ID   ACYP_THET8              Reviewed;          88 AA.
AC   Q5SKS6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Acylphosphatase;
DE            EC=3.6.1.7;
DE   AltName: Full=Acylphosphate phosphohydrolase;
GN   Name=acyP; OrderedLocusNames=TTHA0567;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) 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   -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR   EMBL; AP008226; BAD70390.1; -; Genomic_DNA.
DR   RefSeq; WP_008631905.1; NC_006461.1.
DR   RefSeq; YP_143833.1; NC_006461.1.
DR   PDB; 1ULR; X-ray; 1.30 A; A=1-88.
DR   PDBsum; 1ULR; -.
DR   AlphaFoldDB; Q5SKS6; -.
DR   SMR; Q5SKS6; -.
DR   STRING; 300852.55771949; -.
DR   EnsemblBacteria; BAD70390; BAD70390; BAD70390.
DR   GeneID; 3170007; -.
DR   KEGG; ttj:TTHA0567; -.
DR   PATRIC; fig|300852.9.peg.566; -.
DR   eggNOG; COG1254; Bacteria.
DR   HOGENOM; CLU_141932_2_1_0; -.
DR   OMA; VGFRWSM; -.
DR   PhylomeDB; Q5SKS6; -.
DR   BRENDA; 3.6.1.7; 2305.
DR   EvolutionaryTrace; Q5SKS6; -.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR020456; Acylphosphatase.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   PANTHER; PTHR47268; PTHR47268; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   SUPFAM; SSF54975; SSF54975; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Reference proteome.
FT   CHAIN           1..88
FT                   /note="Acylphosphatase"
FT                   /id="PRO_0000326836"
FT   DOMAIN          3..88
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   STRAND          3..11
FT                   /evidence="ECO:0007829|PDB:1ULR"
FT   STRAND          13..16
FT                   /evidence="ECO:0007829|PDB:1ULR"
FT   HELIX           17..27
FT                   /evidence="ECO:0007829|PDB:1ULR"
FT   STRAND          31..36
FT                   /evidence="ECO:0007829|PDB:1ULR"
FT   STRAND          42..48
FT                   /evidence="ECO:0007829|PDB:1ULR"
FT   HELIX           50..62
FT                   /evidence="ECO:0007829|PDB:1ULR"
FT   STRAND          68..77
FT                   /evidence="ECO:0007829|PDB:1ULR"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:1ULR"
SQ   SEQUENCE   88 AA;  9679 MW;  DFBD2365517774C7 CRC64;
     MPRLVALVKG RVQGVGYRAF AQKKALELGL SGYAENLPDG RVEVVAEGPK EALELFLHHL
     KQGPRLARVE AVEVQWGEEA GLKGFHVY