ACYP_THEVO
ID ACYP_THEVO Reviewed; 90 AA.
AC Q97CT1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Acylphosphatase;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphate phosphohydrolase;
GN Name=acyP; OrderedLocusNames=TV0020; ORFNames=TVG0019502;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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; BA000011; BAB59162.1; -; Genomic_DNA.
DR RefSeq; WP_010916277.1; NC_002689.2.
DR AlphaFoldDB; Q97CT1; -.
DR SMR; Q97CT1; -.
DR STRING; 273116.14324234; -.
DR EnsemblBacteria; BAB59162; BAB59162; BAB59162.
DR GeneID; 1441506; -.
DR KEGG; tvo:TVG0019502; -.
DR eggNOG; arCOG01674; Archaea.
DR HOGENOM; CLU_141932_1_0_2; -.
DR OMA; INFRSNT; -.
DR OrthoDB; 111329at2157; -.
DR PhylomeDB; Q97CT1; -.
DR Proteomes; UP000001017; 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 PRINTS; PR00112; ACYLPHPHTASE.
DR SUPFAM; SSF54975; SSF54975; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..90
FT /note="Acylphosphatase"
FT /id="PRO_0000326873"
FT DOMAIN 4..90
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 90 AA; 10532 MW; BEA50B3AC5A81A56 CRC64;
MLTTRRVRFY GRVQGINFRS NTLVKALELG VKGWIKNLPD GSVEALFSGE SEQIEKLISY
CVSNMPYAEV KRYDVYIEPY TEFQDFQIKR