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Database: UniProt
Entry: A0A1A1YSK2_9MYCO
LinkDB: A0A1A1YSK2_9MYCO
Original site: A0A1A1YSK2_9MYCO 
ID   A0A1A1YSK2_9MYCO        Unreviewed;        94 AA.
AC   A0A1A1YSK2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=A5724_17180 {ECO:0000313|EMBL:OBF34279.1};
OS   Mycobacterium sp. ACS1612.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF34279.1, ECO:0000313|Proteomes:UP000092025};
RN   [1] {ECO:0000313|Proteomes:UP000092025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA   Musoke P., Ssengooba W., Joloba M.;
RL   Submitted (JUN-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:OBF34279.1}.
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DR   EMBL; LZHZ01000032; OBF34279.1; -; Genomic_DNA.
DR   RefSeq; WP_067802338.1; NZ_LZHZ01000032.1.
DR   AlphaFoldDB; A0A1A1YSK2; -.
DR   STRING; 1834117.A5724_17180; -.
DR   OrthoDB; 3182027at2; -.
DR   Proteomes; UP000092025; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092025}.
FT   DOMAIN          8..94
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   ACT_SITE        23
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        41
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   94 AA;  10511 MW;  2B3FDA0CA262310F CRC64;
     MQELAEVRLT AWVHGYVQGV GFRWWTRSRA LELGLVGYAS NRPDGRVQVV AQGPREACER
     LLDLLQSGNT PGRVDKVIAD WSEPGDSLQG FTER
//
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