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Protein

3-ketoacyl-CoA thiolase, peroxisomal

Gene

POT1

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

Functioni

Catalytic activityi

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

Pathwayi: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei125Acyl-thioester intermediate1
Active sitei375Proton acceptor1
Active sitei403Proton acceptor1

GO - Molecular functioni

  • acetyl-CoA C-acyltransferase activity Source: SGD
  • mRNA binding Source: SGD

GO - Biological processi

  • 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.
BRENDAi2.3.1.16. 984.
ReactomeiR-SCE-2046106. alpha-linolenic acid (ALA) metabolism.
R-SCE-390247. Beta-oxidation of very long chain fatty acids.
R-SCE-6798695. Neutrophil degranulation.
UniPathwayiUPA00199.

Chemistry databases

SwissLipidsiSLP:000001408.

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
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL160C.
SGDiS000001422. POT1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial intermembrane space Source: SGD
  • peroxisomal matrix Source: SGD
  • peroxisome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000034078? – 4173-ketoacyl-CoA thiolase, peroxisomal
Transit peptidei1 – ?Peroxisome

Proteomic databases

PRIDEiP27796.

2D gel databases

UCD-2DPAGEP27796.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi34832. 70 interactors.
DIPiDIP-1504N.
IntActiP27796. 3 interactors.
MINTiMINT-412295.

Structurei

Secondary structure

1417
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 15Combined sources15
Turni26 – 29Combined sources4
Beta strandi36 – 43Combined sources8
Turni49 – 51Combined sources3
Turni53 – 56Combined sources4
Helixi59 – 72Combined sources14
Helixi76 – 79Combined sources4
Helixi82 – 84Combined sources3
Beta strandi88 – 91Combined sources4
Beta strandi93 – 96Combined sources4
Helixi97 – 99Combined sources3
Helixi100 – 109Combined sources10
Beta strandi118 – 122Combined sources5
Helixi124 – 126Combined sources3
Helixi127 – 140Combined sources14
Beta strandi145 – 154Combined sources10
Helixi155 – 158Combined sources4
Helixi159 – 161Combined sources3
Helixi162 – 164Combined sources3
Helixi171 – 175Combined sources5
Helixi179 – 183Combined sources5
Helixi186 – 196Combined sources11
Helixi201 – 220Combined sources20
Turni225 – 227Combined sources3
Helixi251 – 255Combined sources5
Turni263 – 265Combined sources3
Turni270 – 272Combined sources3
Beta strandi276 – 287Combined sources12
Helixi288 – 293Combined sources6
Beta strandi300 – 309Combined sources10
Helixi312 – 317Combined sources6
Helixi318 – 330Combined sources13
Helixi334 – 336Combined sources3
Beta strandi338 – 342Combined sources5
Helixi347 – 357Combined sources11
Helixi361 – 363Combined sources3
Helixi370 – 373Combined sources4
Turni377 – 379Combined sources3
Helixi380 – 391Combined sources12
Beta strandi397 – 404Combined sources8
Turni405 – 407Combined sources3
Beta strandi408 – 416Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AFWX-ray1.80A/B25-417[»]
1AFYmodel-A/B25-417[»]
1PXTX-ray2.80A/B28-417[»]
3W15X-ray1.80C1-15[»]
ProteinModelPortaliP27796.
SMRiP27796.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27796.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00760000119318.
HOGENOMiHOG000012239.
InParanoidiP27796.
KOiK07513.
OMAiAPKGMFR.
OrthoDBiEOG092C2K2G.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
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

        10         20         30         40         50
MSQRLQSIKD HLVESAMGKG ESKRKNSLLE KRPEDVVIVA ANRSAIGKGF
60 70 80 90 100
KGAFKDVNTD YLLYNFLNEF IGRFPEPLRA DLNLIEEVAC GNVLNVGAGA
110 120 130 140 150
TEHRAACLAS GIPYSTPFVA LNRQCSSGLT AVNDIANKIK VGQIDIGLAL
160 170 180 190 200
GVESMTNNYK NVNPLGMISS EELQKNREAK KCLIPMGITN ENVAANFKIS
210 220 230 240 250
RKDQDEFAAN SYQKAYKAKN EGLFEDEILP IKLPDGSICQ SDEGPRPNVT
260 270 280 290 300
AESLSSIRPA FIKDRGTTTA GNASQVSDGV AGVLLARRSV ANQLNLPVLG
310 320 330 340 350
RYIDFQTVGV PPEIMGVGPA YAIPKVLEAT GLQVQDIDIF EINEAFAAQA
360 370 380 390 400
LYCIHKLGID LNKVNPRGGA IALGHPLGCT GARQVATILR ELKKDQIGVV
410
SMCIGTGMGA AAIFIKE
Length:417
Mass (Da):44,730
Last modified:August 1, 1992 - v1
Checksum:iB22AA06130829DE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AFWX-ray1.80A/B25-417[»]
1AFYmodel-A/B25-417[»]
1PXTX-ray2.80A/B28-417[»]
3W15X-ray1.80C1-15[»]
ProteinModelPortaliP27796.
SMRiP27796.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34832. 70 interactors.
DIPiDIP-1504N.
IntActiP27796. 3 interactors.
MINTiMINT-412295.

Chemistry databases

SwissLipidsiSLP:000001408.

2D gel databases

UCD-2DPAGEP27796.

Proteomic databases

PRIDEiP27796.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YIL160C.
SGDiS000001422. POT1.

Phylogenomic databases

GeneTreeiENSGT00760000119318.
HOGENOMiHOG000012239.
InParanoidiP27796.
KOiK07513.
OMAiAPKGMFR.
OrthoDBiEOG092C2K2G.

Enzyme and pathway databases

UniPathwayiUPA00199.
BioCyciMetaCyc:YIL160C-MONOMER.
YEAST:YIL160C-MONOMER.
BRENDAi2.3.1.16. 984.
ReactomeiR-SCE-2046106. alpha-linolenic acid (ALA) metabolism.
R-SCE-390247. Beta-oxidation of very long chain fatty acids.
R-SCE-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP27796.
PROiP27796.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 166 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.