ID   ACYP_GEOSL              Reviewed;          91 AA.
AC   Q74ES0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   04-NOV-2026, entry version 103.
DE   RecName: Full=Acylphosphatase;
DE            EC=3.6.1.7;
DE   AltName: Full=Acylphosphate phosphohydrolase;
GN   Name=acyP; OrderedLocusNames=GSU0889;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfuromonadia;
OC   Geobacterales; Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR34219.1; -; Genomic_DNA.
DR   RefSeq; WP_010941553.1; NC_002939.5.
DR   AlphaFoldDB; Q74ES0; -.
DR   SMR; Q74ES0; -.
DR   FunCoup; Q74ES0; 301.
DR   STRING; 243231.GSU0889; -.
DR   EnsemblBacteria; AAR34219; AAR34219; GSU0889.
DR   KEGG; gsu:GSU0889; -.
DR   PATRIC; fig|243231.5.peg.887; -.
DR   eggNOG; COG1254; Bacteria.
DR   HOGENOM; CLU_141932_1_0_7; -.
DR   InParanoid; Q74ES0; -.
DR   OMA; AACFKAW; -.
DR   OrthoDB; 5295388at2; -.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0003998; F:acylphosphatase activity; IBA:GO_Central.
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   NCBIfam; NF011011; PRK14438.1; 1.
DR   PANTHER; PTHR10029; ACYLPHOSPHATASE; 1.
DR   PANTHER; PTHR10029:SF3; ACYLPHOSPHATASE-RELATED; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   PRINTS; PR00112; ACYLPHPHTASE.
DR   SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 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..91
FT                   /note="Acylphosphatase"
FT                   /id="PRO_0000326716"
FT   DOMAIN          4..91
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   91 AA;  10289 MW;  4121E9D5E263F876 CRC64;
     MKIRAIVTIK GLVQGVAFRH HTVQQAQRLG VSGWVKNLAG GDVQGCFEGE EEAVDALVAW
     CHHGPSRARV DRVILEREHY RGEFDDFDVR Y
//