ID   A0A136L7P1_9BACT        Unreviewed;        90 AA.
AC   A0A136L7P1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-JUN-2023, entry version 22.
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   Name=acyP {ECO:0000313|EMBL:KXK17659.1};
GN   ORFNames=UZ18_ATM001001033 {ECO:0000313|EMBL:KXK17659.1};
OS   Armatimonadetes bacterium OLB18.
OC   Bacteria; Armatimonadota.
OX   NCBI_TaxID=1617424 {ECO:0000313|EMBL:KXK17659.1, ECO:0000313|Proteomes:UP000070351};
RN   [1] {ECO:0000313|EMBL:KXK17659.1, ECO:0000313|Proteomes:UP000070351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB18 {ECO:0000313|EMBL:KXK17659.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Improved understanding of the partial-nitritation anammox process through
RT   23 genomes representing the majority of the microbial community.";
RL   Submitted (MAR-2015) 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:KXK17659.1}.
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DR   EMBL; JZQX01000112; KXK17659.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136L7P1; -.
DR   STRING; 1617424.UZ18_ATM001001033; -.
DR   Proteomes; UP000070351; 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   ECO:0000313|EMBL:KXK17659.1}.
FT   DOMAIN          3..88
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   REGION          70..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   90 AA;  9837 MW;  BD2C82BD9C239991 CRC64;
     MTGYRIVVRG QVQGVGFRAF VYREATYVGL RGRVWNRSDG GVEIVAYAEG PSTLDSFVVR
     LQQGPGRIDS VEVDSHVGEP PSNFDIGPTH
//