ID A0A6P5A105_BRABE Unreviewed; 262 AA.
AC A0A6P5A105;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE RecName: Full=Thiamine-triphosphatase {ECO:0000256|ARBA:ARBA00020088};
DE EC=3.6.1.28 {ECO:0000256|ARBA:ARBA00012378};
GN Name=LOC109479368 {ECO:0000313|RefSeq:XP_019636882.1};
OS Branchiostoma belcheri (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7741 {ECO:0000313|Proteomes:UP000515135, ECO:0000313|RefSeq:XP_019636882.1};
RN [1] {ECO:0000313|RefSeq:XP_019636882.1}
RP IDENTIFICATION.
RC TISSUE=Gonad {ECO:0000313|RefSeq:XP_019636882.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- FUNCTION: Hydrolase highly specific for thiamine triphosphate (ThTP).
CC {ECO:0000256|ARBA:ARBA00002106}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=thiamine triphosphate + H2O = thiamine diphosphate + phosphate
CC + H(+); Xref=Rhea:RHEA:11744, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58937, ChEBI:CHEBI:58938; EC=3.6.1.28;
CC Evidence={ECO:0000256|ARBA:ARBA00048194};
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 RefSeq; XP_019636882.1; XM_019781323.1.
DR AlphaFoldDB; A0A6P5A105; -.
DR GeneID; 109479368; -.
DR KEGG; bbel:109479368; -.
DR OrthoDB; 442176at2759; -.
DR Proteomes; UP000515135; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:TreeGrafter.
DR GO; GO:0050333; F:thiamine triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0042357; P:thiamine diphosphate metabolic process; IEA:TreeGrafter.
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:UP000515135}.
FT DOMAIN 59..246
FT /note="CYTH"
FT /evidence="ECO:0000259|PROSITE:PS51707"
FT REGION 19..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..46
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 262 AA; 29113 MW; 61E6022E51835163 CRC64;
MNVFRLQTHR RIVLSAVDME VQEGGGSSSA GTKGEGGDVA GGGEGASGPR DHNNKPSGVI
EVERKFSFSE GSEEKLRKAG AVCKEESSFH DVYFDTEEFV LTLADHWLRK REGRWELKCP
PASRDRASLV EQYVELQHEA DILKQLAAIL NVRAGSVDEL VRRASCEPFC NFQTDRKTYT
LEGGFKIDLD QTDFGFRVGE IELICQKQDD VPEALRKIDA LAEKLGFVSK TKIPGKMSAF
LKTFREKHYD ALVKGGLLTP IT
//
