ID   TYPH_LEGPA              Reviewed;         517 AA.
AC   Q5X2M8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=lpp2359;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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; CR628336; CAH13512.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5X2M8; -.
DR   SMR; Q5X2M8; -.
DR   KEGG; lpp:lpp2359; -.
DR   LegioList; lpp2359; -.
DR   HOGENOM; CLU_025040_6_0_6; -.
DR   OMA; QMVASIM; -.
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_0000225646"
SQ   SEQUENCE   517 AA;  55341 MW;  71830C78AF8F000E CRC64;
     MHHSFLSANG GIVVSKQTSH GLRLKHLGIK TYHEAIIYMR EDCHVCHSEG FEVQTRIQVT
     LGQRSIIATL NVVTSELLQP GEAGLSDYAW ESLHAKEGDE IQVSHPKPLE SLSYVHTKIY
     GKELSYEQMK VIIDDVLSGR LSDVQISAFL AASSAGRLTR TEIMKLTKAM IDSGDRLSWS
     SPLVVDKHCV GGLPGNRTTL IVVPIVAAFG LMIPKTSSRA ITSPAGTADT METLAPVHLS
     PQKMRQVVEQ ENGCIVWGGA VSLSPADDVL IRVERAIDLD SEGQLVASIL SKKIATGATH
     AVIDIPVGPT AKVRNQSMAL LLKQLLEEVG NELGLVVRTL LTDGSQPVGH GIGPSLEARD
     VMAVLQGLPD APNDLRERAL TLAGAALECS SKVPPGLGKS IATQLLDSGQ AFKKFQAICE
     AQGGMRELTK ARFTYPVVAA KAGKVSLIDN RKLAKIAKLA GAPKSKSAGI DLHSHVGESV
     EKGEPLFTIH SESSGELHYA CDLLRDKQDI IILGENS