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P27796 (THIK_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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 [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] [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. 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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. 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] [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.
PIRS22784.
RefSeqNP_012106.1. NM_001179508.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AFWX-ray1.80A/B25-417[»]
1AFYmodel-A/B25-417[»]
1PXTX-ray2.80A/B28-417[»]
3W15X-ray1.80C1-15[»]
ProteinModelPortalP27796.
SMRP27796. Positions 25-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34832. 69 interactions.
DIPDIP-1504N.
IntActP27796. 3 interactions.
MINTMINT-412295.
STRING4932.YIL160C.

2D gel databases

UCD-2DPAGEP27796.

Proteomic databases

PaxDbP27796.
PeptideAtlasP27796.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL160C; YIL160C; YIL160C.
GeneID854646.
KEGGsce:YIL160C.

Organism-specific databases

CYGDYIL160c.
SGDS000001422. POT1.

Phylogenomic databases

eggNOGCOG0183.
GeneTreeENSGT00750000117749.
HOGENOMHOG000012239.
KOK00632.
OMALYGVESM.
OrthoDBEOG7PCJSX.

Enzyme and pathway databases

BioCycMetaCyc:YIL160C-MONOMER.
YEAST:YIL160C-MONOMER.
UniPathwayUPA00199.

Gene expression databases

GenevestigatorP27796.

Family and domain databases

Gene3D3.40.47.10. 4 hits.
InterProIPR002155. 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]
PfamPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMSSF53901. SSF53901. 2 hits.
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

EvolutionaryTraceP27796.
NextBio977187.
PROP27796.

Entry information

Entry nameTHIK_YEAST
AccessionPrimary (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: June 11, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways