ID   ACH1_EREGS              Reviewed;         523 AA.
AC   Q754Q2;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 3.
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=AFR020W;
OS   Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Ashbya gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 437.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53391.2; -; Genomic_DNA.
DR   RefSeq; NP_985567.2; NM_210921.2.
DR   AlphaFoldDB; Q754Q2; -.
DR   SMR; Q754Q2; -.
DR   STRING; 284811.Q754Q2; -.
DR   EnsemblFungi; AAS53391; AAS53391; AGOS_AFR020W.
DR   GeneID; 4621806; -.
DR   KEGG; ago:AGOS_AFR020W; -.
DR   eggNOG; KOG2828; Eukaryota.
DR   HOGENOM; CLU_019748_3_0_1; -.
DR   InParanoid; Q754Q2; -.
DR   OMA; DEALSWH; -.
DR   OrthoDB; 100792at2759; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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..523
FT                   /note="Acetyl-CoA hydrolase"
FT                   /id="PRO_0000215516"
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   523 AA;  57808 MW;  A768E4F08028CADA CRC64;
     MTVSQLLKQR VRYAPYLSKV RRAEELLPLF KHGQYIGWSG FTGVGAPKVI PTALADHVEK
     NGLQGQLAFN LFVGASAGPE ENRWADLDMI LRRAPHQVGK PIARAINDGR IKFFDKHLSM
     FPQDLTYGYY TRERTDGKIL DYAIVEATAI KEDGSIVLGP SVGGSPEFMS AADKLIVEVN
     TATPSFEGLH DIDMPVLPPH RVPYPYTRVD ERSGLDAVPV DPARVVALVE STERDKVGPN
     TPSDEGSRAI AGHLVEFFEN EVRHGRLPAN LLPLQSGIGN IANAVIEGLA GASFRNLTVW
     TEVLQDSFLD LFENGSLEFA TATSIRLTEA GFEKFFANWD EYSSKLCLRS QVVSNSPEMI
     RRLGVIAMNT PVEVDIYAHA NSTNVSGSRM LNGLGGSADF LRNAKLSIMH APSARPSKTD
     PTGISTIVPM ASHVDQTEHD LDVLVTDQGL ADLRGLCPRE RAREIIRQCA HPDYKPILTD
     YLDRAEHYAQ RSRSMHEPHI LQQALRFHTH LAEKGTMKVP SWD
//