ID A0A2A5R0Q7_9EURY Unreviewed; 92 AA.
AC A0A2A5R0Q7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=acylphosphatase {ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520};
GN ORFNames=CP557_08255 {ECO:0000313|EMBL:PCR92667.1};
OS Natrinema ejinorense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=373386 {ECO:0000313|EMBL:PCR92667.1, ECO:0000313|Proteomes:UP000219689};
RN [1] {ECO:0000313|EMBL:PCR92667.1, ECO:0000313|Proteomes:UP000219689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13890 {ECO:0000313|EMBL:PCR92667.1,
RC ECO:0000313|Proteomes:UP000219689};
RA Roh S.W., Kim Y.B., Kim J.Y.;
RT "Genome sequences of Natrinema ejinorence JCM 13890T.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:PCR92667.1}.
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DR EMBL; NXNI01000001; PCR92667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5R0Q7; -.
DR OrthoDB; 6643at2157; -.
DR Proteomes; UP000219689; 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; PS00151; ACYLPHOSPHATASE_2; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520}.
FT DOMAIN 6..92
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 21
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 92 AA; 10332 MW; 568DC2B415346F18 CRC64;
MSDRTRARVF VSGTVQGVYY RANTRDTAHE RGIDGWVRNL EDGRVEAVFE GPADAVESMV
EWCQTGSPAA NVEDVEAEYE EPQGEDGFEI RY
//
