3-ketoacyl-CoA thiolase, peroxisomal precursor - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P27796 (THIK_YEAST)

Last modified November 3, 2009. Version 97. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    3-ketoacyl-CoA thiolase, peroxisomal
    EC=2.3.1.16
Alternative name(s):
    Beta-ketothiolase
    Acetyl-CoA acyltransferase
    Peroxisomal 3-oxoacyl-CoA thiolase

Gene names

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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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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.

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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.

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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
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-acyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
PEX18	P38855	2	EBI-19236,EBI-24803
PEX7	P39108	3	EBI-19236,EBI-13183

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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

Acyl-thioester intermediate

Active site

375

Proton acceptor

Active site

403

Proton acceptor

Secondary structure

417

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P27796-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: B22AA06130829DE5
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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

« Hide

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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: 1715273] [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: 1872029] [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. Barrell B.G. Nature 387:84-87(1997) [PubMed: 9169870] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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: 8125978] [Abstract] Cited for: MUTAGENESIS OF N-TERMINAL PTS REGION.
[6]	"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: 7812714] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[7]	"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: 9402066] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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

PIR

S22784.

RefSeq

NP_012106.1.

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1504N.

IntAct

P27796. 4 interactions.

STRING

P27796.

Proteomic databases

PeptideAtlas

P27796.

Genome annotation databases

Ensembl

YIL160C; YIL160C; YIL160C; Saccharomyces cerevisiae. [Genome view]

GeneID

854646.

GenomeReviews

Gene locus YIL160C in contig Z47047_GR.

KEGG

sce:YIL160C.

NMPDR

fig|4932.3.peg.1626.

Organism-specific databases

CYGD

YIL160c.

SGD

S000001422. POT1.

Phylogenomic databases

HOGENOM

P27796.

OMA

PNTTMEG.

Enzyme and pathway databases

BRENDA

2.3.1.16. 250.

Gene expression databases

ArrayExpress

P27796.

Genevestigator

P27796.

GermOnline

YIL160C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002155. Thiolase.
IPR016038. Thiolase-like_subgr.
[Graphical view]

Gene3D

G3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.

PANTHER

PTHR18919. Thiolase. 1 hit.

Pfam

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

PIRSF

PIRSF000429. Ac-CoA_Ac_transf. 1 hit.

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 Resources

NextBio

977187.

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Entry information

Entry name

THIK_YEAST

Accession

Primary (citable) accession number: P27796

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	November 3, 2009
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents