Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peroxisomal acyl-coenzyme A thioester hydrolase 1

Gene

TES1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acyl-coenzyme A (acyl-CoA) thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Contributes to growth on fatty acids.1 Publication

Catalytic activityi

Palmitoyl-CoA + H2O = CoA + palmitate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei259 – 2591Charge relay systemBy similarity
Active sitei282 – 2821Charge relay systemBy similarity
Active sitei333 – 3331Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

  • acyl-CoA metabolic process Source: InterPro
  • fatty acid beta-oxidation Source: SGD
  • fatty acid oxidation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BioCyciMetaCyc:YJR019C-MONOMER.
YEAST:YJR019C-MONOMER.
BRENDAi3.1.2.2. 984.
3.1.2.20. 984.
ReactomeiR-SCE-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-SCE-2046106. alpha-linolenic acid (ALA) metabolism.
R-SCE-389887. Beta-oxidation of pristanoyl-CoA.
R-SCE-390247. Beta-oxidation of very long chain fatty acids.
R-SCE-75105. Fatty Acyl-CoA Biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal acyl-coenzyme A thioester hydrolase 1 (EC:3.1.2.21 Publication)
Alternative name(s):
Peroxisomal long-chain acyl-CoA thioesterase 1
Gene namesi
Name:TES1
Synonyms:PTE1
Ordered Locus Names:YJR019C
ORF Names:J1456
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR019C.
SGDiS000003780. TES1.

Subcellular locationi

GO - Cellular componenti

  • peroxisome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Peroxisomal acyl-coenzyme A thioester hydrolase 1PRO_0000202158Add
BLAST

Proteomic databases

MaxQBiP41903.
PeptideAtlasiP41903.

Expressioni

Inductioni

Up-regulated by oleic acid.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi33774. 31 interactions.
DIPiDIP-4480N.
IntActiP41903. 6 interactions.
MINTiMINT-473706.

Structurei

Secondary structure

1
349
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 193Combined sources
Beta strandi21 – 299Combined sources
Helixi42 – 5413Combined sources
Beta strandi62 – 709Combined sources
Beta strandi81 – 899Combined sources
Beta strandi91 – 10212Combined sources
Beta strandi105 – 11511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TBUX-ray2.20A/B/C/D1-118[»]
ProteinModelPortaliP41903.
SMRiP41903. Positions 8-336.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41903.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi347 – 3493Microbody targeting signalSequence analysis

Sequence similaritiesi

Belongs to the C/M/P thioester hydrolase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000004207.
HOGENOMiHOG000115762.
InParanoidiP41903.
KOiK01068.
OMAiNDWVLYS.
OrthoDBiEOG7CNZSX.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
InterProiIPR003703. Acyl_CoA_thio.
IPR025652. Acyl_CoA_thio_II_dom.
IPR029069. HotDog_dom.
[Graphical view]
PANTHERiPTHR11066. PTHR11066. 1 hit.
PfamiPF02551. Acyl_CoA_thio. 2 hits.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 2 hits.
TIGRFAMsiTIGR00189. tesB. 1 hit.

Sequencei

Sequence statusi: Complete.

P41903-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASKMAMSN LEKILELVPL SPTSFVTKYL PAAPVGSKGT FGGTLVSQSL
60 70 80 90 100
LASLHTVPLN FFPTSLHSYF IKGGDPRTKI TYHVQNLRNG RNFIHKQVSA
110 120 130 140 150
YQHDKLIFTS MILFAVQRSK EHDSLQHWET IPGLQGKQPD PHRYEEATSL
160 170 180 190 200
FQKEVLDPQK LSRYASLSDR FQDATSMSKY VDAFQYGVME YQFPKDMFYS
210 220 230 240 250
ARHTDELDYF VKVRPPITTV EHAGDESSLH KHHPYRIPKS ITPENDARYN
260 270 280 290 300
YVAFAYLSDS YLLLTIPYFH NLPLYCHSFS VSLDHTIYFH QLPHVNNWIY
310 320 330 340
LKISNPRSHW DKHLVQGKYF DTQSGRIMAS VSQEGYVVYG SERDIRAKF
Length:349
Mass (Da):40,260
Last modified:November 1, 1995 - v1
Checksum:iF1B5A51C9A46783E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85972 Genomic DNA. Translation: CAA59960.1.
X87611 Genomic DNA. Translation: CAA60943.1.
AF124265 Genomic DNA. Translation: AAD27617.1.
Z49519 Genomic DNA. Translation: CAA89543.1.
BK006943 Genomic DNA. Translation: DAA08810.1.
PIRiS52763.
RefSeqiNP_012553.3. NM_001181677.3.

Genome annotation databases

EnsemblFungiiYJR019C; YJR019C; YJR019C.
GeneIDi853477.
KEGGisce:YJR019C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85972 Genomic DNA. Translation: CAA59960.1.
X87611 Genomic DNA. Translation: CAA60943.1.
AF124265 Genomic DNA. Translation: AAD27617.1.
Z49519 Genomic DNA. Translation: CAA89543.1.
BK006943 Genomic DNA. Translation: DAA08810.1.
PIRiS52763.
RefSeqiNP_012553.3. NM_001181677.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TBUX-ray2.20A/B/C/D1-118[»]
ProteinModelPortaliP41903.
SMRiP41903. Positions 8-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33774. 31 interactions.
DIPiDIP-4480N.
IntActiP41903. 6 interactions.
MINTiMINT-473706.

Proteomic databases

MaxQBiP41903.
PeptideAtlasiP41903.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR019C; YJR019C; YJR019C.
GeneIDi853477.
KEGGisce:YJR019C.

Organism-specific databases

EuPathDBiFungiDB:YJR019C.
SGDiS000003780. TES1.

Phylogenomic databases

GeneTreeiENSGT00390000004207.
HOGENOMiHOG000115762.
InParanoidiP41903.
KOiK01068.
OMAiNDWVLYS.
OrthoDBiEOG7CNZSX.

Enzyme and pathway databases

BioCyciMetaCyc:YJR019C-MONOMER.
YEAST:YJR019C-MONOMER.
BRENDAi3.1.2.2. 984.
3.1.2.20. 984.
ReactomeiR-SCE-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-SCE-2046106. alpha-linolenic acid (ALA) metabolism.
R-SCE-389887. Beta-oxidation of pristanoyl-CoA.
R-SCE-390247. Beta-oxidation of very long chain fatty acids.
R-SCE-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

EvolutionaryTraceiP41903.
NextBioi974083.
PROiP41903.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
InterProiIPR003703. Acyl_CoA_thio.
IPR025652. Acyl_CoA_thio_II_dom.
IPR029069. HotDog_dom.
[Graphical view]
PANTHERiPTHR11066. PTHR11066. 1 hit.
PfamiPF02551. Acyl_CoA_thio. 2 hits.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 2 hits.
TIGRFAMsiTIGR00189. tesB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Hani J., Stumpf G., Domdey H.
    Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DH484.
  2. "Identification of peroxisomal acyl-CoA thioesterases in yeast and humans."
    Jones J.M., Nau K., Geraghty M.T., Erdmann R., Gould S.J.
    J. Biol. Chem. 274:9216-9223(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION.
  3. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.

Entry informationi

Entry nameiPTE1_YEAST
AccessioniPrimary (citable) accession number: P41903
Secondary accession number(s): D6VWJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 138 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.