ID   ACH1_YARLI              Reviewed;         524 AA.
AC   Q6C3Z9;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=Acetyl-CoA hydrolase;
DE            EC=3.1.2.1;
DE   AltName: Full=Acetyl-CoA deacylase;
DE            Short=Acetyl-CoA acylase;
GN   Name=ACH1; OrderedLocusNames=YALI0E30965g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Presumably involved in regulating the intracellular acetyl-
CC       CoA pool for fatty acid and cholesterol synthesis and fatty acid
CC       oxidation. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=3.1.2.1;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC       {ECO:0000305}.
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DR   EMBL; CR382131; CAG80217.1; -; Genomic_DNA.
DR   RefSeq; XP_504613.1; XM_504613.1.
DR   AlphaFoldDB; Q6C3Z9; -.
DR   SMR; Q6C3Z9; -.
DR   STRING; 284591.Q6C3Z9; -.
DR   EnsemblFungi; CAG80217; CAG80217; YALI0_E30965g.
DR   GeneID; 2911920; -.
DR   KEGG; yli:YALI0E30965g; -.
DR   VEuPathDB; FungiDB:YALI0_E30965g; -.
DR   HOGENOM; CLU_019748_3_0_1; -.
DR   InParanoid; Q6C3Z9; -.
DR   OMA; DEALSWH; -.
DR   OrthoDB; 100792at2759; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IBA:GO_Central.
DR   GO; GO:0003986; F:acetyl-CoA hydrolase activity; IBA:GO_Central.
DR   GO; GO:0006083; P:acetate metabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.750.70; 4-hydroxybutyrate coenzyme like domains; 1.
DR   Gene3D; 3.40.1080.20; Acetyl-CoA hydrolase/transferase C-terminal domain; 1.
DR   Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 1.
DR   InterPro; IPR026888; AcetylCoA_hyd_C.
DR   InterPro; IPR038460; AcetylCoA_hyd_C_sf.
DR   InterPro; IPR046433; ActCoA_hydro.
DR   InterPro; IPR003702; ActCoA_hydro_N.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   PANTHER; PTHR43609; ACETYL-COA HYDROLASE; 1.
DR   PANTHER; PTHR43609:SF1; ACETYL-COA HYDROLASE; 1.
DR   Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR   Pfam; PF02550; AcetylCoA_hydro; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..524
FT                   /note="Acetyl-CoA hydrolase"
FT                   /id="PRO_0000215523"
FT   ACT_SITE        304
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         279..283
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         398
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
SQ   SEQUENCE   524 AA;  58051 MW;  EBF47FC1AE51C647 CRC64;
     MSAVLKQRIR YKPYLDKIRT AAQCVDLFGA KPNQYIGWSG FTGVGAPKVV PDAVSKHVEE
     NNLQGHENWR YNLFVGASAG MEIESRWANN NMIARRSPHQ VGKPIAAAIN EGRTDFFDKH
     LSMWAQDLTY GFYTRDKKEN SLDIAVIEAT AITEDGHLIP GPAVGASPEI VHMADKIIIE
     LNTKTPSFEG LHDINMPVLP PFRQPYQITD VSQKMGTPYI PLDPSKVVAI VESEFADVVG
     ANSPADEGSK AIAANLIELF QQEVKAGRLP ENLLPLQSGI GNIANAVVEG LADASFKDLN
     VWTEVLQDSF LDFFESGNLN FATATSIRLT EDGFKRFFDN WDEFSKKLLL RSQVVSNNPE
     IIRRLGVIAM NTPVEVDIYA HANSTCVNGS KMLHGLGGSG DFLRNAKLSI MHTPSARPSK
     TDPLGISCIV PFATHIDQTE HDLDIVVTEQ GLADLRGLSP KERSREMINK CAHPSYRDQL
     LAYVEQAEFE CAKSRSLHEP HVLKNAFKMH TNLAENGTMR LDKW
//