ID A0A0G1Q6T7_9BACT Unreviewed; 89 AA.
AC A0A0G1Q6T7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
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=UX55_C0001G0017 {ECO:0000313|EMBL:KKU40704.1};
OS Candidatus Azambacteria bacterium GW2011_GWE2_46_45.
OC Bacteria; Candidatus Azambacteria.
OX NCBI_TaxID=1618625 {ECO:0000313|EMBL:KKU40704.1, ECO:0000313|Proteomes:UP000034202};
RN [1] {ECO:0000313|EMBL:KKU40704.1, ECO:0000313|Proteomes:UP000034202}
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};
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:KKU40704.1}.
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DR EMBL; LCMQ01000001; KKU40704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1Q6T7; -.
DR Proteomes; UP000034202; 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; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520}.
FT DOMAIN 4..89
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 89 AA; 10092 MW; 634405788A110969 CRC64;
MKKRITIIIY GLVQGVFFRV EAKEKAKLLG LVGWSGNEDG NVKIVAEGEE GALNQLLEWC
RKGPSGARID KVEVNWQEAT QEFERFRIV
//