ID   TYPH_LEGPC              Reviewed;         517 AA.
AC   A5IFN1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   13-SEP-2023, 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=LPC_2257;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABQ56181.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000675; ABQ56181.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A5IFN1; -.
DR   SMR; A5IFN1; -.
DR   KEGG; lpc:LPC_2257; -.
DR   HOGENOM; CLU_025040_6_0_6; -.
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; 2.40.40.20; -; 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..517
FT                   /note="Putative thymidine phosphorylase"
FT                   /id="PRO_0000314700"
SQ   SEQUENCE   517 AA;  55259 MW;  63735B276D67D4E4 CRC64;
     MHHSFLSANG GVVMSKKTAH GLRLKHLGIK TYHEAIIYMR EDCHVCHSEG FEVQTRIQVT
     LGQHSIIATL NVVTSELLAP GEAGLSDYAW DALHAKEGDE IQVSHPKPLE SLSYVHTKIY
     GNELSYEQMK VIIDDVLSGR LSDVQISAFL AASSAGRLTR TEIMKLTKAM IDSGDRLSWS
     SPLVVDKHCV GGLPGNRTTL IVVPIVAAFG LMIPKTSSRA ITSPAGTADT METLAPVHLS
     PQKMRQVVEQ ENGCIVWGGA VSLSPADDVL IRVERAIDLD SEGQLVASIL SKKIATGATH
     AVIDIPVGPT AKVRNQSMAL LLKQSLEEVG NELGLVVHTI LTDGSQPVGH GIGPSLEARD
     VMSVLQGLPD APNDLRERAL TLAGAALECS SKVQPGLGKS IAKQILESGK AFKKFQAICE
     AQGGMRELTK ARFTHPVVAA KEGKVSLIDN RKLAKIAKLA GAPKSKSAGI DLHAHVGESV
     EQGEPLFTIH SESSGELNYA CDLLRDKQDI IILGENS
//