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Database: UniProt
Entry: U2ERA1_9GAMM
LinkDB: U2ERA1_9GAMM
Original site: U2ERA1_9GAMM 
ID   U2ERA1_9GAMM            Unreviewed;        91 AA.
AC   U2ERA1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Acylphosphatase {ECO:0000256|ARBA:ARBA00015991, 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:ERJ20532.1};
GN   ORFNames=SSPSH_000642 {ECO:0000313|EMBL:ERJ20532.1};
OS   Salinisphaera shabanensis E1L3A.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC   Salinisphaeraceae; Salinisphaera.
OX   NCBI_TaxID=1033802 {ECO:0000313|EMBL:ERJ20532.1, ECO:0000313|Proteomes:UP000006242};
RN   [1] {ECO:0000313|EMBL:ERJ20532.1, ECO:0000313|Proteomes:UP000006242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E1L3A {ECO:0000313|EMBL:ERJ20532.1,
RC   ECO:0000313|Proteomes:UP000006242};
RX   PubMed=21705588; DOI=10.1128/JB.05459-11;
RA   Antunes A., Alam I., Bajic V.B., Stingl U.;
RT   "Genome sequence of Salinisphaera shabanensis, a gammaproteobacterium from
RT   the harsh, variable environment of the brine-seawater interface of the
RT   Shaban Deep in the Red Sea.";
RL   J. Bacteriol. 193:4555-4556(2011).
RN   [2] {ECO:0000313|EMBL:ERJ20532.1, ECO:0000313|Proteomes:UP000006242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E1L3A {ECO:0000313|EMBL:ERJ20532.1,
RC   ECO:0000313|Proteomes:UP000006242};
RX   PubMed=24324765;
RA   Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA   Bajic V.B.;
RT   "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT   the Red Sea Extremophiles.";
RL   PLoS ONE 8:E82210-E82210(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|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:ERJ20532.1}.
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DR   EMBL; AFNV02000003; ERJ20532.1; -; Genomic_DNA.
DR   RefSeq; WP_006914067.1; NZ_AFNV02000003.1.
DR   AlphaFoldDB; U2ERA1; -.
DR   STRING; 1033802.SSPSH_000642; -.
DR   eggNOG; COG1254; Bacteria.
DR   OrthoDB; 5295388at2; -.
DR   Proteomes; UP000006242; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006242}.
FT   DOMAIN          4..91
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   91 AA;  9898 MW;  A9E149F4FFC1AF2B CRC64;
     MKNTRQFLVS GRVQGVGFRD ATRTRANELG LAGWVRNLSD GRVEVQAAGS GEKLNALADW
     LQDGPPSAKV EHVDTQYIES SDTAPEPFAV R
//
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