ACH1_CANAL
ID ACH1_CANAL Reviewed; 524 AA.
AC P83773; A0A1D8PNC1; Q59YK9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 03-AUG-2022, entry version 90.
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=CAALFM_C502000CA;
GN ORFNames=CaO19.10681, CaO19.3171;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP PROTEIN SEQUENCE OF 82-91 AND 350-359, SUBCELLULAR LOCATION, AND
RP ANTIGENICITY.
RC STRAIN=SC5314 / ATCC MYA-2876; TISSUE=Protoplast;
RX PubMed=15378761; DOI=10.1002/pmic.200400903;
RA Pitarch A., Abian J., Carrascal M., Sanchez M., Nombela C., Gil C.;
RT "Proteomics-based identification of novel Candida albicans antigens for
RT diagnosis of systemic candidiasis in patients with underlying hematological
RT malignancies.";
RL Proteomics 4:3084-3106(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:0000269|PubMed:15378761}.
CC -!- MISCELLANEOUS: Has antigenic properties. Elicits a specific immune
CC response in systemic candidiasis human patients undergoing malignant
CC hematological disorders.
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC {ECO:0000305}.
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DR EMBL; CP017627; AOW29629.1; -; Genomic_DNA.
DR RefSeq; XP_714589.2; XM_709496.2.
DR AlphaFoldDB; P83773; -.
DR SMR; P83773; -.
DR BioGRID; 1226697; 1.
DR STRING; 237561.P83773; -.
DR COMPLUYEAST-2DPAGE; P83773; -.
DR PRIDE; P83773; -.
DR GeneID; 3643773; -.
DR KEGG; cal:CAALFM_C502000CA; -.
DR CGD; CAL0000189008; ACH1.
DR VEuPathDB; FungiDB:C5_02000C_A; -.
DR eggNOG; KOG2828; Eukaryota.
DR HOGENOM; CLU_019748_3_0_1; -.
DR InParanoid; P83773; -.
DR OMA; DEALSWH; -.
DR OrthoDB; 1016647at2759; -.
DR PRO; PR:P83773; -.
DR Proteomes; UP000000559; 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; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Reference proteome.
FT CHAIN 1..524
FT /note="Acetyl-CoA hydrolase"
FT /id="PRO_0000215517"
FT ACT_SITE 300
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:B3EY95"
FT BINDING 275..279
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95"
FT BINDING 390
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95"
FT BINDING 394
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95"
SQ SEQUENCE 524 AA; 58005 MW; 199E55926290CB7A CRC64;
MSAILKQRVR YAPYLKKLRT GEQCIDLFKH GQYLGWSGFT GVGAPKVIPT TLVDHVEKNN
LQGKLGFHLF VGASAGPEES RWAENNMILT RAPHQVGKPI AAAINDGRTQ FFDKHLSMFP
QDLTYGFYTK DKPNGSNLDY TIIEATAITE DGSIVPGPAV GASPEMISVS DKIIIEVNTK
TPSFEGIHDI DMPVNPPFRQ PYPHTSADFK IGKTAIPVDP EKVVAIVEST SGDKVPPNTP
SDEQSRGIAN HLIEFLEHEV KQGRLPANLH PLQSGIGNIA NAVVEGLASS NFKNLTVWTE
VLQDSFLDFF ESGSLDYATA TSIRLTNDGF KKFYDNWDTY SKKLCLRSQV VSNSPEIIRR
LGVIAMNTPV EVDIYGHANS TNVMGSRMLN GLGGSADFLR NAKLSIMHTP SARPSKVDPT
GLSCIVPMAS HVDQTEHDLD VVVTEQGLAD LRGLAPKARA KVIIDKCSHP DYKPQLQEYY
DRSVFYATKK KTLHEPHILR DVFKMHLNFQ ENGTMKLDSW DQKF
