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Reviewed, UniProtKB/Swiss-Prot P27796 (THIK_YEAST)

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

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processfatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacetyl-CoA C-acyltransferase activity

Inferred from electronic annotation. Source: EC

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PEX18P388552EBI-19236,EBI-24803
PEX7P391083EBI-19236,EBI-13183

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Peroxisome
Chain? – 4173-ketoacyl-CoA thiolase, peroxisomalPRO_0000034078

Sites

Active site1251Acyl-thioester intermediate
Active site3751Proton acceptor
Active site4031Proton acceptor

Secondary structure

..................................................................... 417
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27796-1 [UniParc].

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

FASTA41744,730
        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

References

« Hide '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. expand/collapse author list , 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: 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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., 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.

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.
PIRS22784.
RefSeqNP_012106.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AFWX-ray1.80A/B25-417[»]
1AFYmodel-A/B25-417[»]
1PXTX-ray2.80A/B28-417[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:1504N.
IntActP27796. 4 interactions.
STRINGP27796.

Proteomic databases

PeptideAtlasP27796.

Genome annotation databases

EnsemblYIL160C; YIL160C; YIL160C; Saccharomyces cerevisiae. [Genome view]
GeneID854646.
GenomeReviewsGene locus YIL160C in contig Z47047_GR.
KEGGsce:YIL160C.
NMPDRfig|4932.3.peg.1626.

Organism-specific databases

CYGDYIL160c.
SGDS000001422. POT1.

Phylogenomic databases

HOGENOMP27796.
OMAPNTTMEG.

Enzyme and pathway databases

BRENDA2.3.1.16. 250.

Gene expression databases

ArrayExpressP27796.
GenevestigatorP27796.
GermOnlineYIL160C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR002155. Thiolase.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHERPTHR18919. Thiolase. 1 hit.
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
TIGRFAMsTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio977187.

Entry information

Entry nameTHIK_YEAST
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents