ID   ACH1_DEBHA              Reviewed;         523 AA.
AC   Q6BKW1;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 89.
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=DEHA2F18744g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC   2968;
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; CR382138; CAG89543.1; -; Genomic_DNA.
DR   RefSeq; XP_461160.1; XM_461160.1.
DR   AlphaFoldDB; Q6BKW1; -.
DR   SMR; Q6BKW1; -.
DR   STRING; 284592.Q6BKW1; -.
DR   GeneID; 2903722; -.
DR   KEGG; dha:DEHA2F18744g; -.
DR   VEuPathDB; FungiDB:DEHA2F18744g; -.
DR   eggNOG; KOG2828; Eukaryota.
DR   HOGENOM; CLU_019748_3_0_1; -.
DR   InParanoid; Q6BKW1; -.
DR   OMA; DEALSWH; -.
DR   OrthoDB; 100792at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR   GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006083; P:acetate metabolic process; IEA:InterPro.
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..523
FT                   /note="Acetyl-CoA hydrolase"
FT                   /id="PRO_0000215519"
FT   ACT_SITE        299
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         274..278
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         389
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         393
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
SQ   SEQUENCE   523 AA;  58294 MW;  9EED942E19750768 CRC64;
     MSSILKQRVR YAPYLQKLRT AEQCVELFKH GQYLGWSGFT GVGAPKVVPD AIADHVEKNN
     LQGKLGFNLF VGASAGPEEG RWAENDMLLR RSPHQVGKPI AKAINTGKTK FFDKHLSMFP
     QDLTYGFYTR EKENDLLDYT IIEATAITED GSIVPGPAVG ASPEMISVSD KIIIEVNTVT
     PSFEGLHDID MPVNPPFRQP YPHTTVDYRT GLTAIPVDPS KVVAIVESQT RDKVPPNTPS
     DETSRNIANN LLEFFEHEAK LGRLPENLHP LQSGIGNIAN AVVEGLADSK FKNLTVWTEV
     LQDSFLDFFE SGSLDFATAT SIRLTEAGFD KFYENWDTYS KKLCLRSQVV SNSPEIIRRL
     GTIAMNTPVE VDIYAHANST NVMGSRMLNG LGGSADFLRN SKLSVMHTPS ARPSKTDKTG
     VSCIVPFATH VDQTEHDLDI VVTDQGLADL RGLSPKERAR EIITKTSHPD YRDQLTDYLD
     RATFYAEKSK CLHEPHILQD AFKMHLNFQE NGTMKLDSWD KKF
//