ID   TYPH_BURCH              Reviewed;         438 AA.
AC   A0KCQ9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Thymidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01628};
DE            EC=2.4.2.4 {ECO:0000255|HAMAP-Rule:MF_01628};
DE   AltName: Full=TdRPase {ECO:0000255|HAMAP-Rule:MF_01628};
GN   Name=deoA {ECO:0000255|HAMAP-Rule:MF_01628};
GN   OrderedLocusNames=Bcen2424_6240;
OS   Burkholderia cenocepacia (strain HI2424).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=331272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI2424;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F.,
RA   Konstantinidis K., Tiedje J.M., Richardson P.;
RT   "Complete sequence of chromosome 3 of Burkholderia cenocepacia HI2424.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The enzymes which catalyze the reversible phosphorolysis of
CC       pyrimidine nucleosides are involved in the degradation of these
CC       compounds and in their utilization as carbon and energy sources, or in
CC       the rescue of pyrimidine bases for nucleotide synthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01628}.
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:0000255|HAMAP-Rule:MF_01628};
CC   -!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway;
CC       dTMP from thymine: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01628}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01628}.
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. {ECO:0000255|HAMAP-Rule:MF_01628}.
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DR   EMBL; CP000460; ABK12972.1; -; Genomic_DNA.
DR   RefSeq; WP_011545784.1; NC_008544.1.
DR   AlphaFoldDB; A0KCQ9; -.
DR   SMR; A0KCQ9; -.
DR   KEGG; bch:Bcen2424_6240; -.
DR   HOGENOM; CLU_025040_0_1_4; -.
DR   UniPathway; UPA00578; UER00638.
DR   GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR   GO; GO:0016154; F:pyrimidine-nucleoside 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:0046104; P:thymidine metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   Gene3D; 3.90.1170.30; Pyrimidine nucleoside phosphorylase-like, C-terminal domain; 1.
DR   HAMAP; MF_01628; Thymid_phosp; 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; IPR036566; PYNP-like_C_sf.
DR   InterPro; IPR013102; PYNP_C.
DR   InterPro; IPR018090; Pyrmidine_PPas_bac/euk.
DR   InterPro; IPR017872; Pyrmidine_PPase_CS.
DR   InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR   InterPro; IPR013465; Thymidine_Pase.
DR   NCBIfam; TIGR02643; T_phosphoryl; 1.
DR   NCBIfam; TIGR02644; Y_phosphoryl; 1.
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   Pfam; PF07831; PYNP_C; 1.
DR   PIRSF; PIRSF000478; TP_PyNP; 1.
DR   SMART; SM00941; PYNP_C; 1.
DR   SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1.
DR   SUPFAM; SSF54680; Pyrimidine nucleoside phosphorylase C-terminal domain; 1.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..438
FT                   /note="Thymidine phosphorylase"
FT                   /id="PRO_0000335771"
SQ   SEQUENCE   438 AA;  45454 MW;  1EEEEB4AC6F92063 CRC64;
     MFLPQEFIRR KRDGQPLDRD DMAAFVRGVT DGSVTEGQVA AFAMAVYFND LSTDERVALT
     LAQRDSGDVL DWRALDLGGP VIDKHSTGGV GDVVSLMLGP MVAACGGYVP MISGRGLGHT
     GGTLDKLSAI PGYDVMPDTD AFRRTVREVG VAIIGQTARL APADKRIYAI RDVTATVESV
     AMITASILSK KLAAGLDGLV MDVKVGSGAF MPTAEKSAEL ARSIVDVGNG AGMKTTAILT
     DMNQSLAPCA GNALEVACAI DYLTGKSRPA RLHDVTMALS AELLVTGGLA RDAAHAREKL
     QQALDSGAAA ERFARMVAAL GGPADLLDAP ARHLARAAVI VPVPAPVSGV VQRVDCRALG
     LAVVALGGGR TRAEDAIDVS VGLSALAEIG QRIEAGEPLG FVHARDEAAA AHAVDAIRRG
     YVLGETGEAP PTLYQRVD
//