ID   ACH1_CANGA              Reviewed;         526 AA.
AC   Q6FPF3;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, 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=CAGL0J04268g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380956; CAG60840.1; -; Genomic_DNA.
DR   RefSeq; XP_447891.1; XM_447891.1.
DR   AlphaFoldDB; Q6FPF3; -.
DR   SMR; Q6FPF3; -.
DR   STRING; 5478.XP_447891.1; -.
DR   EnsemblFungi; CAG60840; CAG60840; CAGL0J04268g.
DR   GeneID; 2889653; -.
DR   KEGG; cgr:CAGL0J04268g; -.
DR   CGD; CAL0133538; CAGL0J04268g.
DR   VEuPathDB; FungiDB:CAGL0J04268g; -.
DR   eggNOG; KOG2828; Eukaryota.
DR   HOGENOM; CLU_019748_3_0_1; -.
DR   InParanoid; Q6FPF3; -.
DR   OMA; DEALSWH; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IEA:EnsemblFungi.
DR   GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006083; P:acetate metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
DR   Gene3D; 3.40.1080.20; -; 1.
DR   InterPro; IPR026888; AcetylCoA_hyd_C.
DR   InterPro; IPR038460; AcetylCoA_hyd_C_sf.
DR   InterPro; IPR003702; ActCoA_hydro.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR   Pfam; PF02550; AcetylCoA_hydro; 1.
DR   SUPFAM; SSF100950; SSF100950; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..526
FT                   /note="Acetyl-CoA hydrolase"
FT                   /id="PRO_0000215518"
FT   ACT_SITE        302
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         277..281
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         392
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         396
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
SQ   SEQUENCE   526 AA;  58578 MW;  D36573740EBAD8FF CRC64;
     MTVSKLLKER VRYAPYLAKV KTPEELIPLF KNGQYLGWSG FTGVGTPKAV PDALIKHVED
     NNLQGKLRFN LFVGASAGPE ENKWAEHDMI IRRAPHQVGK PIAKAINNGK IQFFDKHLSM
     FPQDLTYGYY TRDRTDGKIL DYMIIEATAI KEDGSIVPGP SVGGSPEFIS VSDKVIIEVN
     TATPSFEGVH DIDMPVNPPH RVPYPYTKVD QKIGVDSIPV DPERVIAIVE SKTRDQVGPN
     TPSDDMSKAI AGNLIEFFRN EVKHGRLPEN LLPLQSGIGN IANAVIEGLT DANFKHLNVW
     TEVLQDSFLD LFENGSLDYA TATSIRLTEP GFERVFKNWD FYKSRLCLRS QVVSNNPELI
     RRLGVIAMNT PVEADIYAHA NSTNVNGSRM LNGLGGSADF LRNAKLSIMH CPAARPTKVD
     PTGISSIVPM VSHVDQTEHD LDVLVTDQGL ADLRGLSPRE RAREIINKCA HPDYKPLLQD
     YLDRAEHYAT KHGCLHEPHM LKNAFKFHTN LAEKGTMKVE SWDPVE