ID A0A1M3G373_9SPHI Unreviewed; 91 AA.
AC A0A1M3G373;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=BGO54_02210 {ECO:0000313|EMBL:OJW34332.1};
OS Sphingobacteriales bacterium 46-32.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895839 {ECO:0000313|EMBL:OJW34332.1, ECO:0000313|Proteomes:UP000184358};
RN [1] {ECO:0000313|EMBL:OJW34332.1, ECO:0000313|Proteomes:UP000184358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=46-32 {ECO:0000313|EMBL:OJW34332.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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|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:OJW34332.1}.
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DR EMBL; MKTY01000017; OJW34332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3G373; -.
DR STRING; 1895839.BGO54_02210; -.
DR Proteomes; UP000184358; 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 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; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520}.
FT DOMAIN 5..91
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT ACT_SITE 20
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 38
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 91 AA; 10293 MW; 168D9B139B1B7950 CRC64;
MVRKTIRIKV SGKVQGVFYR QSTLQKAKEL HLCGEVWNNT DGTVGIFATG DEDILLQLTD
WCSKGPSRAE VHSVEVTDQP LQEFPDFSVR R
//
