ID   THTPA_MACFA             Reviewed;         230 AA.
AC   Q9BGW0;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Thiamine-triphosphatase;
DE            Short=ThTPase;
DE            EC=3.6.1.28;
GN   Name=THTPA; ORFNames=QflA-12514;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Frontal cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolase highly specific for thiamine triphosphate (ThTP).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + thiamine triphosphate = H(+) + phosphate + thiamine
CC         diphosphate; Xref=Rhea:RHEA:11744, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58937,
CC         ChEBI:CHEBI:58938; EC=3.6.1.28;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ThTPase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB055296; BAB21921.1; -; mRNA.
DR   RefSeq; NP_001270466.1; NM_001283537.1.
DR   AlphaFoldDB; Q9BGW0; -.
DR   SMR; Q9BGW0; -.
DR   STRING; 9541.XP_005560942.1; -.
DR   GeneID; 102122817; -.
DR   CTD; 79178; -.
DR   eggNOG; ENOG502S5G9; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0050333; F:thiamin-triphosphatase activity; ISS:UniProtKB.
DR   GO; GO:0042357; P:thiamine diphosphate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR   CDD; cd07758; ThTPase; 1.
DR   InterPro; IPR033469; CYTH-like_dom_sf.
DR   InterPro; IPR023577; CYTH_domain.
DR   InterPro; IPR039582; THTPA.
DR   InterPro; IPR012177; ThTPase_euk.
DR   PANTHER; PTHR14586; PTHR14586; 1.
DR   Pfam; PF01928; CYTH; 1.
DR   PIRSF; PIRSF036561; ThTPase; 1.
DR   SMART; SM01118; CYTH; 1.
DR   SUPFAM; SSF55154; SSF55154; 1.
DR   PROSITE; PS51707; CYTH; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8MKF1"
FT   CHAIN           2..230
FT                   /note="Thiamine-triphosphatase"
FT                   /id="PRO_0000221491"
FT   DOMAIN          5..201
FT                   /note="CYTH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01044"
FT   BINDING         7
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8MKF1"
SQ   SEQUENCE   230 AA;  25342 MW;  99F683E6475705C3 CRC64;
     MAQGLIEVER KFLPGPGTEE RLQELGGTLE HRVTFRDTYY DTPELSLMQA DHWLRRREDS
     GWELKCPGAA GVLGHHTEYK ELTAEPTIVA QLCKVLGADG LGAGDVAAVL DPLGLQEVAS
     FVTKRSAWKL VLLGTDEEEP QLKVDLGTAD FGYAVGEVEA LVHEEAEVPA ALEKIHRLSS
     MLGVPAQETA PAKLIVYLQR FRPQNYQRLL EVNSSKQRPQ ATEDPDNCLG