ACYP_PYRIL
ID ACYP_PYRIL Reviewed; 95 AA.
AC A1RU25;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Acylphosphatase;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphate phosphohydrolase;
GN Name=acyP; OrderedLocusNames=Pisl_1294;
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) 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; CP000504; ABL88457.1; -; Genomic_DNA.
DR RefSeq; WP_011763032.1; NC_008701.1.
DR AlphaFoldDB; A1RU25; -.
DR SMR; A1RU25; -.
DR STRING; 384616.Pisl_1294; -.
DR PRIDE; A1RU25; -.
DR EnsemblBacteria; ABL88457; ABL88457; Pisl_1294.
DR GeneID; 4618270; -.
DR KEGG; pis:Pisl_1294; -.
DR eggNOG; arCOG01674; Archaea.
DR HOGENOM; CLU_141932_3_2_2; -.
DR OMA; VGFRWSM; -.
DR OrthoDB; 111329at2157; -.
DR Proteomes; UP000002595; 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 InterPro; IPR017968; Acylphosphatase_CS.
DR PANTHER; PTHR47268; PTHR47268; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR PRINTS; PR00112; ACYLPHPHTASE.
DR SUPFAM; SSF54975; SSF54975; 1.
DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..95
FT /note="Acylphosphatase"
FT /id="PRO_0000326868"
FT DOMAIN 5..93
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 95 AA; 10934 MW; 212AA90E482F2837 CRC64;
MENVRAHLYI KGKVQGVFFR QSMKEIAVRY GVRGWVRNRS DGRTVEAVLE GPRDAVAKVI
EWAKVGPPGA RVEEVEVDWE EYKGEFQDFR ILPTV
