ID B8PZW7_9BACT Unreviewed; 93 AA.
AC B8PZW7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 22-FEB-2023, entry version 31.
DE RecName: Full=acylphosphatase {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|PROSITE-ProRule:PRU00520};
GN Name=acyP {ECO:0000313|EMBL:ACA34425.1};
OS uncultured bacterium pTW3.
OC Bacteria; Candidatus Dojkabacteria; environmental samples.
OX NCBI_TaxID=504467 {ECO:0000313|EMBL:ACA34425.1};
RN [1] {ECO:0000313|EMBL:ACA34425.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19218412; DOI=10.1128/AEM.02136-08;
RA Waschkowitz T., Rockstroh S., Daniel R.;
RT "Isolation and characterization of metalloproteases with a novel domain
RT structure by construction and screening of metagenomic libraries.";
RL Appl. Environ. Microbiol. 75:2506-2516(2009).
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 Evidence={ECO:0000256|ARBA:ARBA00000744, ECO:0000256|PROSITE-
CC ProRule:PRU00520};
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000256|ARBA:ARBA00005614, ECO:0000256|RuleBase:RU004168}.
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DR EMBL; EU333169; ACA34425.1; -; Genomic_DNA.
DR AlphaFoldDB; B8PZW7; -.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.70.100; -; 1.
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; ACYLPHOSPHATASE; 1.
DR PANTHER; PTHR47268:SF4; ACYLPHOSPHATASE; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520}.
FT DOMAIN 7..93
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 22
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 40
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 93 AA; 9859 MW; 36049C4D1043E88F CRC64;
MPAMDRSARF LISGKVQGVC FRASTRDEAL RLGLRGHARN LPDGRVEVLA TGNAAALDAL
AQWLQHGPPL ARVDAVEHHE TDGGGAMRGF SVG
//
