ID A0A2K5Z8X0_MANLE Unreviewed; 230 AA.
AC A0A2K5Z8X0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Thiamine-triphosphatase {ECO:0000256|ARBA:ARBA00020088, ECO:0000256|PIRNR:PIRNR036561};
DE Short=ThTPase {ECO:0000256|PIRNR:PIRNR036561};
DE EC=3.6.1.28 {ECO:0000256|ARBA:ARBA00012378, ECO:0000256|PIRNR:PIRNR036561};
GN Name=THTPA {ECO:0000313|Ensembl:ENSMLEP00000024257.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000024257.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000024257.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Hydrolase highly specific for thiamine triphosphate (ThTP).
CC {ECO:0000256|ARBA:ARBA00002106, ECO:0000256|PIRNR:PIRNR036561}.
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 Evidence={ECO:0000256|ARBA:ARBA00000052,
CC ECO:0000256|PIRNR:PIRNR036561};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR036561-2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR036561-2};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC ECO:0000256|PIRNR:PIRNR036561}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR036561}.
CC -!- SIMILARITY: Belongs to the ThTPase family.
CC {ECO:0000256|ARBA:ARBA00008181, ECO:0000256|PIRNR:PIRNR036561}.
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DR RefSeq; XP_011846090.1; XM_011990700.1.
DR RefSeq; XP_011846091.1; XM_011990701.1.
DR AlphaFoldDB; A0A2K5Z8X0; -.
DR STRING; 9568.ENSMLEP00000024257; -.
DR Ensembl; ENSMLET00000047779.1; ENSMLEP00000024257.1; ENSMLEG00000036281.1.
DR GeneID; 105547200; -.
DR KEGG; mleu:105547200; -.
DR CTD; 79178; -.
DR GeneTree; ENSGT00390000005996; -.
DR OMA; SLMRADH; -.
DR OrthoDB; 5489660at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0050333; F:thiamine triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:Ensembl.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:Ensembl.
DR GO; GO:0006772; P:thiamine metabolic process; IEA:InterPro.
DR CDD; cd07758; ThTPase; 1.
DR Gene3D; 2.40.320.10; Hypothetical Protein Pfu-838710-001; 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; THIAMINE-TRIPHOSPHATASE; 1.
DR PANTHER; PTHR14586:SF1; THIAMINE-TRIPHOSPHATASE; 1.
DR Pfam; PF01928; CYTH; 1.
DR PIRSF; PIRSF036561; ThTPase; 1.
DR SMART; SM01118; CYTH; 1.
DR SUPFAM; SSF55154; CYTH-like phosphatases; 1.
DR PROSITE; PS51707; CYTH; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR036561};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036561};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036561-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036561-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT DOMAIN 5..201
FT /note="CYTH"
FT /evidence="ECO:0000259|PROSITE:PS51707"
FT REGION 211..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-2"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-2"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-1"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-1"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-1"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-1"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-1"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-2"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-2"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-1"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-2"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036561-1"
SQ SEQUENCE 230 AA; 25357 MW; 83D32CC7302097BF CRC64;
MAQGLIEVER KFLPGPGTEE RLQELGGTLE HRVTFRDTYY DTPELSLMQA DHWLRRREDS
GWELKCPGAA GVLGHHTEYK ELTAEPTIVA QLCKVLGADG LGAGDVAAVL GPLGLQEVAS
FVTKRSAWKL VLLGTDEEEP QLRVDLDTAD FGYAVGEVEA LVHEEAEVPA ALEKIHRLSS
MLGVPAQETA PAKLIVYLQR FRPQDYQRLL EVNSSKQRPQ GTEDPDNCLG
//