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P38295 (MCFS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
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 names
Name:EHT1
Ordered Locus Names:YBR177C
ORF Names:YBR1239
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Catalytic activity

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

Miscellaneous

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

Sequence similarities

Belongs to the AB hydrolase superfamily. AB hydrolase 4 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Medium-chain fatty acid ethyl ester synthase/esterase 2
PRO_0000212454

Sites

Active site2471Charge relay system By similarity
Active site3951Charge relay system By similarity
Active site4231Charge relay system By similarity

Sequences

Sequence LengthMass (Da)Tools
P38295 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 48D48ABF4CC97029

FASTA45151,255
        10         20         30         40         50         60 
MSEVSKWPAI NPFHWGYNGT VSHIVGENGS IKLHLKDNKE QVDFDEFANK YVPTLKNGAQ 

        70         80         90        100        110        120 
FKLSPYLFTG ILQTLYLGAA DFSKKFPVFY GREIVKFSDG GVCTADWLID SWKKDYEFDQ 

       130        140        150        160        170        180 
STTSFDKKKF DKDEKATHPE GWPRLQPRTR YLKDNELEEL REVDLPLVVI LHGLAGGSHE 

       190        200        210        220        230        240 
PIIRSLAENL SRSGRFQVVV LNTRGCARSK ITTRNLFTAY HTMDIREFLQ REKQRHPDRK 

       250        260        270        280        290        300 
LYAVGCSFGA TMLANYLGEE GDKSPLSAAA TLCNPWDLLL SAIRMSQDWW SRTLFSKNIA 

       310        320        330        340        350        360 
QFLTRTVQVN MGELGVPNGS LPDHPPTVKN PSFYMFTPEN LIKAKSFKST REFDEVYTAP 

       370        380        390        400        410        420 
ALGFPNAMEY YKAASSINRV DTIRVPTLVI NSRDDPVVGP DQPYSIVEKN PRILYCRTDL 

       430        440        450 
GGHLAYLDKD NNSWATKAIA EFFTKFDELV V 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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.
[3]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z36046 Genomic DNA. Translation: CAA85138.1.
BK006936 Genomic DNA. Translation: DAA07292.1.
PIRS46048.
RefSeqNP_009736.3. NM_001178525.3.

3D structure databases

ProteinModelPortalP38295.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32876. 61 interactions.
IntActP38295. 23 interactions.
MINTMINT-660335.
STRING4932.YBR177C.

Proteomic databases

MaxQBP38295.
PaxDbP38295.
PeptideAtlasP38295.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR177C; YBR177C; YBR177C.
GeneID852476.
KEGGsce:YBR177C.

Organism-specific databases

CYGDYBR177c.
SGDS000000381. EHT1.

Phylogenomic databases

eggNOGCOG0429.
GeneTreeENSGT00530000062981.
HOGENOMHOG000248589.
KOK07019.
OMAGCCRTKI.
OrthoDBEOG7X9GHP.

Enzyme and pathway databases

BioCycYEAST:YBR177C-MONOMER.

Gene expression databases

GenevestigatorP38295.

Family and domain databases

Gene3D3.40.50.1820. 2 hits.
InterProIPR012020. AB-Hydro_YheT.
IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000952. UPF0017_hydro-like_CS.
[Graphical view]
PfamPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFPIRSF005211. Ab_hydro_YheT. 1 hit.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS01133. UPF0017. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971438.
PROP38295.

Entry information

Entry nameMCFS2_YEAST
AccessionPrimary (citable) accession number: P38295
Secondary accession number(s): D6VQH2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 9, 2014
This is version 118 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 II

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

Yeast

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

SIMILARITY comments

Index of protein domains and families