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Database: UniProt
Entry: Q8PNV0
LinkDB: Q8PNV0
Original site: Q8PNV0 
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   01-OCT-2014, entry version 70.
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.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
CC   -!- CATALYTIC ACTIVITY: An acylphosphate + H(2)O = a carboxylate +
CC       phosphate.
CC   -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 acylphosphatase-like domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00520}.
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DR   EMBL; AE008923; AAM35827.1; -; Genomic_DNA.
DR   RefSeq; NP_641291.1; NC_003919.1.
DR   ProteinModelPortal; Q8PNV0; -.
DR   STRING; 190486.XAC0939; -.
DR   EnsemblBacteria; AAM35827; AAM35827; XAC0939.
DR   GeneID; 1155010; -.
DR   KEGG; xac:XAC0939; -.
DR   PATRIC; 24053822; VBIXanAxo33670_1009.
DR   eggNOG; NOG117913; -.
DR   HOGENOM; HOG000292686; -.
DR   KO; K01512; -.
DR   OMA; ALEAWLC; -.
DR   OrthoDB; EOG61P6Z6; -.
DR   BioCyc; XAXO190486:GH55-939-MONOMER; -.
DR   GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   SUPFAM; SSF54975; SSF54975; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase.
FT   CHAIN         1     85       Acylphosphatase.
FT                                /FTId=PRO_0000326845.
FT   DOMAIN        3     85       Acylphosphatase-like.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00520}.
FT   ACT_SITE     18     18       {ECO:0000255|PROSITE-ProRule:PRU00520}.
FT   ACT_SITE     36     36       {ECO:0000255|PROSITE-ProRule:PRU00520}.
SQ   SEQUENCE   85 AA;  9291 MW;  B9FC715EA55C6BB2 CRC64;
     MQAARFVVSG VVQGVYYRAC TRQRAVALGL VGHARNQADG SVDVVAAGSA AALDALEAWL
     CRARRPPRSR RSRARPARFR RLKTL
//
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