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Database: UniProt
Entry: A0A0G1WXT4_9BACT
LinkDB: A0A0G1WXT4_9BACT
Original site: A0A0G1WXT4_9BACT 
ID   A0A0G1WXT4_9BACT        Unreviewed;        90 AA.
AC   A0A0G1WXT4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   03-MAY-2023, entry version 27.
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   ORFNames=UY22_C0001G0057 {ECO:0000313|EMBL:KKU95113.1};
OS   Candidatus Amesbacteria bacterium GW2011_GWC1_48_10.
OC   Bacteria; Candidatus Amesbacteria.
OX   NCBI_TaxID=1618365 {ECO:0000313|EMBL:KKU95113.1, ECO:0000313|Proteomes:UP000034877};
RN   [1] {ECO:0000313|EMBL:KKU95113.1, ECO:0000313|Proteomes:UP000034877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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, ECO:0000256|RuleBase:RU000553};
CC   -!- SIMILARITY: Belongs to the acylphosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005614, ECO:0000256|RuleBase:RU004168}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKU95113.1}.
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DR   EMBL; LCPE01000001; KKU95113.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1WXT4; -.
DR   PATRIC; fig|1618365.3.peg.64; -.
DR   Proteomes; UP000034877; Unassembled WGS sequence.
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   PRINTS; PR00112; ACYLPHPHTASE.
DR   SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 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 {ECO:0000256|PROSITE-ProRule:PRU00520,
KW   ECO:0000256|RuleBase:RU000553}.
FT   DOMAIN          4..90
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        37
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   90 AA;  10009 MW;  F512EB88442BA2A3 CRC64;
     MTPHLDITIS GFVQGVSFRY YAAAKAKNLK LTGYVQNQPD GTVYIEAEGD PKALQDFIAW
     CRQGPRFAQV GKVQSSPGPA KNYSRFEIRL
//
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