ID TYPH_RALN1 Reviewed; 507 AA. AC Q8Y2X7; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 118. 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=RSc0204; ORFNames=RS00636; OS Ralstonia nicotianae (strain GMI1000) (Ralstonia solanacearum). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=267608; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GMI1000; RX PubMed=11823852; DOI=10.1038/415497a; RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M., RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M., RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M., RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P., RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.; RT "Genome sequence of the plant pathogen Ralstonia solanacearum."; RL Nature 415:497-502(2002). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL646052; CAD13732.1; -; Genomic_DNA. DR RefSeq; WP_011000171.1; NC_003295.1. DR AlphaFoldDB; Q8Y2X7; -. DR SMR; Q8Y2X7; -. DR STRING; 267608.RSc0204; -. DR EnsemblBacteria; CAD13732; CAD13732; RSc0204. DR GeneID; 60499713; -. DR KEGG; rso:RSc0204; -. DR eggNOG; COG0213; Bacteria. DR HOGENOM; CLU_025040_6_0_4; -. DR Proteomes; UP000001436; 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; 1.20.970.50; -; 1. 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_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 NCBIfam; TIGR02645; ARCH_P_rylase; 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 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..507 FT /note="Putative thymidine phosphorylase" FT /id="PRO_0000059096" SQ SEQUENCE 507 AA; 53886 MW; DF121AC8CB2489AA CRC64; MLAPPEVAAL PDRLTFKPLG IDTWQEHVIY MHPDCAICRA EGFTAQARVE VRIGLRSLIA TLNLVGSGLL EMCEVSLSVS AVETLMARPG DIVTVSHAPA LESLRAVRAK IYGAHLDTHQ LASVVGDIAK ERYADVHIAA FLSACAGGRM SVKETIDLTQ AMVDSGECLE WDREIVADKH CVGGLPGNRT SPIVVAIAAA AGLLLPKTSS RAITSPAGTA DTMETLTRVA LSATELRRVV DRVGASLAWG GALSLSPADD VLIRVERALD VDSDAQLAAS ILSKKIAAGS THVLIDVPVG PTAKVRSLQD LERLRMLLER VARSFGVRVT IVRTDGSQPV GRGIGPALEA RDVLAVLQRS PAAPFDLRER SLLLAATLLE FCGAVEQGAG LEMATGVLDS GAAWRKFEEI CEAQGGLRVP GEAIFRRDVV AEQDGIVTEI DNRHLARIAK LAGAPMRQVA GVEMHVRLHD QVKAGRPLFT IHAQASGELE YSVAYALMHP AVSIAPT //