ID   TYPH_RHOPT              Reviewed;         514 AA.
AC   B3QKL9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Rpal_4625;
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) 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; CP001096; ACF03116.1; -; Genomic_DNA.
DR   RefSeq; WP_012497413.1; NC_011004.1.
DR   AlphaFoldDB; B3QKL9; -.
DR   SMR; B3QKL9; -.
DR   EnsemblBacteria; ACF03116; ACF03116; Rpal_4625.
DR   KEGG; rpt:Rpal_4625; -.
DR   HOGENOM; CLU_025040_6_0_5; -.
DR   OMA; QMVASIM; -.
DR   OrthoDB; 1724909at2; -.
DR   BioCyc; RPAL395960:RPAL_RS22885-MON; -.
DR   Proteomes; UP000001725; 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; 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..514
FT                   /note="Putative thymidine phosphorylase"
FT                   /id="PRO_1000132353"
SQ   SEQUENCE   514 AA;  54652 MW;  245697DBC324B925 CRC64;
     MNAPDLTRPP LTIRRISLDT GRENVAVISR RSRALRPEVF RGFSRVELRI NSKVLLATLM
     ITDDDAMIGP DEVGLSEPAF RRFNEPVGSA VSVTPARSPA SLDAVRAKIQ GHTLSAAEIT
     AIVDDLAHFR YSDMEIAAFL ISAARFTTTD ELLALVGAMA SVGTKLTWDT PIVVDKHCIG
     GIPGNRTTMI VVPIVAAHGL MIPKTSSRAI TSPAGTADTM ELLARVDLDV EQMKQVVHAC
     GGCLVWGGHV NLSPADDILI SVERPLSLDT PEQMVASIMS KKLAAGSTRL LIDFPVGPSA
     KVTSANEAMR LRKLFEFVGD HFGISVEVVT TDGRQPIGRG IGPVLEARDV MAVLGNKPGA
     PADLREKSLR LAAHLLEYDP KLRGGTGYAR AKELLDSGAA LKKMQQIIDA QGPSPCPAEL
     GSYAADVLAA ADGVVNGIDC LRINRLARSA GAPVAKGAGI DLFKKIGDRV EKGEPLYRVY
     ASDRSEFDLA LAAAQAESGF AINHHTPADV DLVS