P27796 (THIK_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-ketoacyl-CoA thiolase, peroxisomal
EC=2.3.1.16

Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Peroxisomal 3-oxoacyl-CoA thiolase

Gene names

Name:	POT1
Synonyms:	FOX3, POX3
Ordered Locus Names:	YIL160C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
Pathway	Lipid metabolism; fatty acid metabolism.
Subunit structure	Homodimer.
Subcellular location	Peroxisome.
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Domain	Transit peptide
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation Inferred from mutant phenotype PubMed 12819196. Source: SGD
Cellular_component	mitochondrial intermembrane space Inferred from direct assay PubMed 22984289. Source: SGD peroxisomal matrix Inferred from direct assay PubMed 7754706Ref.6. Source: SGD
Molecular_function	acetyl-CoA C-acyltransferase activity Inferred from direct assay PubMed 7754706. Source: SGD mRNA binding Inferred from direct assay PubMed 21124907. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PEX7	P39108	3	EBI-19236,EBI-13183

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Peroxisome

Chain

? – 417

3-ketoacyl-CoA thiolase, peroxisomal

PRO_0000034078

Sites

Active site

125

1

Acyl-thioester intermediate

Active site

375

1

Proton acceptor

Active site

403

1

Proton acceptor

Secondary structure

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417

Helix Strand Turn

Details...

Turn

26 – 29

4

Beta strand

36 – 43

8

Turn

49 – 51

3

Turn

53 – 56

4

Helix

59 – 72

14

Helix

76 – 79

4

Helix

82 – 84

3

Beta strand

88 – 91

4

Beta strand

93 – 96

4

Helix

97 – 99

3

Helix

100 – 109

10

Beta strand

118 – 122

5

Helix

124 – 126

3

Helix

127 – 140

14

Beta strand

145 – 154

10

Helix

155 – 158

4

Helix

159 – 161

3

Helix

171 – 175

5

Helix

179 – 183

5

Helix

186 – 196

11

Helix

201 – 220

20

Turn

225 – 227

3

Helix

251 – 255

5

Turn

270 – 272

3

Beta strand

276 – 287

12

Helix

288 – 293

6

Beta strand

300 – 309

10

Helix

312 – 317

6

Helix

318 – 330

13

Helix

334 – 336

3

Beta strand

338 – 342

5

Helix

347 – 357

11

Helix

361 – 363

3

Helix

370 – 373

4

Turn

377 – 379

3

Helix

380 – 391

12

Beta strand

397 – 404

8

Turn

405 – 407

3

Beta strand

408 – 416

9

Sequences

	Sequence		Length	Mass (Da)
	P27796 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: B22AA06130829DE5	FASTA	417	44,730
	10 20 30 40 50 60 MSQRLQSIKD HLVESAMGKG ESKRKNSLLE KRPEDVVIVA ANRSAIGKGF KGAFKDVNTD 70 80 90 100 110 120 YLLYNFLNEF IGRFPEPLRA DLNLIEEVAC GNVLNVGAGA TEHRAACLAS GIPYSTPFVA 130 140 150 160 170 180 LNRQCSSGLT AVNDIANKIK VGQIDIGLAL GVESMTNNYK NVNPLGMISS EELQKNREAK 190 200 210 220 230 240 KCLIPMGITN ENVAANFKIS RKDQDEFAAN SYQKAYKAKN EGLFEDEILP IKLPDGSICQ 250 260 270 280 290 300 SDEGPRPNVT AESLSSIRPA FIKDRGTTTA GNASQVSDGV AGVLLARRSV ANQLNLPVLG 310 320 330 340 350 360 RYIDFQTVGV PPEIMGVGPA YAIPKVLEAT GLQVQDIDIF EINEAFAAQA LYCIHKLGID 370 380 390 400 410 LNKVNPRGGA IALGHPLGCT GARQVATILR ELKKDQIGVV SMCIGTGMGA AAIFIKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulation of transcription of the gene coding for peroxisomal 3-oxoacyl-CoA thiolase of Saccharomyces cerevisiae." Einerhand A.W.C., Voorn-Brouwer M.M., Erdmann R., Kunau W.H., Tabak H.F. Eur. J. Biochem. 200:113-122(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BJ1991.
[2]	"A new glucose-repressible gene identified from the analysis of chromatin structure in deletion mutants of yeast SUC2 locus." Igual J.C., Matallana E., Gonzalez-Bosch C., Franco L., Perez-Ortin J.E. Yeast 7:379-389(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Mutagenesis of the amino targeting signal of Saccharomyces cerevisiae 3-ketoacyl-CoA thiolase reveals conserved amino acids required for import into peroxisomes in vivo." Glover J.R., Andrews D.W., Subramani S., Rachubinski R.A. J. Biol. Chem. 269:7558-7563(1994) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF N-TERMINAL PTS REGION.
[7]	"The 2.8 A crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: a five-layered alpha beta alpha beta alpha structure constructed from two core domains of identical topology." Mathieu M., Zeelen J.P., Pauptit R.A., Erdmann R., Kunau W.-H., Wierenga R.K. Structure 2:797-808(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[8]	"The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism." Mathieu M., Modis Y., Zeelen J.P., Engel C.K., Abagyan R.A., Ahlberg A., Rasmussen B., Lamzin V.S., Kunau W.H., Wierenga R.K. J. Mol. Biol. 273:714-728(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z38059 Genomic DNA. Translation: CAA86118.1.
X53946 Genomic DNA. Translation: CAA37893.1.
X53395 Genomic DNA. Translation: CAA37472.1.
AY693184 Genomic DNA. Translation: AAT93203.1.
BK006942 Genomic DNA. Translation: DAA08392.1.

PIR

S22784.

RefSeq

NP_012106.1. NM_001179508.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AFW	X-ray	1.80	A/B	25-417	[»]
1AFY	model	-	A/B	25-417	[»]
1PXT	X-ray	2.80	A/B	28-417	[»]

ProteinModelPortal

P27796.

SMR

P27796. Positions 25-417.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1504N.

IntAct

P27796. 3 interactions.

MINT

MINT-412295.

STRING

4932.YIL160C.

2D gel databases

UCD-2DPAGE

P27796.

Proteomic databases

PaxDb

P27796.

PeptideAtlas

P27796.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YIL160C; YIL160C; YIL160C.

GeneID

854646.

KEGG

sce:YIL160C.

Organism-specific databases

CYGD

YIL160c.

SGD

S000001422. POT1.

Phylogenomic databases

eggNOG

COG0183.

GeneTree

ENSGT00620000087956.

HOGENOM

HOG000012239.

KO

K00632.

OMA

TIYSARE.

OrthoDB

EOG45MRDV.

Enzyme and pathway databases

UniPathway

UPA00199.

Gene expression databases

Genevestigator

P27796.

GermOnline

YIL160C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.40.47.10. 4 hits.

InterPro

IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]

PANTHER

PTHR18919. PTHR18919. 1 hit.

Pfam

PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000429. Ac-CoA_Ac_transf. 1 hit.

SUPFAM

SSF53901. Thiolase-like. 2 hits.

TIGRFAMs

TIGR01930. AcCoA-C-Actrans. 1 hit.

PROSITE

PS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P27796.

NextBio

977187.

Entry information

Entry name

THIK_YEAST

Accession

Primary (citable) accession number: P27796
Secondary accession number(s): D6VVC6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	April 3, 2013
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program