ID   ACYP_DECAR              Reviewed;          92 AA.
AC   Q47GU0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Acylphosphatase;
DE            EC=3.6.1.7;
DE   AltName: Full=Acylphosphate phosphohydrolase;
GN   Name=acyP; OrderedLocusNames=Daro_1185;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RX   PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA   Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA   Lapidus A.;
RT   "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT   indications of a surprisingly complex life-style and cryptic anaerobic
RT   pathways for aromatic degradation.";
RL   BMC Genomics 10:351-351(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC   -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR   EMBL; CP000089; AAZ45941.1; -; Genomic_DNA.
DR   RefSeq; WP_011286950.1; NC_007298.1.
DR   AlphaFoldDB; Q47GU0; -.
DR   SMR; Q47GU0; -.
DR   STRING; 159087.Daro_1185; -.
DR   EnsemblBacteria; AAZ45941; AAZ45941; Daro_1185.
DR   KEGG; dar:Daro_1185; -.
DR   eggNOG; COG1254; Bacteria.
DR   HOGENOM; CLU_141932_3_2_4; -.
DR   OMA; GTVEAMF; -.
DR   OrthoDB; 2034659at2; -.
DR   GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR020456; Acylphosphatase.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR017968; Acylphosphatase_CS.
DR   PANTHER; PTHR47268; PTHR47268; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   PRINTS; PR00112; ACYLPHPHTASE.
DR   SUPFAM; SSF54975; SSF54975; 1.
DR   PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..92
FT                   /note="Acylphosphatase"
FT                   /id="PRO_0000326695"
FT   DOMAIN          5..90
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        20
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   92 AA;  10175 MW;  5EC5F8FAAF7DD147 CRC64;
     MARIRRQLII EGRVQGVGYR WSMAEQARKL GVVGWVRNLA DGRVEAMAVG EEMAVLELIA
     WARRGPSHAI VRQVSVALGD GDFPSFEQRA NG