ACH1_SCHPO
ID ACH1_SCHPO Reviewed; 521 AA.
AC Q9UUJ9; P78872;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=SPAC1952.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-521.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
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; CU329670; CAB52573.1; -; Genomic_DNA.
DR EMBL; D89222; BAA13883.1; -; mRNA.
DR PIR; T37937; T37937.
DR PIR; T43043; T43043.
DR RefSeq; NP_594811.1; NM_001020240.2.
DR AlphaFoldDB; Q9UUJ9; -.
DR SMR; Q9UUJ9; -.
DR BioGRID; 278973; 24.
DR STRING; 4896.SPAC1952.09c.1; -.
DR SwissPalm; Q9UUJ9; -.
DR MaxQB; Q9UUJ9; -.
DR PaxDb; Q9UUJ9; -.
DR PRIDE; Q9UUJ9; -.
DR EnsemblFungi; SPAC1952.09c.1; SPAC1952.09c.1:pep; SPAC1952.09c.
DR GeneID; 2542515; -.
DR KEGG; spo:SPAC1952.09c; -.
DR PomBase; SPAC1952.09c; -.
DR VEuPathDB; FungiDB:SPAC1952.09c; -.
DR eggNOG; KOG2828; Eukaryota.
DR HOGENOM; CLU_019748_3_0_1; -.
DR InParanoid; Q9UUJ9; -.
DR OMA; DEALSWH; -.
DR PhylomeDB; Q9UUJ9; -.
DR PRO; PR:Q9UUJ9; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; ISS:PomBase.
DR GO; GO:0006083; P:acetate metabolic process; ISS:PomBase.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; ISS:PomBase.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISM:PomBase.
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 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..521
FT /note="Acetyl-CoA hydrolase"
FT /id="PRO_0000215522"
FT ACT_SITE 301
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:B3EY95"
FT BINDING 276..280
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95"
FT BINDING 391
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95"
FT BINDING 395
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95"
FT CONFLICT 223
FT /note="Missing (in Ref. 2; BAA13883)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="N -> K (in Ref. 2; BAA13883)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="L -> P (in Ref. 2; BAA13883)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="W -> WCI (in Ref. 2; BAA13883)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 57916 MW; 6053AD3CA38C7195 CRC64;
MPSLLSSRIR NAEFAKKIVT DPAKLVPYFK NGDYVGWSGF TGVGYPKMIP NALARHVEEN
NLQGKLRFKL FVGASGGADT ECKWAELNMI ERRCPHQVGK PISKGINSGR IQFFDKHLSM
FPQDLLYGYY TRNRESNTID TAIIEATAIT EDGGIVPGAS VGASPELMQL AEKIIIEVNT
AIPSFEGLHD IVEIPNPPHR TPININRVDD RIGKPYIKVD PKKVIGIVEA DYGDITCANS
PQDETSQAIA GHLVDFFHHE VSVGRLPKNL HPLQSGIGNI ANAIIGGLAH SPFKDLEVWT
EVLQDTFLPL FDSEKLRFAT ATSTRFSPQG FEKFYSNYDY YKERILLRPQ VISNHPEIIR
RLGCIAMNTP VEADIYAHAN STNVLGSRML NGLGGSADFL RNAKLSIMHT PSVRPSKKDP
TGITCIVPMA THVDQTEHDL DILVTEQGLA DLRGLSPTER AREVIDKCAH PDYKPLLREY
FDIAENYCLA RGAGHEPHIL ANAFKMQLNL LEKGTMKIDH W
