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Database: UniProt
Entry: U1PRX0_9EURY
LinkDB: U1PRX0_9EURY
Original site: U1PRX0_9EURY 
ID   U1PRX0_9EURY            Unreviewed;        92 AA.
AC   U1PRX0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=acylphosphatase {ECO:0000256|PROSITE-ProRule:PRU00520};
DE            EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520};
GN   ORFNames=J07HQW2_03002 {ECO:0000313|EMBL:ERG96522.1};
OS   Haloquadratum walsbyi J07HQW2.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=1238425 {ECO:0000313|EMBL:ERG96522.1, ECO:0000313|Proteomes:UP000030710};
RN   [1] {ECO:0000313|EMBL:ERG96522.1, ECO:0000313|Proteomes:UP000030710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J07HQW2 {ECO:0000313|Proteomes:UP000030710};
RX   PubMed=23637883;
RA   Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA   Allen E.E.;
RT   "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL   PLoS ONE 8:E61692-E61692(2013).
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|PROSITE-ProRule:PRU00520};
CC   -!- SIMILARITY: Belongs to the acylphosphatase family.
CC       {ECO:0000256|RuleBase:RU004168}.
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DR   EMBL; KE356561; ERG96522.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1PRX0; -.
DR   STRING; 1238425.J07HQW2_03002; -.
DR   eggNOG; arCOG01674; Archaea.
DR   HOGENOM; CLU_141932_3_2_2; -.
DR   Proteomes; UP000030710; 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   SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 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}.
FT   DOMAIN          7..92
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   92 AA;  10194 MW;  EE37DD6862AF2A41 CRC64;
     MSETRTRAHV FISGTVQGVY YRASTRDAAR ERGVKGWVRN LDDGRVEAVF EGAESAVDSL
     IEWCHTGSPN ANVSDVSVSY TDPEGIDDFR IR
//
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