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Database: UniProt
Entry: A0A1Y3TA25_9FIRM
LinkDB: A0A1Y3TA25_9FIRM
Original site: A0A1Y3TA25_9FIRM 
ID   A0A1Y3TA25_9FIRM        Unreviewed;        90 AA.
AC   A0A1Y3TA25;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=B5G27_12230 {ECO:0000313|EMBL:OUN33401.1};
OS   Lachnoclostridium sp. An76.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1965654 {ECO:0000313|EMBL:OUN33401.1, ECO:0000313|Proteomes:UP000199802};
RN   [1] {ECO:0000313|Proteomes:UP000199802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000199802};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUN33401.1}.
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DR   EMBL; NFHL01000007; OUN33401.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3TA25; -.
DR   OrthoDB; 9808093at2; -.
DR   Proteomes; UP000199802; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199802}.
FT   DOMAIN          5..90
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   90 AA;  10345 MW;  9C31E82357CA8691 CRC64;
     MSEVRKHIVF YGRVQGVGFR YTAKYLTRSL GLTGWVRNDP DGTVTMEVQG REALINKLLV
     GLNGGHFISI EWMDTKEIPL EEEREFVVKM
//
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