ID A0A1J5H8V5_9BACT Unreviewed; 91 AA.
AC A0A1J5H8V5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 17.
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=AUK45_02695 {ECO:0000313|EMBL:OIP80892.1};
OS Candidatus Peregrinibacteria bacterium CG2_30_44_17.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1805324 {ECO:0000313|EMBL:OIP80892.1, ECO:0000313|Proteomes:UP000183123};
RN [1] {ECO:0000313|EMBL:OIP80892.1, ECO:0000313|Proteomes:UP000183123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_44_17 {ECO:0000313|EMBL:OIP80892.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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}.
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:OIP80892.1}.
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DR EMBL; MNZJ01000025; OIP80892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5H8V5; -.
DR STRING; 1805324.AUK45_02695; -.
DR Proteomes; UP000183123; 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 3..90
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 91 AA; 10415 MW; 7CC2599C985B87D9 CRC64;
MPAYKLKIHG KVQGVFYRDF ARKQAEALDI SGWAKNDSDG TVTAYIQGEE DKIDYFLVLL
WSGPEASKVQ NIQKEPSVED PMITLFEIRY D
//
