ACYP_BURVG
ID ACYP_BURVG Reviewed; 98 AA.
AC A4JK94;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Acylphosphatase;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphate phosphohydrolase;
GN Name=acyP; OrderedLocusNames=Bcep1808_3712;
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000615; ABO56697.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JK94; -.
DR SMR; A4JK94; -.
DR STRING; 269482.Bcep1808_3712; -.
DR EnsemblBacteria; ABO56697; ABO56697; Bcep1808_3712.
DR KEGG; bvi:Bcep1808_3712; -.
DR eggNOG; COG1254; Bacteria.
DR HOGENOM; CLU_141932_1_2_4; -.
DR OMA; VGFRWSM; -.
DR Proteomes; UP000002287; Chromosome 2.
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; Reference proteome.
FT CHAIN 1..98
FT /note="Acylphosphatase"
FT /id="PRO_0000326677"
FT DOMAIN 12..98
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 98 AA; 11400 MW; C3ED2F5B8F9EACC9 CRC64;
MSRNELDERI ETYYVRVRGV VQGVGFRHAT VREAHALKLR GWVANLEDGS VEAMIQGPGA
QIDRMLAWLR HGPPAARVTE VTFEERHVER RFERFQQQ