ID   TYPH_POLSJ              Reviewed;         511 AA.
AC   Q12E97;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Putative thymidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_00703};
DE            EC=2.4.2.4 {ECO:0000255|HAMAP-Rule:MF_00703};
DE   AltName: Full=TdRPase {ECO:0000255|HAMAP-Rule:MF_00703};
GN   OrderedLocusNames=Bpro_1194;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX   NCBI_TaxID=296591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500;
RX   PubMed=18723656; DOI=10.1128/aem.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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_00703};
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. Type 2 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00703}.
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DR   EMBL; CP000316; ABE43145.1; -; Genomic_DNA.
DR   RefSeq; WP_011482146.1; NC_007948.1.
DR   AlphaFoldDB; Q12E97; -.
DR   SMR; Q12E97; -.
DR   STRING; 296591.Bpro_1194; -.
DR   EnsemblBacteria; ABE43145; ABE43145; Bpro_1194.
DR   KEGG; pol:Bpro_1194; -.
DR   eggNOG; COG0213; Bacteria.
DR   HOGENOM; CLU_025040_6_0_4; -.
DR   OMA; QMVASIM; -.
DR   OrthoDB; 1724909at2; -.
DR   Proteomes; UP000001983; Chromosome.
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:InterPro.
DR   Gene3D; 3.40.1030.10; -; 1.
DR   Gene3D; 3.90.1170.30; -; 1.
DR   HAMAP; MF_00703; Thymid_phosp_2; 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; IPR017872; Pyrmidine_PPase_CS.
DR   InterPro; IPR028579; Thym_Pase_Put.
DR   InterPro; IPR013466; Thymidine/AMP_Pase.
DR   InterPro; IPR000053; Thymidine/pyrmidine_PPase.
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   SMART; SM00941; PYNP_C; 1.
DR   SUPFAM; SSF47648; SSF47648; 1.
DR   SUPFAM; SSF52418; SSF52418; 1.
DR   SUPFAM; SSF54680; SSF54680; 1.
DR   TIGRFAMs; TIGR02645; ARCH_P_rylase; 1.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..511
FT                   /note="Putative thymidine phosphorylase"
FT                   /id="PRO_0000314706"
SQ   SEQUENCE   511 AA;  53699 MW;  39A4B6625FA46595 CRC64;
     MQTPPTPLSS LTPHKLRLRR LGIDTYQEPV LYMHRDCRVC HSEGFEAQSR VELALGDRTI
     VATLNVVSGD FLAPDEAGLS EAAWRLLGAQ EGDMVSPRHP APIESLGHVR AKVYGRHLTQ
     AAITAVIEDV TAGRYSDLQL AAFVTACAGD RLDQEETVSL TRAMVAAGER IDWGEGLVMD
     KHCVGGLPGN RTTMVIVPIV AACGLRMPKT SSRAITSPAG TADTMETLAP VDLDVAQIRR
     VVERTGGCVV WGGAVRLSPA DDILIRVERP LDLDSQGQLV ASILSKKVAA GSTHVLIDMP
     VGPTAKVRSA EAADLLGRLL GQVGQTLGLR MRVVQTDGLA PVGRGIGPAL EARDVLAVLR
     NLATAPADLA QRSLLLAGEV LEFGGAAPAG GGLALASAVL ADGRAWRKFQ DICAAQGGLR
     EPPVAAHQQA VHALRSGSVL AIDNRRLARI AKLAGAPGAA CAGIDLHVRP GEFVERGQPL
     FTLHAATPGE LAYALEYAAS QAETVHVLED A