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Protein

Medium-chain fatty acid ethyl ester synthase/esterase 2

Gene

EHT1

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

Displays enzymatic activity both for medium-chain fatty acid (MCFA) ethyl ester synthesis and hydrolysis (esterase activity). MCFA are toxic for yeast and this enzyme could thus be involved in their detoxification by esterification.1 Publication

Catalytic activityi

Acetyl-CoA + an alcohol = CoA + an acetyl ester.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei247 – 2471Charge relay systemBy similarity
Active sitei395 – 3951Charge relay systemBy similarity
Active sitei423 – 4231Charge relay systemBy similarity

GO - Molecular functioni

  • alcohol O-acetyltransferase activity Source: UniProtKB-EC
  • alcohol O-butanoyltransferase activity Source: SGD
  • short-chain carboxylesterase activity Source: SGD

GO - Biological processi

  • cellular lipid metabolic process Source: SGD
  • medium-chain fatty acid biosynthetic process Source: SGD
  • medium-chain fatty acid catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Hydrolase, Serine esterase, Transferase

Enzyme and pathway databases

BioCyciYEAST:YBR177C-MONOMER.

Protein family/group databases

ESTHERiyeast-MCFS2. abh_upf0017.

Names & Taxonomyi

Protein namesi
Recommended name:
Medium-chain fatty acid ethyl ester synthase/esterase 2
Alternative name(s):
Alcohol O-acetyltransferase (EC:2.3.1.84, EC:3.1.1.-)
Ethanol hexanoyl transferase 1
Gene namesi
Name:EHT1
Ordered Locus Names:YBR177C
ORF Names:YBR1239
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome II

Organism-specific databases

CYGDiYBR177c.
EuPathDBiFungiDB:YBR177C.
SGDiS000000381. EHT1.

Subcellular locationi

GO - Cellular componenti

  • lipid particle Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Medium-chain fatty acid ethyl ester synthase/esterase 2PRO_0000212454Add
BLAST

Proteomic databases

MaxQBiP38295.
PaxDbiP38295.
PeptideAtlasiP38295.

Interactioni

Protein-protein interaction databases

BioGridi32876. 62 interactions.
IntActiP38295. 23 interactions.
MINTiMINT-660335.

Structurei

3D structure databases

ProteinModelPortaliP38295.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0429.
GeneTreeiENSGT00530000062981.
HOGENOMiHOG000248589.
InParanoidiP38295.
KOiK07019.
OMAiGCCRTKI.
OrthoDBiEOG7X9GHP.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR012020. ABHD1/2/3.
IPR000952. UPF0017_hydro-like_CS.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF005211. Ab_hydro_YheT. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS01133. UPF0017. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38295-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEVSKWPAI NPFHWGYNGT VSHIVGENGS IKLHLKDNKE QVDFDEFANK
60 70 80 90 100
YVPTLKNGAQ FKLSPYLFTG ILQTLYLGAA DFSKKFPVFY GREIVKFSDG
110 120 130 140 150
GVCTADWLID SWKKDYEFDQ STTSFDKKKF DKDEKATHPE GWPRLQPRTR
160 170 180 190 200
YLKDNELEEL REVDLPLVVI LHGLAGGSHE PIIRSLAENL SRSGRFQVVV
210 220 230 240 250
LNTRGCARSK ITTRNLFTAY HTMDIREFLQ REKQRHPDRK LYAVGCSFGA
260 270 280 290 300
TMLANYLGEE GDKSPLSAAA TLCNPWDLLL SAIRMSQDWW SRTLFSKNIA
310 320 330 340 350
QFLTRTVQVN MGELGVPNGS LPDHPPTVKN PSFYMFTPEN LIKAKSFKST
360 370 380 390 400
REFDEVYTAP ALGFPNAMEY YKAASSINRV DTIRVPTLVI NSRDDPVVGP
410 420 430 440 450
DQPYSIVEKN PRILYCRTDL GGHLAYLDKD NNSWATKAIA EFFTKFDELV

V
Length:451
Mass (Da):51,255
Last modified:October 1, 1994 - v1
Checksum:i48D48ABF4CC97029
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36046 Genomic DNA. Translation: CAA85138.1.
BK006936 Genomic DNA. Translation: DAA07292.1.
PIRiS46048.
RefSeqiNP_009736.3. NM_001178525.3.

Genome annotation databases

EnsemblFungiiYBR177C; YBR177C; YBR177C.
GeneIDi852476.
KEGGisce:YBR177C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36046 Genomic DNA. Translation: CAA85138.1.
BK006936 Genomic DNA. Translation: DAA07292.1.
PIRiS46048.
RefSeqiNP_009736.3. NM_001178525.3.

3D structure databases

ProteinModelPortaliP38295.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32876. 62 interactions.
IntActiP38295. 23 interactions.
MINTiMINT-660335.

Protein family/group databases

ESTHERiyeast-MCFS2. abh_upf0017.

Proteomic databases

MaxQBiP38295.
PaxDbiP38295.
PeptideAtlasiP38295.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR177C; YBR177C; YBR177C.
GeneIDi852476.
KEGGisce:YBR177C.

Organism-specific databases

CYGDiYBR177c.
EuPathDBiFungiDB:YBR177C.
SGDiS000000381. EHT1.

Phylogenomic databases

eggNOGiCOG0429.
GeneTreeiENSGT00530000062981.
HOGENOMiHOG000248589.
InParanoidiP38295.
KOiK07019.
OMAiGCCRTKI.
OrthoDBiEOG7X9GHP.

Enzyme and pathway databases

BioCyciYEAST:YBR177C-MONOMER.

Miscellaneous databases

NextBioi971438.
PROiP38295.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR012020. ABHD1/2/3.
IPR000952. UPF0017_hydro-like_CS.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF005211. Ab_hydro_YheT. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS01133. UPF0017. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  4. "The Saccharomyces cerevisiae EHT1 and EEB1 genes encode novel enzymes with medium-chain fatty acid ethyl ester synthesis and hydrolysis capacity."
    Saerens S.M.G., Verstrepen K.J., Van Laere S.D., Voet A.R., Van Dijck P., Delvaux F.R., Thevelein J.M.
    J. Biol. Chem. 281:4446-4456(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMCFS2_YEAST
AccessioniPrimary (citable) accession number: P38295
Secondary accession number(s): D6VQH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 22, 2015
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2550 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

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 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.