ID   TYPH_SHEPC              Reviewed;         443 AA.
AC   A4Y9A7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=Sputcn32_2821;
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 / ATCC BAA-453;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) 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; CP000681; ABP76540.1; -; Genomic_DNA.
DR   RefSeq; WP_011788541.1; NC_009438.1.
DR   AlphaFoldDB; A4Y9A7; -.
DR   SMR; A4Y9A7; -.
DR   STRING; 319224.Sputcn32_2821; -.
DR   GeneID; 45043310; -.
DR   KEGG; spc:Sputcn32_2821; -.
DR   eggNOG; COG0213; Bacteria.
DR   HOGENOM; CLU_025040_0_1_6; -.
DR   OMA; DVWRRMI; -.
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; -; 1.
DR   Gene3D; 3.90.1170.30; -; 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   PANTHER; PTHR10515; PTHR10515; 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; SSF47648; SSF47648; 1.
DR   SUPFAM; SSF52418; SSF52418; 1.
DR   SUPFAM; SSF54680; SSF54680; 1.
DR   TIGRFAMs; TIGR02643; T_phosphoryl; 1.
DR   TIGRFAMs; TIGR02644; Y_phosphoryl; 1.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..443
FT                   /note="Thymidine phosphorylase"
FT                   /id="PRO_1000069671"
SQ   SEQUENCE   443 AA;  46903 MW;  10207C9236BB2BE6 CRC64;
     MFLAQEIIRK KRNGLALSPA EIQFFVQGIT TNAVSEGQIA AFGMAVYFND MNMDERIALT
     TAMRDSGTVL NWQSLGLNGP VIDKHSTGGV GDVISLMLGP MAAACGGYVP MISGRGLGHT
     GGTLDKFDAI PGYQTEPSSE LFRKVVKEVG VAIIGQTGDL VPADKRFYSI RDNTATVESI
     SLITASILSK KLACNLDALA MDVKVGSGAF MPTYEASEEL ARSITAVANG AGTKTTALLT
     DMNQVLASCA GNAVEVKEAI DFLTGAYRNP RLYEVTMGLC AEMLLLGGLA SNETEARAKL
     NRVLDNGRAA EIFGKMVSGL GGPVDFVENY SKYLPQSQII RPVFADAKGY AYSMDTRELG
     LAVVTLGGGR RKPGDALDYS VGLTQVCALG DKIDSSTPIA VIHAQSEAAF TEAENAVKKA
     IHIGETAPEK TPEIYAYIRA ADL