ACYP_BURP1
ID ACYP_BURP1 Reviewed; 98 AA.
AC Q3JJ17;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Acylphosphatase;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphate phosphohydrolase;
GN Name=acyP; OrderedLocusNames=BURPS1710b_A1279;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA52674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000125; ABA52674.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_004187760.1; NC_007435.1.
DR AlphaFoldDB; Q3JJ17; -.
DR SMR; Q3JJ17; -.
DR EnsemblBacteria; ABA52674; ABA52674; BURPS1710b_A1279.
DR GeneID; 56598334; -.
DR KEGG; bpm:BURPS1710b_A1279; -.
DR HOGENOM; CLU_1746217_0_0_4; -.
DR OrthoDB; 2034659at2; -.
DR Proteomes; UP000002700; Chromosome II.
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..98
FT /note="Acylphosphatase"
FT /id="PRO_0000326673"
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; 11254 MW; D5B03E686EBC2B79 CRC64;
MSGDDLDERI ETYYVRVRGV VQGVGFRHAT VREAHALKLR GWVANLDDGS VEAMLQGSAP
QIDRMLAWLR HGPPAAHVTE VTFEEHRTDK RFERFQQH