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 27-MAR-2024, entry version 96.
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; Deinococcota; 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 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 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 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 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
//
