ID   ACYP_RHIWR              Reviewed;          99 AA.
AC   A5VFP2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   04-NOV-2026, entry version 88.
DE   RecName: Full=Acylphosphatase;
DE            EC=3.6.1.7;
DE   AltName: Full=Acylphosphate phosphohydrolase;
GN   Name=acyP; OrderedLocusNames=Swit_4771;
OS   Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC
OS   105917 / EY 4224 / RW1) (Sphingomonas wittichii).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Sphingomonadales; Rhizorhabdaceae; Rhizorhabdus.
OX   NCBI_TaxID=392499;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 /
RC   RW1;
RX   PubMed=20833805; DOI=10.1128/jb.01030-10;
RA   Miller T.R., Delcher A.L., Salzberg S.L., Saunders E., Detter J.C.,
RA   Halden R.U.;
RT   "Genome sequence of the dioxin-mineralizing bacterium Sphingomonas
RT   wittichii RW1.";
RL   J. Bacteriol. 192:6101-6102(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + H2O = a carboxylate + phosphate + H(+);
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; CP000699; ABQ71108.1; -; Genomic_DNA.
DR   SMR; A5VFP2; -.
DR   STRING; 392499.Swit_4771; -.
DR   PaxDb; 392499-Swit_4771; -.
DR   KEGG; swi:Swit_4771; -.
DR   eggNOG; COG1254; Bacteria.
DR   HOGENOM; CLU_141932_3_2_5; -.
DR   OMA; AACFKAW; -.
DR   OrthoDB; 5295388at2; -.
DR   Gene3D; 3.30.70.100; -; 1.
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; ACYLPHOSPHATASE; 1.
DR   PANTHER; PTHR47268:SF4; ACYLPHOSPHATASE; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   PRINTS; PR00112; ACYLPHPHTASE.
DR   SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR   NCBIfam; NF010996; PRK14421.1; 1.
DR   PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR   PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR   GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR   Proteomes; UP000001989; Chromosome.
DR   AlphaFoldDB; A5VFP2; -.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..99
FT                   /note="Acylphosphatase"
FT                   /id="PRO_0000326807"
FT   DOMAIN          11..97
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   99 AA;  10742 MW;  48DDEC25AD9D8406 CRC64;
     MSGADRPDRI ARRIHVKGKV QGVWFRAWTV EQAAELGLDG WVRNRADGSV EAVAAGPADR
     VEEMIARCRR GSPASRVDSI DVEDTPGVVA QGFTQKPTV
//