ID   TYPH_RHOPS              Reviewed;         514 AA.
AC   Q13B59;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=RPD_1443;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-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}.
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DR   EMBL; CP000283; ABE38680.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q13B59; -.
DR   SMR; Q13B59; -.
DR   STRING; 316057.RPD_1443; -.
DR   KEGG; rpd:RPD_1443; -.
DR   eggNOG; COG0213; Bacteria.
DR   HOGENOM; CLU_025040_6_0_5; -.
DR   BioCyc; RPAL316057:RPD_RS07290-MONOMER; -.
DR   Proteomes; UP000001818; 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..514
FT                   /note="Putative thymidine phosphorylase"
FT                   /id="PRO_0000314716"
SQ   SEQUENCE   514 AA;  54666 MW;  1253EE274B903BB7 CRC64;
     MNASHLSRPP LTIRRISLDT GRENVAVISR RSRALRADVF RGFSRVALRI NTKVLLATLM
     ITDDDAMIGP DELGLSEPAF RRFNEPVGSA VSVSPAQPPA SLDAVRAKIQ GHTLTPAEIT
     AVIDDVAHFR YSDMEIAAFL ISAARFTSTD ELLALVDAMA SVGTRLKWQN PIVVDKHCIG
     GIPGNRTTMI VVPIVAAQGL MIPKTSSRAI TSPAGTADTM EVLARVDLDV EQMKRVVTTC
     GGCLIWGGHV NLSPADDILI SVERPLSLDT PEQMVASIMS KKLAAGSTRL LIDFPVGPSA
     KIASASEAMR LRKLFEFVGD HFGIAVEVVT TDGRQPIGRG IGPVLEARDV MAVLGNEPNA
     PADLREKSLR LAAHLLEYDP LLRGGAGYAR AKELLDSGAA LKKMQQIIDA QGPSVCNSEL
     GSHAADVLAP ADGVVNGIDC LRINRLARTA GAPIVKGAGI DLFKKIGDRV DQGEPIYRIY
     ASDRSELDLA IAAAEAESGF SVNHHSPAAV EPVS
//