ID A0A068YM40_ECHMU Unreviewed; 506 AA.
AC A0A068YM40;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Acetyl-CoA hydrolase {ECO:0000256|ARBA:ARBA00017958};
DE EC=3.1.2.1 {ECO:0000256|ARBA:ARBA00011920};
DE AltName: Full=Acetyl-CoA deacylase {ECO:0000256|ARBA:ARBA00029672};
GN ORFNames=EmuJ_001087900 {ECO:0000313|EMBL:CDS43149.1};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS43149.1};
RN [1] {ECO:0000313|EMBL:CDS43149.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CDS43149.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001831};
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC {ECO:0000256|ARBA:ARBA00009632}.
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DR EMBL; LN902844; CDS43149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068YM40; -.
DR STRING; 6211.A0A068YM40; -.
DR eggNOG; KOG2828; Eukaryota.
DR OMA; MTHIVEV; -.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006083; P:acetate metabolic process; IEA:InterPro.
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; PTHR21432:SF20; ACETYL-COA HYDROLASE; 1.
DR PANTHER; PTHR21432; ACETYL-COA HYDROLASE-RELATED; 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 Hydrolase {ECO:0000313|EMBL:CDS43149.1};
KW Transferase {ECO:0000313|EMBL:CDS43149.1}.
FT DOMAIN 38..210
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 305..459
FT /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13336"
SQ SEQUENCE 506 AA; 54937 MW; 7AFCADB9F3B868F8 CRC64;
MRTAILSSRF SPLLSRFLSV RSLHDLRMPT CAIANKAPKQ VDSAAELFQH LQSGQNVFVQ
GGAMTPTILV KHLCQYAIEK DLTDIKTVHI HTEGEFPVND ESVKHRFRST SLFTGGNCRK
AIASGQGDYV PIFLHEIPKL FRKGIIPLRY ALINVSPPDH HGFCSIGCSV DVTRSALEAA
EIIVAQINPH VPLCKGDAEI HISNIDYTID GPMPLYELAS KPSSPQEKKI AELIASELVA
DEATLQTGIG SIPDSVLALL TNHKNLGVHT ELFSDGLVDL FKSGAVTNAK KRLFPGKIVS
SFIIGTKKSF DFANANNGID LLDIAWTNDP SNIAQNPRPT AINSCIEIDI TGQIVSDSIG
SRIYSGFGGQ VDFLRGAAIA TDGLGVPIIA LASTTKKGQS KIVPYLQKGA GVVTTRAHAH
YVVTEHGIAF LFGKSLRQRA YELIRIADPA HREQLEKDAF EILKVMPSRQ FVFAAAAFVY
CSSISDIAVS HAHLFCYSFL PIIATL
//
