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Protein

Acetyl-CoA hydrolase

Gene

ACH1

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

Presumably involved in regulating the intracellular acetyl-CoA pool for fatty acid and cholesterol synthesis and fatty acid oxidation. It may be involved in overall regulation of acetylation during melatonin synthesis.

Catalytic activityi

Acetyl-CoA + H2O = CoA + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei302 – 30215-glutamyl coenzyme A thioester intermediateBy similarity
Binding sitei392 – 3921Coenzyme ABy similarity
Binding sitei396 – 3961Coenzyme A; via amide nitrogenBy similarity

GO - Molecular functioni

  1. acetate CoA-transferase activity Source: SGD
  2. acetyl-CoA hydrolase activity Source: SGD

GO - Biological processi

  1. acetate metabolic process Source: SGD
  2. acetyl-CoA metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17664.
YEAST:YBL015W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA hydrolase (EC:3.1.2.1)
Alternative name(s):
Acetyl-CoA deacylase
Short name:
Acetyl-CoA acylase
Gene namesi
Name:ACH1
Ordered Locus Names:YBL015W
ORF Names:YBL03.18, YBL0304
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome II

Organism-specific databases

CYGDiYBL015w.
EuPathDBiFungiDB:YBL015W.
SGDiS000000111. ACH1.

Subcellular locationi

  1. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: SGD
  2. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 526526Acetyl-CoA hydrolasePRO_0000215524Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Blocked amino end (Thr)
Modified residuei350 – 3501Phosphoserine1 Publication

Post-translational modificationi

Glycosylated; contains mannose.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP32316.
PaxDbiP32316.
PeptideAtlasiP32316.

Expressioni

Gene expression databases

GenevestigatoriP32316.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi32683. 93 interactions.
DIPiDIP-6548N.
IntActiP32316. 1 interaction.
MINTiMINT-681658.
STRINGi4932.YBL015W.

Structurei

3D structure databases

ProteinModelPortaliP32316.
SMRiP32316. Positions 8-517.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni277 – 2815Coenzyme A bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0427.
GeneTreeiENSGT00390000011259.
HOGENOMiHOG000172597.
InParanoidiP32316.
KOiK01067.
OMAiPHQVGKP.
OrthoDBiEOG7TQV8M.

Family and domain databases

InterProiIPR026888. AcetylCoA_hyd_C.
IPR003702. ActCoA_hydro.
[Graphical view]
PfamiPF13336. AcetylCoA_hyd_C. 1 hit.
PF02550. AcetylCoA_hydro. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32316-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTISNLLKQR VRYAPYLKKV KEAHELIPLF KNGQYLGWSG FTGVGTPKAV
60 70 80 90 100
PEALIDHVEK NNLQGKLRFN LFVGASAGPE ENRWAEHDMI IKRAPHQVGK
110 120 130 140 150
PIAKAINQGR IEFFDKHLSM FPQDLTYGFY TRERKDNKIL DYTIIEATAI
160 170 180 190 200
KEDGSIVPGP SVGGSPEFIT VSDKVIIEVN TATPSFEGIH DIDMPVNPPF
210 220 230 240 250
RKPYPYLKVD DKCGVDSIPV DPEKVVAIVE STMRDQVPPN TPSDDMSRAI
260 270 280 290 300
AGHLVEFFRN EVKHGRLPEN LLPLQSGIGN IANAVIEGLA GAQFKHLTVW
310 320 330 340 350
TEVLQDSFLD LFENGSLDYA TATSVRLTEK GFDRAFANWE NFKHRLCLRS
360 370 380 390 400
QVVSNNPEMI RRLGVIAMNT PVEVDIYAHA NSTNVNGSRM LNGLGGSADF
410 420 430 440 450
LRNAKLSIMH APSARPTKVD PTGISTIVPM ASHVDQTEHD LDILVTDQGL
460 470 480 490 500
ADLRGLSPKE RAREIINKCA HPDYQALLTD YLDRAEHYAK KHNCLHEPHM
510 520
LKNAFKFHTN LAEKGTMKVD SWEPVD
Length:526
Mass (Da):58,712
Last modified:January 4, 2005 - v2
Checksum:i7133A291F18AA1E4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti308 – 3081F → L in AAA34388 (PubMed:1970569).Curated
Sequence conflicti320 – 3201A → S in AAA34388 (PubMed:1970569).Curated
Sequence conflicti363 – 3642LG → FP in AAA34388 (PubMed:1970569).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31036 mRNA. Translation: AAA34388.1.
X68577 Genomic DNA. Translation: CAA48570.1.
Z35776 Genomic DNA. Translation: CAA84834.1.
BK006936 Genomic DNA. Translation: DAA07105.1.
PIRiS28549.
RefSeqiNP_009538.1. NM_001178255.1.

Genome annotation databases

EnsemblFungiiYBL015W; YBL015W; YBL015W.
GeneIDi852266.
KEGGisce:YBL015W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31036 mRNA. Translation: AAA34388.1.
X68577 Genomic DNA. Translation: CAA48570.1.
Z35776 Genomic DNA. Translation: CAA84834.1.
BK006936 Genomic DNA. Translation: DAA07105.1.
PIRiS28549.
RefSeqiNP_009538.1. NM_001178255.1.

3D structure databases

ProteinModelPortaliP32316.
SMRiP32316. Positions 8-517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32683. 93 interactions.
DIPiDIP-6548N.
IntActiP32316. 1 interaction.
MINTiMINT-681658.
STRINGi4932.YBL015W.

Proteomic databases

MaxQBiP32316.
PaxDbiP32316.
PeptideAtlasiP32316.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL015W; YBL015W; YBL015W.
GeneIDi852266.
KEGGisce:YBL015W.

Organism-specific databases

CYGDiYBL015w.
EuPathDBiFungiDB:YBL015W.
SGDiS000000111. ACH1.

Phylogenomic databases

eggNOGiCOG0427.
GeneTreeiENSGT00390000011259.
HOGENOMiHOG000172597.
InParanoidiP32316.
KOiK01067.
OMAiPHQVGKP.
OrthoDBiEOG7TQV8M.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17664.
YEAST:YBL015W-MONOMER.

Miscellaneous databases

NextBioi970868.
PROiP32316.

Gene expression databases

GenevestigatoriP32316.

Family and domain databases

InterProiIPR026888. AcetylCoA_hyd_C.
IPR003702. ActCoA_hydro.
[Graphical view]
PfamiPF13336. AcetylCoA_hyd_C. 1 hit.
PF02550. AcetylCoA_hydro. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A glucose-repressible gene encodes acetyl-CoA hydrolase from Saccharomyces cerevisiae."
    Lee F.-J.S., Lin L.-W., Smith J.A.
    J. Biol. Chem. 265:7413-7418(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, BLOCKED N-TERMINUS.
  2. "An 11.4 kb DNA segment on the left arm of yeast chromosome II carries the carboxypeptidase Y sorting gene PEP1, as well as ACH1, FUS3 and a putative ARS."
    van Dyck L., Purnelle B., Skala J., Goffeau A.
    Yeast 8:769-776(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC 204508 / S288c.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
    Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
    Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 174-181, SUBCELLULAR LOCATION.
    Strain: ATCC 201238 / W303-1B.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
    Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
    Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACH1_YEAST
AccessioniPrimary (citable) accession number: P32316
Secondary accession number(s): D6VPY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 4, 2005
Last modified: April 29, 2015
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4890 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.