ID   ACYP_MYCTA              Reviewed;          93 AA.
AC   A5U6S8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-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=MRA_2948;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ74728.1; -; Genomic_DNA.
DR   RefSeq; WP_003414811.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U6S8; -.
DR   SMR; A5U6S8; -.
DR   STRING; 419947.MRA_2948; -.
DR   EnsemblBacteria; ABQ74728; ABQ74728; MRA_2948.
DR   GeneID; 45426910; -.
DR   KEGG; mra:MRA_2948; -.
DR   eggNOG; COG1254; Bacteria.
DR   HOGENOM; CLU_141932_3_0_11; -.
DR   OMA; FRWWTRA; -.
DR   OrthoDB; 2034659at2; -.
DR   Proteomes; UP000001988; 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   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..93
FT                   /note="Acylphosphatase"
FT                   /id="PRO_0000326754"
FT   DOMAIN          7..93
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   93 AA;  10206 MW;  63A90ED2D780DDEB CRC64;
     MSAPDVRLTA WVHGWVQGVG FRWWTRCRAL ELGLTGYAAN HADGRVLVVA QGPRAACQKL
     LQLLQGDTTP GRVAKVVADW SQSTEQITGF SER