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Database: UniProt
Entry: V2X4P6_MONRO
LinkDB: V2X4P6_MONRO
Original site: V2X4P6_MONRO 
ID   V2X4P6_MONRO            Unreviewed;       543 AA.
AC   V2X4P6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   22-FEB-2023, entry version 34.
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=Moror_11650 {ECO:0000313|EMBL:ESK87430.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK87430.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK87430.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK87430.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
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:ESK87430.1}.
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DR   EMBL; AWSO01000785; ESK87430.1; -; Genomic_DNA.
DR   RefSeq; XP_007853275.1; XM_007855084.1.
DR   AlphaFoldDB; V2X4P6; -.
DR   STRING; 1381753.V2X4P6; -.
DR   KEGG; mrr:Moror_11650; -.
DR   HOGENOM; CLU_019748_3_0_1; -.
DR   OrthoDB; 100792at2759; -.
DR   Proteomes; UP000017559; 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; 3.40.1080.20; 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; PTHR43609; ACETYL-COA HYDROLASE; 1.
DR   PANTHER; PTHR43609:SF1; ACETYL-COA HYDROLASE; 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:ESK87430.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT   DOMAIN          25..250
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          351..501
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
SQ   SEQUENCE   543 AA;  60455 MW;  21F5B92FEA0EA6BB CRC64;
     MKATRTLRNA SIAGPSAALR ERVRRPQYFK KLAKPSNLAP LFKNDDYIGW SGFTGVGYPK
     GTPTAIADHI EANNLQANPE TKKRFNLFVG ASVGPEVEDR WARMDMIARR YPHQVGKDIA
     KGINTGKIEF ADKHLSMFPQ DLTYGYYSLQ KKHGDPKKPL DWAIVEATAI TEEGFIVPGA
     SIGATPEIVQ SAEKIIIEVN TRIPNLEGLH DINHSFIPPH RQPYLITHPS DRIGTTAIPI
     DTERVVAVVE SNQPDNTGEN APENEESRAI ARHLIEFLQS EVEAGRLPKN LLPLQSGIGN
     VANSIIGGLA GGPFEKVQVW TEVLQDTFIE FFDSGKLDFA TATSIRFSPG GFDHFYKNWE
     RYKDRLLLRS QQVANSPELI RRLGVIAMNT PLEVDIYGHA NSTNALGSRM LNGLGGSADF
     LRNAKLSIMH TPSSRPTKTD PTGISCIVPF SSHIDQTEHD LDVVVTEQGL ADLRGLSPRE
     RAPIIIKQCA HPDYRDMLLE YYDRALHECM KRGAGHEPHM LRNAFKLHTN FLEKGTMKIT
     SWD
//
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