ID A0A3Q3NMH3_9LABR Unreviewed; 215 AA.
AC A0A3Q3NMH3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Thiamine-triphosphatase {ECO:0000256|ARBA:ARBA00020088};
DE EC=3.6.1.28 {ECO:0000256|ARBA:ARBA00012378};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000036455.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000036455.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Hydrolase highly specific for thiamine triphosphate (ThTP).
CC {ECO:0000256|ARBA:ARBA00002106}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ThTPase family.
CC {ECO:0000256|ARBA:ARBA00008181}.
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DR AlphaFoldDB; A0A3Q3NMH3; -.
DR STRING; 56723.ENSLBEP00000036455; -.
DR Ensembl; ENSLBET00000037983.1; ENSLBEP00000036455.1; ENSLBEG00000027284.1.
DR GeneTree; ENSGT00390000005996; -.
DR InParanoid; A0A3Q3NMH3; -.
DR Proteomes; UP000261660; 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 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660}.
FT DOMAIN 2..201
FT /note="CYTH"
FT /evidence="ECO:0000259|PROSITE:PS51707"
SQ SEQUENCE 215 AA; 24826 MW; BA2C61EC4D71B8E9 CRC64;
MSVEVERKFL CNADILKTLE ETEVTCVGQH QFKDQYFDSP NFDLTLKDMW LRKRKECWEL
KSPTAEETSG EQSKSAALCT RYKEITNLPE IQLRVKEVLK DVCEDTEKSS SMENESWHSK
MNLACFAEFT TVRRSFILED GVRIDLDQAD FGYHVGEIEV LVPEEGDVQS ALEKIERTAR
KLGLAGDQRV EGKMSVYLKR NNPEHYAKLL RAHVL
//
