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   25-MAY-2022, entry version 74.
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; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; 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 / RW1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Halden R.U., Miller T.R., Salzberg S.L., Eisen J.A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Sphingomonas wittichii RW1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000699; ABQ71108.1; -; Genomic_DNA.
DR   RefSeq; WP_012050944.1; NC_009511.1.
DR   AlphaFoldDB; A5VFP2; -.
DR   SMR; A5VFP2; -.
DR   STRING; 392499.Swit_4771; -.
DR   EnsemblBacteria; ABQ71108; ABQ71108; Swit_4771.
DR   KEGG; swi:Swit_4771; -.
DR   eggNOG; COG1254; Bacteria.
DR   HOGENOM; CLU_141932_3_2_5; -.
DR   OMA; VGFRWSM; -.
DR   OrthoDB; 2034659at2; -.
DR   Proteomes; UP000001989; Chromosome.
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; PS00150; ACYLPHOSPHATASE_1; 1.
DR   PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
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