ID   P845_THEAC              Reviewed;         208 AA.
AC   Q9HJW8;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Phosphatase Ta0845;
DE            EC=3.1.3.-;
GN   OrderedLocusNames=Ta0845;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
RN   [2]
RP   FUNCTION.
RX   PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
RA   Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA   Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT   "Enzyme genomics: application of general enzymatic screens to discover new
RT   enzymes.";
RL   FEMS Microbiol. Rev. 29:263-279(2005).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of the artificial chromogenic
CC       substrate p-nitrophenyl phosphate (pNPP).
CC       {ECO:0000269|PubMed:15808744}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AL445065; CAC11974.1; -; Genomic_DNA.
DR   RefSeq; WP_010901256.1; NC_002578.1.
DR   AlphaFoldDB; Q9HJW8; -.
DR   SMR; Q9HJW8; -.
DR   STRING; 273075.Ta0845; -.
DR   EnsemblBacteria; CAC11974; CAC11974; CAC11974.
DR   GeneID; 1456388; -.
DR   KEGG; tac:Ta0845; -.
DR   eggNOG; arCOG02293; Archaea.
DR   HOGENOM; CLU_045011_19_3_2; -.
DR   OMA; PFHMLQR; -.
DR   OrthoDB; 93004at2157; -.
DR   BRENDA; 3.1.3.41; 6324.
DR   Proteomes; UP000001024; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.150.240; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   Pfam; PF13419; HAD_2; 1.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR   TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..208
FT                   /note="Phosphatase Ta0845"
FT                   /id="PRO_0000058147"
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   208 AA;  23548 MW;  5A7F7710957E25D2 CRC64;
     MAMQIKGVIF DFDGTLLDSV ELRITAWKKA FQNFGVNVPE DLIRPMIGYP GIDLAKKFVK
     NPLDVEMLQE DYFLKNIESA KFFQDVIPTL AELRKRGIKT AVVTSTRRIV MQKFSLQVDH
     VVTIDDVSKG KPDPEPYLKA LKMMGIPAEE CIVVGDIEND LIPAKKLRCI SVLVKHGRDI
     SSNYADYEIE NIADILNVID HLAEKNNR