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P27796

- THIK_YEAST

UniProt

P27796 - THIK_YEAST

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Protein

3-ketoacyl-CoA thiolase, peroxisomal

Gene
POT1, FOX3, POX3, YIL160C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei125 – 1251Acyl-thioester intermediate
Active sitei375 – 3751Proton acceptor
Active sitei403 – 4031Proton acceptor

GO - Molecular functioni

  1. acetyl-CoA C-acyltransferase activity Source: SGD
  2. mRNA binding Source: SGD
  3. protein binding Source: IntAct

GO - Biological processi

  1. fatty acid beta-oxidation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:YIL160C-MONOMER.
YEAST:YIL160C-MONOMER.
ReactomeiREACT_188947. alpha-linolenic acid (ALA) metabolism.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
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 namesi
Name:POT1
Synonyms:FOX3, POX3
Ordered Locus Names:YIL160C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IX

Organism-specific databases

CYGDiYIL160c.
SGDiS000001422. POT1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial intermembrane space Source: SGD
  2. peroxisomal matrix Source: SGD
  3. peroxisome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 4173-ketoacyl-CoA thiolase, peroxisomalPRO_0000034078
Transit peptidei1 – ?Peroxisome

Proteomic databases

PaxDbiP27796.
PeptideAtlasiP27796.

2D gel databases

UCD-2DPAGEP27796.

Expressioni

Gene expression databases

GenevestigatoriP27796.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
PEX7P391083EBI-19236,EBI-13183

Protein-protein interaction databases

BioGridi34832. 69 interactions.
DIPiDIP-1504N.
IntActiP27796. 3 interactions.
MINTiMINT-412295.
STRINGi4932.YIL160C.

Structurei

Secondary structure

417
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1515
Turni26 – 294
Beta strandi36 – 438
Turni49 – 513
Turni53 – 564
Helixi59 – 7214
Helixi76 – 794
Helixi82 – 843
Beta strandi88 – 914
Beta strandi93 – 964
Helixi97 – 993
Helixi100 – 10910
Beta strandi118 – 1225
Helixi124 – 1263
Helixi127 – 14014
Beta strandi145 – 15410
Helixi155 – 1584
Helixi159 – 1613
Helixi162 – 1643
Helixi171 – 1755
Helixi179 – 1835
Helixi186 – 19611
Helixi201 – 22020
Turni225 – 2273
Helixi251 – 2555
Turni270 – 2723
Beta strandi276 – 28712
Helixi288 – 2936
Beta strandi300 – 30910
Helixi312 – 3176
Helixi318 – 33013
Helixi334 – 3363
Beta strandi338 – 3425
Helixi347 – 35711
Helixi361 – 3633
Helixi370 – 3734
Turni377 – 3793
Helixi380 – 39112
Beta strandi397 – 4048
Turni405 – 4073
Beta strandi408 – 4169

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AFWX-ray1.80A/B25-417[»]
1AFYmodel-A/B25-417[»]
1PXTX-ray2.80A/B28-417[»]
3W15X-ray1.80C1-15[»]
ProteinModelPortaliP27796.
SMRiP27796. Positions 25-417.

Miscellaneous databases

EvolutionaryTraceiP27796.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00750000117749.
HOGENOMiHOG000012239.
KOiK00632.
OMAiLYGVESM.
OrthoDBiEOG7PCJSX.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. 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]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27796-1 [UniParc]FASTAAdd to Basket

« Hide

MSQRLQSIKD HLVESAMGKG ESKRKNSLLE KRPEDVVIVA ANRSAIGKGF    50
KGAFKDVNTD YLLYNFLNEF IGRFPEPLRA DLNLIEEVAC GNVLNVGAGA 100
TEHRAACLAS GIPYSTPFVA LNRQCSSGLT AVNDIANKIK VGQIDIGLAL 150
GVESMTNNYK NVNPLGMISS EELQKNREAK KCLIPMGITN ENVAANFKIS 200
RKDQDEFAAN SYQKAYKAKN EGLFEDEILP IKLPDGSICQ SDEGPRPNVT 250
AESLSSIRPA FIKDRGTTTA GNASQVSDGV AGVLLARRSV ANQLNLPVLG 300
RYIDFQTVGV PPEIMGVGPA YAIPKVLEAT GLQVQDIDIF EINEAFAAQA 350
LYCIHKLGID LNKVNPRGGA IALGHPLGCT GARQVATILR ELKKDQIGVV 400
SMCIGTGMGA AAIFIKE 417
Length:417
Mass (Da):44,730
Last modified:August 1, 1992 - v1
Checksum:iB22AA06130829DE5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS22784.
RefSeqiNP_012106.1. NM_001179508.1.

Genome annotation databases

EnsemblFungiiYIL160C; YIL160C; YIL160C.
GeneIDi854646.
KEGGisce:YIL160C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S22784.
RefSeqi NP_012106.1. NM_001179508.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
3W15 X-ray 1.80 C 1-15 [» ]
ProteinModelPortali P27796.
SMRi P27796. Positions 25-417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34832. 69 interactions.
DIPi DIP-1504N.
IntActi P27796. 3 interactions.
MINTi MINT-412295.
STRINGi 4932.YIL160C.

2D gel databases

UCD-2DPAGE P27796.

Proteomic databases

PaxDbi P27796.
PeptideAtlasi P27796.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YIL160C ; YIL160C ; YIL160C .
GeneIDi 854646.
KEGGi sce:YIL160C.

Organism-specific databases

CYGDi YIL160c.
SGDi S000001422. POT1.

Phylogenomic databases

eggNOGi COG0183.
GeneTreei ENSGT00750000117749.
HOGENOMi HOG000012239.
KOi K00632.
OMAi LYGVESM.
OrthoDBi EOG7PCJSX.

Enzyme and pathway databases

UniPathwayi UPA00199 .
BioCyci MetaCyc:YIL160C-MONOMER.
YEAST:YIL160C-MONOMER.
Reactomei REACT_188947. alpha-linolenic acid (ALA) metabolism.

Miscellaneous databases

EvolutionaryTracei P27796.
NextBioi 977187.
PROi P27796.

Gene expression databases

Genevestigatori P27796.

Family and domain databases

Gene3Di 3.40.47.10. 4 hits.
InterProi 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 ]
Pfami PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMi SSF53901. SSF53901. 2 hits.
TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEi PS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. 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).

Entry informationi

Entry nameiTHIK_YEAST
AccessioniPrimary (citable) accession number: P27796
Secondary accession number(s): D6VVC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: September 3, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

External Data

Dasty 3

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