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Entry: A0A2K5Z8X0_MANLE
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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
//
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