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Database: UniProt
Entry: X6MLE2_RETFI
LinkDB: X6MLE2_RETFI
Original site: X6MLE2_RETFI 
ID   X6MLE2_RETFI            Unreviewed;       396 AA.
AC   X6MLE2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
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};
DE   Flags: Fragment;
GN   ORFNames=RFI_23097 {ECO:0000313|EMBL:ETO14272.1};
OS   Reticulomyxa filosa.
OC   Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC   Reticulomyxidae; Reticulomyxa.
OX   NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO14272.1, ECO:0000313|Proteomes:UP000023152};
RN   [1] {ECO:0000313|EMBL:ETO14272.1, ECO:0000313|Proteomes:UP000023152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24332546;
RA   Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA   Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA   Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT   "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL   Curr. Biol. 0:0-0(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETO14272.1}.
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DR   EMBL; ASPP01020127; ETO14272.1; -; Genomic_DNA.
DR   AlphaFoldDB; X6MLE2; -.
DR   EnsemblProtists; ETO14272; ETO14272; RFI_23097.
DR   OMA; NPKMTAI; -.
DR   OrthoDB; 5486434at2759; -.
DR   Proteomes; UP000023152; Unassembled WGS sequence.
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; 2.
DR   Pfam; PF02550; AcetylCoA_hydro; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 3.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ETO14272.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023152}.
FT   DOMAIN          13..128
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          199..241
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   DOMAIN          274..386
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ETO14272.1"
SQ   SEQUENCE   396 AA;  43658 MW;  5DF4C0A6EEF2F435 CRC64;
     KKKKFSYFKK KKKKISPEYS AHFRDNSLFI GGNLRNAVNS GLADFTPIFL SEIPRLFQDP
     DYKLDVALLQ VSPPDKHGFC SLGTSVDCTR AAILAAKYVV GLVNKNVPRT HGDGQIHISH
     FQNVVHHDTS LPEIKAGGEV DEAADKIDSV LKNLTHHKDI GIHTEMCSDG MLHLVNSGVI
     SNSYKYQHRG KTVSSFCMGS KKLYDFINDN PSVLFFDCSY VNDVGVIRSN DRVHAINSCI
     EAGEGGPLQT SNFFLLILFL FVLFLNEKKG CLICQQVDIT GQVCADSIGT RMYSGVGGQM
     DFMRGASLSK EGKAIMAFSS TTGKGQSKIV PTLKQGSGVV TTRAHVQYVV TEYGFAKLYG
     KSLRERAKLL INLAHPDHRE SLEKAAVERF GKLDLD
//
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