THIK_YEAST
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 03-AUG-2022, entry version 203.
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.
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 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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
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).
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 -!- 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. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22984289}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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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; 277.
DR DIP; DIP-1504N; -.
DR IntAct; P27796; 4.
DR MINT; P27796; -.
DR STRING; 4932.YIL160C; -.
DR SwissLipids; SLP:000001408; -.
DR UCD-2DPAGE; P27796; -.
DR PaxDb; P27796; -.
DR PRIDE; P27796; -.
DR EnsemblFungi; YIL160C_mRNA; YIL160C; YIL160C.
DR GeneID; 854646; -.
DR KEGG; sce:YIL160C; -.
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; DYYWGMG; -.
DR BioCyc; MetaCyc:YIL160C-MON; -.
DR BioCyc; YEAST:YIL160C-MON; -.
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 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 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 3D-structure; Acyltransferase; Fatty acid metabolism; Lipid metabolism;
KW Mitochondrion; Peroxisome; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Peroxisome"
FT CHAIN ?..417
FT /note="3-ketoacyl-CoA thiolase, peroxisomal"
FT /id="PRO_0000034078"
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
