRID-ORCS; 854646; 2 hits in 10 CRISPR screens. DR EvolutionaryTrace; P27796; -. DR PRO; PR:P27796; -. DR Proteomes; UP000002311; Chromosome IX. DR RNAct; P27796; Protein. DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD. DR GO; GO:0005782; C:peroxisomal matrix; IDA:SGD. DR GO; GO:0005777; C:peroxisome; IDA:SGD. DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IDA:SGD. DR GO; GO:0003729; F:mRNA binding; IDA:SGD. DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:SGD. 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 NCBIfam; TIGR01930; AcCoA-C-Actrans; 1. DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1. DR PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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; PS00098; THIOLASE_1; 1. DR PROSITE; PS00737; THIOLASE_2; 1. DR PROSITE; PS00099; THIOLASE_3; 1. DR UCD-2DPAGE; P27796; -. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Fatty acid metabolism; Lipid metabolism; KW Mitochondrion; Peroxisome; Reference proteome; Transferase; KW Transit peptide. FT TRANSIT 1..15 FT /note="Peroxisome" FT /evidence="ECO:0000305|PubMed:23812376" FT CHAIN 16..417 FT /note="3-ketoacyl-CoA thiolase, peroxisomal" FT /evidence="ECO:0000305|PubMed:23812376" FT /id="PRO_0000034078" FT REGION 1..15 FT /note="PTS2-type peroxisomal targeting signal" FT /evidence="ECO:0000269|PubMed:23812376" FT ACT_SITE 125 FT /note="Acyl-thioester intermediate" FT ACT_SITE 375 FT /note="Proton acceptor" FT ACT_SITE 403 FT /note="Proton acceptor" FT HELIX 1..15 FT /evidence="ECO:0007829|PDB:3W15" FT TURN 26..29 FT /evidence="ECO:0007829|PDB:1AFW" FT STRAND 36..43 FT /evidence="ECO:0007829|PDB:1AFW" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:1AFW" FT TURN 53..56 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 59..72 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 76..79 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:1AFW" FT STRAND 88..91 FT /evidence="ECO:0007829|PDB:1AFW" FT STRAND 93..96 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 100..109 FT /evidence="ECO:0007829|PDB:1AFW" FT STRAND 118..122 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 127..140 FT /evidence="ECO:0007829|PDB:1AFW" FT STRAND 145..154 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 155..158 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 171..175 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 179..183 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 186..196 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 201..220 FT /evidence="ECO:0007829|PDB:1AFW" FT TURN 225..227 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 251..255 FT /evidence="ECO:0007829|PDB:1AFW" FT TURN 263..265 FT /evidence="ECO:0007829|PDB:1AFW" FT TURN 270..272 FT /evidence="ECO:0007829|PDB:1AFW" FT STRAND 276..287 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 288..293 FT /evidence="ECO:0007829|PDB:1AFW" FT STRAND 300..309 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 312..317 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 318..330 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 334..336 FT /evidence="ECO:0007829|PDB:1AFW" FT STRAND 338..342 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 347..357 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 361..363 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 370..373 FT /evidence="ECO:0007829|PDB:1AFW" FT TURN 377..379 FT /evidence="ECO:0007829|PDB:1AFW" FT HELIX 380..391 FT /evidence="ECO:0007829|PDB:1AFW" FT STRAND 397..404 FT /evidence="ECO:0007829|PDB:1AFW" FT TURN 405..407 FT /evidence="ECO:0007829|PDB:1AFW" FT STRAND 408..416 FT /evidence="ECO:0007829|PDB:1AFW" SQ SEQUENCE 417 AA; 44730 MW; B22AA06130829DE5 CRC64; MSQRLQSIKD HLVESAMGKG ESKRKNSLLE KRPEDVVIVA ANRSAIGKGF KGAFKDVNTD YLLYNFLNEF IGRFPEPLRA DLNLIEEVAC GNVLNVGAGA TEHRAACLAS GIPYSTPFVA LNRQCSSGLT AVNDIANKIK VGQIDIGLAL GVESMTNNYK NVNPLGMISS EELQKNREAK KCLIPMGITN ENVAANFKIS RKDQDEFAAN SYQKAYKAKN EGLFEDEILP IKLPDGSICQ SDEGPRPNVT AESLSSIRPA FIKDRGTTTA GNASQVSDGV AGVLLARRSV ANQLNLPVLG RYIDFQTVGV PPEIMGVGPA YAIPKVLEAT GLQVQDIDIF EINEAFAAQA LYCIHKLGID LNKVNPRGGA IALGHPLGCT GARQVATILR ELKKDQIGVV SMCIGTGMGA AAIFIKE //