ID   ACYP_RHIL3              Reviewed;          94 AA.
AC   Q1MFT8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Acylphosphatase;
DE            EC=3.6.1.7;
DE   AltName: Full=Acylphosphate phosphohydrolase;
GN   Name=acyP; OrderedLocusNames=RL2696;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
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; AM236080; CAK08185.1; -; Genomic_DNA.
DR   RefSeq; WP_011652233.1; NC_008380.1.
DR   AlphaFoldDB; Q1MFT8; -.
DR   SMR; Q1MFT8; -.
DR   STRING; 216596.RL2696; -.
DR   EnsemblBacteria; CAK08185; CAK08185; RL2696.
DR   KEGG; rle:RL2696; -.
DR   eggNOG; COG1254; Bacteria.
DR   HOGENOM; CLU_141932_3_2_5; -.
DR   OMA; VGFRWSM; -.
DR   OrthoDB; 2034659at2; -.
DR   Proteomes; UP000006575; 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.
FT   CHAIN           1..94
FT                   /note="Acylphosphatase"
FT                   /id="PRO_0000326780"
FT   DOMAIN          7..94
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   REGION          68..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   94 AA;  10410 MW;  5BD316C94F9CAF7D CRC64;
     MFDHDKAVRV RISGKVQGVG FRYWTRDEAV RLGLTGWVRN EEDGAVVAVI AGPDSAISTM
     IERFRRGPSG ASVSSVETEA TQLEKNPTDF RITR