ACH1_YEAST
ID ACH1_YEAST Reviewed; 526 AA.
AC P32316; D6VPY5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 172.
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=YBL015W; ORFNames=YBL03.18, YBL0304;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT
RP THR-2.
RX PubMed=1970569; DOI=10.1016/s0021-9258(19)39129-x;
RA Lee F.-J.S., Lin L.-W., Smith J.A.;
RT "A glucose-repressible gene encodes acetyl-CoA hydrolase from Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 265:7413-7418(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1441754; DOI=10.1002/yea.320080910;
RA van Dyck L., Purnelle B., Skala J., Goffeau A.;
RT "An 11.4 kb DNA segment on the left arm of yeast chromosome II carries the
RT carboxypeptidase Y sorting gene PEP1, as well as ACH1, FUS3 and a putative
RT ARS.";
RL Yeast 8:769-776(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PROTEIN SEQUENCE OF 174-181, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 201238 / W303-1B;
RX PubMed=11502169; DOI=10.1021/bi010277r;
RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
RA Schmitter J.-M.;
RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT complex.";
RL Biochemistry 40:9758-9769(2001).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Presumably involved in regulating the intracellular acetyl-
CC CoA pool for fatty acid and cholesterol synthesis and fatty acid
CC oxidation. It may be involved in overall regulation of acetylation
CC during melatonin synthesis.
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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11502169}.
CC -!- PTM: Glycosylated; contains mannose.
CC -!- MISCELLANEOUS: Present with 4890 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC {ECO:0000305}.
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DR EMBL; M31036; AAA34388.1; -; mRNA.
DR EMBL; X68577; CAA48570.1; -; Genomic_DNA.
DR EMBL; Z35776; CAA84834.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07105.1; -; Genomic_DNA.
DR PIR; S28549; S28549.
DR RefSeq; NP_009538.1; NM_001178255.1.
DR AlphaFoldDB; P32316; -.
DR SMR; P32316; -.
DR BioGRID; 32683; 148.
DR DIP; DIP-6548N; -.
DR IntAct; P32316; 5.
DR STRING; 4932.YBL015W; -.
DR iPTMnet; P32316; -.
DR MaxQB; P32316; -.
DR PaxDb; P32316; -.
DR PRIDE; P32316; -.
DR EnsemblFungi; YBL015W_mRNA; YBL015W; YBL015W.
DR GeneID; 852266; -.
DR KEGG; sce:YBL015W; -.
DR SGD; S000000111; ACH1.
DR VEuPathDB; FungiDB:YBL015W; -.
DR eggNOG; KOG2828; Eukaryota.
DR GeneTree; ENSGT00390000011259; -.
DR HOGENOM; CLU_019748_3_0_1; -.
DR InParanoid; P32316; -.
DR OMA; DEALSWH; -.
DR BioCyc; MetaCyc:YBL015W-MON; -.
DR BioCyc; YEAST:YBL015W-MON; -.
DR PRO; PR:P32316; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32316; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IDA:SGD.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IDA:SGD.
DR GO; GO:0006083; P:acetate metabolic process; IMP:SGD.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000303|PubMed:1970569"
FT CHAIN 2..526
FT /note="Acetyl-CoA hydrolase"
FT /id="PRO_0000215524"
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"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000303|PubMed:1970569"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT CONFLICT 308
FT /note="F -> L (in Ref. 1; AAA34388)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="A -> S (in Ref. 1; AAA34388)"
FT /evidence="ECO:0000305"
FT CONFLICT 363..364
FT /note="LG -> FP (in Ref. 1; AAA34388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 58712 MW; 7133A291F18AA1E4 CRC64;
MTISNLLKQR VRYAPYLKKV KEAHELIPLF KNGQYLGWSG FTGVGTPKAV PEALIDHVEK
NNLQGKLRFN LFVGASAGPE ENRWAEHDMI IKRAPHQVGK PIAKAINQGR IEFFDKHLSM
FPQDLTYGFY TRERKDNKIL DYTIIEATAI KEDGSIVPGP SVGGSPEFIT VSDKVIIEVN
TATPSFEGIH DIDMPVNPPF RKPYPYLKVD DKCGVDSIPV DPEKVVAIVE STMRDQVPPN
TPSDDMSRAI AGHLVEFFRN EVKHGRLPEN LLPLQSGIGN IANAVIEGLA GAQFKHLTVW
TEVLQDSFLD LFENGSLDYA TATSVRLTEK GFDRAFANWE NFKHRLCLRS QVVSNNPEMI
RRLGVIAMNT PVEVDIYAHA NSTNVNGSRM LNGLGGSADF LRNAKLSIMH APSARPTKVD
PTGISTIVPM ASHVDQTEHD LDILVTDQGL ADLRGLSPKE RAREIINKCA HPDYQALLTD
YLDRAEHYAK KHNCLHEPHM LKNAFKFHTN LAEKGTMKVD SWEPVD
