ID   TYPH_LEGPN              Reviewed;         517 AA.
AC   Q8RNP4;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 88.
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};
OS   Legionella pneumophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=446;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12065505; DOI=10.1128/iai.70.7.3637-3648.2002;
RA   Rankin S., Li Z., Isberg R.R.;
RT   "Macrophage-induced genes of Legionella pneumophila: protection from
RT   reactive intermediates and solute imbalance during intracellular growth.";
RL   Infect. Immun. 70:3637-3648(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}.
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DR   EMBL; AF480912; AAM00626.1; -; Genomic_DNA.
DR   RefSeq; WP_010946757.1; NZ_LOLY01000005.1.
DR   AlphaFoldDB; Q8RNP4; -.
DR   SMR; Q8RNP4; -.
DR   STRING; 91892.BIZ52_11590; -.
DR   PRIDE; Q8RNP4; -.
DR   eggNOG; COG0213; Bacteria.
DR   OrthoDB; 1724909at2; -.
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; Transferase.
FT   CHAIN           1..517
FT                   /note="Putative thymidine phosphorylase"
FT                   /id="PRO_0000059095"
SQ   SEQUENCE   517 AA;  55296 MW;  3903064A69DFB546 CRC64;
     MHDSFLSANG GFVVSKKTPH GLRLKHLGIK TYHEAIIYMR EDCHVCHSEG FEVQTRIQVT
     LGSRSIIATL NVVTSELLQP GEAGLSDYAW ESLHAKEGDE IQVSHPKPLE SLSYVHAKIY
     GNELSFEQMK VIIDDVLSGR LSDVQISAFL AASGAGRLTR TEVMKLTKAM IDSGDRLSWP
     SPLVVDKHCV GGLPGNRTTL IVVPIVASFG LMIPKTSSRA ITSPAGTADT METLAPVHLS
     PQKMRQVVEQ ENGCIVWGGA VSLSPADDVL IRVERAIDLD SEGQLVASIL SKKIATGATH
     AVIDIPVGPT AKVRNQSMAL LLKQSLEEVG NELGLVVRAL FTDGSQPVGH GIGPSLEARD
     VLAVLQGLPD APNDLRERAL TLAGAALECS SKVPPGLGKS IATQLLESGQ AFKKFQAICE
     AQGGMRELTK ARFTYPVVAA KEGKVSLIDN RKLAKIAKLA GAPKSKSAGI DLHAHVGESV
     EQGEPLFTIH SESLGELHYA CDLLRDKQDI IILGENP