ID A0A2U3W2E4_ODORO Unreviewed; 230 AA.
AC A0A2U3W2E4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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|RefSeq:XP_004402129.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004402129.1};
RN [1] {ECO:0000313|RefSeq:XP_004402129.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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}.
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 RefSeq; XP_004402129.1; XM_004402072.1.
DR AlphaFoldDB; A0A2U3W2E4; -.
DR GeneID; 101384998; -.
DR CTD; 79178; -.
DR OrthoDB; 5489660at2759; -.
DR Proteomes; UP000245340; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050333; F:thiamine triphosphate phosphatase activity; IEA:UniProtKB-EC.
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:UP000245340}.
FT DOMAIN 5..201
FT /note="CYTH"
FT /evidence="ECO:0000259|PROSITE:PS51707"
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; 25295 MW; D7AFD85E86D85D39 CRC64;
MAQALIEVER KFVPGPDTQK RLQELGGTLE HRVTFRDSYY DTPELSLMRA DHWLRQREGS
GWELKYPGVA VVSGPHTEYV ELTVEPAIVA QLCEVLGADI LGAGSVAVVL GPLGLQEVAS
FVTKRSAWKL VLSGADEEEP LLRVDLDTAD FGYAVGEVEA LVHEKAEVPA ALEKINSLSS
MLGVLAQERA PAKVIMHLQR FRPQDYQHLL EVFSPRERPQ GTKAPDSSLG
//
