ID   ACH1_DICDI              Reviewed;         532 AA.
AC   Q54K91;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, 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; ORFNames=DDB_G0287519;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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; AAFI02000102; EAL63659.1; -; Genomic_DNA.
DR   RefSeq; XP_637164.1; XM_632072.1.
DR   AlphaFoldDB; Q54K91; -.
DR   SMR; Q54K91; -.
DR   STRING; 44689.DDB0233380; -.
DR   PaxDb; Q54K91; -.
DR   EnsemblProtists; EAL63659; EAL63659; DDB_G0287519.
DR   GeneID; 8626165; -.
DR   KEGG; ddi:DDB_G0287519; -.
DR   dictyBase; DDB_G0287519; -.
DR   eggNOG; KOG2828; Eukaryota.
DR   HOGENOM; CLU_019748_3_0_1; -.
DR   InParanoid; Q54K91; -.
DR   OMA; DEALSWH; -.
DR   PhylomeDB; Q54K91; -.
DR   PRO; PR:Q54K91; -.
DR   Proteomes; UP000002195; Chromosome 5.
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; ISS:dictyBase.
DR   GO; GO:0006083; P:acetate metabolic process; IBA:GO_Central.
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..532
FT                   /note="Acetyl-CoA hydrolase"
FT                   /id="PRO_0000330918"
FT   ACT_SITE        312
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         287..291
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         402
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         406
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
SQ   SEQUENCE   532 AA;  58894 MW;  BA70191A19871714 CRC64;
     MHKIVQQGSK SLIESRIKRK SLLSKVVTDV SQLIPYFQNG HYVSMGGFAG TGYPKVVPIA
     LADHVEKNGL QGKLKMNLFV GASVGPETED RWAMLDMIDK RYPHQNGHHI RNGINSGRIR
     FADQHLSTFA SDLLAGYYTL DKPHGSKRTM DIAIVEATEI TEDGCIVPGA SVGITPEILQ
     MADKIIIEIN TSLPSFKGLH DMVKIALPPF SKPYQITRVD DRIGLEAFPV DPEKIIAIVE
     SQLPDNTSVG APEDETSSAI ANNIVQFFIH EIEQGRFPKN LLPLQSGIGS IANAVIGGLS
     KGPFDNLSVW TEVIQDTFLD FFDNGKLKFA SATSLRFSPP GFNRLFNNWE NYKSKIILRN
     QAISNAAELI SRVGCIALNT PCEVDIYGHV NSTNTMGSKM LNGLGGSGEF LRNSRISIVH
     TPSTRPTKTD PHGISCIVPF ASHIDHTEHD IDIIVTEQGL ADIRGLAPYE RAKVIIQNCA
     HPIYKPILME YLETSRQICL KNHMGHEPHQ LDKAFKFYTN LSEKGTMKID KW