ID   ACYP_POLNA              Reviewed;         101 AA.
AC   A1VW83;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Acylphosphatase;
DE            EC=3.6.1.7;
DE   AltName: Full=Acylphosphate phosphohydrolase;
GN   Name=acyP; OrderedLocusNames=Pnap_4846;
OS   Polaromonas naphthalenivorans (strain CJ2).
OG   Plasmid pPNAP03.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(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; CP000532; ABM39911.1; -; Genomic_DNA.
DR   RefSeq; WP_011798282.1; NC_008759.1.
DR   AlphaFoldDB; A1VW83; -.
DR   SMR; A1VW83; -.
DR   EnsemblBacteria; ABM39911; ABM39911; Pnap_4846.
DR   KEGG; pna:Pnap_4846; -.
DR   HOGENOM; CLU_141932_1_2_4; -.
DR   OMA; INFRSNT; -.
DR   OrthoDB; 2034659at2; -.
DR   Proteomes; UP000000644; Plasmid pPNAP03.
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   SUPFAM; SSF54975; SSF54975; 1.
DR   PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Plasmid; Reference proteome.
FT   CHAIN           1..101
FT                   /note="Acylphosphatase"
FT                   /id="PRO_0000326770"
FT   DOMAIN          11..99
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   101 AA;  11524 MW;  525B54B756557AAE CRC64;
     MQSDKDKTFD SWLVKAIGRV QGVGYRDACI RYARAQDITG WVRNRVDGSV ELMLQGSKEQ
     LADMCRWLRD GIPAAHVEKL EVSKVPPPSP RLNRFDRLPN L