ID   ACYP_YERPS              Reviewed;          92 AA.
AC   Q66CD9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Acylphosphatase {ECO:0000255|HAMAP-Rule:MF_01450};
DE            EC=3.6.1.7 {ECO:0000255|HAMAP-Rule:MF_01450};
DE   AltName: Full=Acylphosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01450};
GN   Name=acyP; OrderedLocusNames=YPTB1464;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01450};
CC   -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01450}.
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DR   EMBL; BX936398; CAH20704.1; -; Genomic_DNA.
DR   RefSeq; WP_002213049.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66CD9; -.
DR   SMR; Q66CD9; -.
DR   EnsemblBacteria; CAH20704; CAH20704; YPTB1464.
DR   GeneID; 66842101; -.
DR   KEGG; ypo:BZ17_1054; -.
DR   KEGG; yps:YPTB1464; -.
DR   PATRIC; fig|273123.14.peg.1119; -.
DR   OMA; VGFRWSM; -.
DR   Proteomes; UP000001011; Chromosome.
DR   GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01450; Acylphosphatase_entero; 1.
DR   InterPro; IPR020456; Acylphosphatase.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR028627; Acylphosphatase_bac.
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.
FT   CHAIN           1..92
FT                   /note="Acylphosphatase"
FT                   /id="PRO_0000326853"
FT   DOMAIN          5..92
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT   ACT_SITE        20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01450"
SQ   SEQUENCE   92 AA;  10292 MW;  5F2FAA18A0FE97C0 CRC64;
     MSKIYIVAYV YGVVQGVGFR YSTQRQAQQL GVTGYAKNCD DGSVEVVASG NPQAVERLME
     WIRQGGPRGA RVDRLLTEPY PPTPFETFSI RY