ID   ACYP_XANAC              Reviewed;          85 AA.
AC   Q8PNV0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Acylphosphatase;
DE            EC=3.6.1.7;
DE   AltName: Full=Acylphosphate phosphohydrolase;
GN   Name=acyP; OrderedLocusNames=XAC0939;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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; AE008923; AAM35827.1; -; Genomic_DNA.
DR   RefSeq; WP_011050631.1; NC_003919.1.
DR   AlphaFoldDB; Q8PNV0; -.
DR   SMR; Q8PNV0; -.
DR   STRING; 190486.XAC0939; -.
DR   EnsemblBacteria; AAM35827; AAM35827; XAC0939.
DR   GeneID; 66910125; -.
DR   KEGG; xac:XAC0939; -.
DR   eggNOG; COG1254; Bacteria.
DR   HOGENOM; CLU_141932_1_3_6; -.
DR   Proteomes; UP000000576; 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   PANTHER; PTHR47268; PTHR47268; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   SUPFAM; SSF54975; SSF54975; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..85
FT                   /note="Acylphosphatase"
FT                   /id="PRO_0000326845"
FT   DOMAIN          3..85
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   REGION          66..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   85 AA;  9291 MW;  B9FC715EA55C6BB2 CRC64;
     MQAARFVVSG VVQGVYYRAC TRQRAVALGL VGHARNQADG SVDVVAAGSA AALDALEAWL
     CRARRPPRSR RSRARPARFR RLKTL