ID A0A0R3VY54_TAEAS Unreviewed; 379 AA.
AC A0A0R3VY54;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Thymidine phosphorylase {ECO:0000256|PIRNR:PIRNR000478};
DE Short=TP {ECO:0000256|PIRNR:PIRNR000478};
DE EC=2.4.2.4 {ECO:0000256|PIRNR:PIRNR000478};
DE AltName: Full=TdRPase {ECO:0000256|PIRNR:PIRNR000478};
GN ORFNames=TASK_LOCUS2349 {ECO:0000313|EMBL:VDK24933.1};
OS Taenia asiatica (Asian tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000234801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TASK_0000234801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK24933.1, ECO:0000313|Proteomes:UP000282613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible phosphorolysis of thymidine. The
CC produced molecules are then utilized as carbon and energy sources or in
CC the rescue of pyrimidine bases for nucleotide synthesis.
CC {ECO:0000256|PIRNR:PIRNR000478}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate +
CC thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, ChEBI:CHEBI:17821,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.4;
CC Evidence={ECO:0000256|PIRNR:PIRNR000478};
CC -!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway;
CC dTMP from thymine: step 1/2. {ECO:0000256|PIRNR:PIRNR000478}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000478}.
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. {ECO:0000256|PIRNR:PIRNR000478}.
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DR EMBL; UYRS01001496; VDK24933.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3VY54; -.
DR STRING; 60517.A0A0R3VY54; -.
DR WBParaSite; TASK_0000234801-mRNA-1; TASK_0000234801-mRNA-1; TASK_0000234801.
DR UniPathway; UPA00578; UER00638.
DR Proteomes; UP000046400; Unplaced.
DR Proteomes; UP000282613; Unassembled WGS sequence.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf.
DR InterPro; IPR035902; Nuc_phospho_transferase.
DR InterPro; IPR017872; Pyrmidine_PPase_CS.
DR InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR PANTHER; PTHR10515; THYMIDINE PHOSPHORYLASE; 1.
DR PANTHER; PTHR10515:SF0; THYMIDINE PHOSPHORYLASE; 1.
DR Pfam; PF02885; Glycos_trans_3N; 1.
DR Pfam; PF00591; Glycos_transf_3; 1.
DR PIRSF; PIRSF000478; TP_PyNP; 1.
DR SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1.
DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|PIRNR:PIRNR000478};
KW Reference proteome {ECO:0000313|Proteomes:UP000282613};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000478}.
FT DOMAIN 8..68
FT /note="Glycosyl transferase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02885"
FT DOMAIN 82..311
FT /note="Glycosyl transferase family 3"
FT /evidence="ECO:0000259|Pfam:PF00591"
SQ SEQUENCE 379 AA; 40742 MW; 6C2DDBB6F9A12474 CRC64;
MPTICISEIL SKKANGGSLS SAEIDHCIKE VVEDKIDVAQ IGAFLMAVFT KGMTPEEVAN
LTAAMVSHSD KLRWNDQQWA KSVVDKHSTG GVGDKTSHIL APVIAACGGK VPMISGRGLG
VTGGTIDKLE SIDGYSASIG EEKLKSMLND TGFFIVGQTE RLVPADRQLY KYRDVTGTVA
SVPLITASIL SKKLCEGLRG LVMDIKLGSG ALFQNLEEVR ELANSLVTVG RKLDLKVVAV
ISWMDQPLGN CIGNALEMAE VFSILNSGPF QGRLRELVLT LGENMMQAAE IATDRAKARA
MMLEAVRDGR AQTTMRKMLV NQGVNAAVAE ALCSPPPPDC LDVIDYYLTV MGKMANGKKF
VKAPRSGELF HLPCVRWAS
//
