THTPA_BOVIN
ID THTPA_BOVIN Reviewed; 219 AA.
AC Q8MKF1; Q2KJ88;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Thiamine-triphosphatase;
DE Short=ThTPase;
DE EC=3.6.1.28;
GN Name=THTPA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT ALA-2, PARTIAL PROTEIN SEQUENCE,
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, CHARACTERIZATION, MASS
RP SPECTROMETRY, AND COFACTOR.
RX PubMed=11827967; DOI=10.1074/jbc.m111241200;
RA Lakaye B., Makarchikov A.F., Antunes A.F., Zorzi W., Coumans B.,
RA De Pauw E., Wins P., Grisar T., Bettendorff L.;
RT "Molecular characterization of a specific thiamine triphosphatase widely
RT expressed in mammalian tissues.";
RL J. Biol. Chem. 277:13771-13777(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolase highly specific for thiamine triphosphate (ThTP).
CC {ECO:0000269|PubMed:11827967}.
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;
CC Evidence={ECO:0000269|PubMed:11827967};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:11827967};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11827967}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11827967}.
CC -!- MASS SPECTROMETRY: Mass=23892; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11827967};
CC -!- SIMILARITY: Belongs to the ThTPase family. {ECO:0000305}.
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DR EMBL; AF432863; AAM22404.1; -; mRNA.
DR EMBL; BC105468; AAI05469.1; -; mRNA.
DR RefSeq; NP_776895.1; NM_174470.4.
DR RefSeq; XP_005211310.1; XM_005211253.3.
DR RefSeq; XP_005211311.1; XM_005211254.3.
DR RefSeq; XP_010807168.1; XM_010808866.2.
DR AlphaFoldDB; Q8MKF1; -.
DR SMR; Q8MKF1; -.
DR STRING; 9913.ENSBTAP00000009334; -.
DR iPTMnet; Q8MKF1; -.
DR PaxDb; Q8MKF1; -.
DR PRIDE; Q8MKF1; -.
DR Ensembl; ENSBTAT00000009334; ENSBTAP00000009334; ENSBTAG00000007097.
DR GeneID; 282090; -.
DR KEGG; bta:282090; -.
DR CTD; 79178; -.
DR VEuPathDB; HostDB:ENSBTAG00000007097; -.
DR VGNC; VGNC:35852; THTPA.
DR eggNOG; ENOG502S5G9; Eukaryota.
DR GeneTree; ENSGT00390000005996; -.
DR HOGENOM; CLU_105907_0_0_1; -.
DR InParanoid; Q8MKF1; -.
DR OrthoDB; 1453157at2759; -.
DR TreeFam; TF333398; -.
DR BRENDA; 3.6.1.28; 908.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000007097; Expressed in semen and 105 other tissues.
DR ExpressionAtlas; Q8MKF1; baseline and differential.
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:0016311; P:dephosphorylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium;
KW Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11827967"
FT CHAIN 2..219
FT /note="Thiamine-triphosphatase"
FT /id="PRO_0000221489"
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:0000269|PubMed:11827967"
SQ SEQUENCE 219 AA; 23983 MW; 6E617AA2FDB7ACC3 CRC64;
MAQGLIEVER KFVPGPSTEE RLQELGGTLE HRVTFRDSYY DTPELSLMRA DYWLRQREGS
GWELKCPGAA GVSGPHTEYT ELTAEPSIVA QLCEVLGAEV PGAGGVAAVL GPLGLQLVAS
FVTKRSAWKL VLSGADGEER LLRVDLDTAD FGYAVGEVEA LVHKEAEVPA ALEKIHHLSS
LLGVLEQGRA PAKLIVYLQR FRPQDYQRLL EVYGSKEKP
