ACYP_THEKO
ID ACYP_THEKO Reviewed; 91 AA.
AC Q5JDG7;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Acylphosphatase;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphate phosphohydrolase;
GN Name=acyP; OrderedLocusNames=TK2031;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD86220.1; -; Genomic_DNA.
DR RefSeq; WP_011250981.1; NC_006624.1.
DR AlphaFoldDB; Q5JDG7; -.
DR SMR; Q5JDG7; -.
DR STRING; 69014.TK2031; -.
DR EnsemblBacteria; BAD86220; BAD86220; TK2031.
DR GeneID; 3235065; -.
DR KEGG; tko:TK2031; -.
DR PATRIC; fig|69014.16.peg.1985; -.
DR eggNOG; arCOG01674; Archaea.
DR HOGENOM; CLU_141932_3_2_2; -.
DR InParanoid; Q5JDG7; -.
DR OMA; VGFRWSM; -.
DR OrthoDB; 111329at2157; -.
DR PhylomeDB; Q5JDG7; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0003998; F:acylphosphatase activity; IBA:GO_Central.
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; PS00151; ACYLPHOSPHATASE_2; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..91
FT /note="Acylphosphatase"
FT /id="PRO_0000158561"
FT DOMAIN 5..91
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 91 AA; 10297 MW; 6C277AE5C4C43838 CRC64;
MKRVRAHLRI YGRVQGVGFR WSMSREARKL GVHGWVRNLP DGTVEAVIEG DPERVEALIG
WAHQGPPLAR VTRVEVKWEE PEGLEGFKVV G