ID A0A1M5P5Y8_9ACTN Unreviewed; 91 AA.
AC A0A1M5P5Y8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ORFNames=SAMN05444351_3809 {ECO:0000313|EMBL:SHG97241.1};
OS Geodermatophilus nigrescens.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1070870 {ECO:0000313|EMBL:SHG97241.1, ECO:0000313|Proteomes:UP000184471};
RN [1] {ECO:0000313|EMBL:SHG97241.1, ECO:0000313|Proteomes:UP000184471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45408 {ECO:0000313|EMBL:SHG97241.1,
RC ECO:0000313|Proteomes:UP000184471};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQVX01000003; SHG97241.1; -; Genomic_DNA.
DR RefSeq; WP_073422023.1; NZ_FQVX01000003.1.
DR AlphaFoldDB; A0A1M5P5Y8; -.
DR STRING; 1070870.SAMN05444351_3809; -.
DR Proteomes; UP000184471; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184471}.
FT DOMAIN 6..91
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 91 AA; 9261 MW; A9B5CF18656971DF CRC64;
MSPDVRVRVL VSGTVQGVGY RWFVRGLADA AGLAGSARNL PDGRVEVELE GPADDVRAVV
AALDGPRAPG SVTGVVSEDR AVQGGQGFTT A
//
