ID   TYPH_RHOPB              Reviewed;         513 AA.
AC   Q20Z21;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=RPC_4089;
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18;
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., Anderson I., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
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; CP000301; ABD89615.1; -; Genomic_DNA.
DR   RefSeq; WP_011474496.1; NC_007925.1.
DR   AlphaFoldDB; Q20Z21; -.
DR   SMR; Q20Z21; -.
DR   STRING; 316056.RPC_4089; -.
DR   EnsemblBacteria; ABD89615; ABD89615; RPC_4089.
DR   KEGG; rpc:RPC_4089; -.
DR   eggNOG; COG0213; Bacteria.
DR   HOGENOM; CLU_025040_6_0_5; -.
DR   OMA; QMVASIM; -.
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..513
FT                   /note="Putative thymidine phosphorylase"
FT                   /id="PRO_0000314715"
SQ   SEQUENCE   513 AA;  54925 MW;  A97C3D79D65D8A8A CRC64;
     MTSADAPRPQ LKIRLIHLDT GRENVAVMSR RSKALRPEVF SGFSRVEIRR NAKSVLATLL
     ITDDDALVGP DELGLAEPAF RRFGEPAGTF VTVSPATPPD SLDAVRGKIQ GRTLSAAEIT
     AIVNDLTRYR YSDMEIAAFL IGAARFMTSD ELLALVSAMA SVGTQLRWDR PIVVDKHCIG
     GIPGNRTSMI LVPIVAAHGL TIPKTSSRAI TSPAGTADTM EVLARVDVSV AEMKEIVAAC
     NGCLIWGGHV NLSPADDILI SVERPLCLDT REQMVASIMS KKLAAGSTHL LVDLPVGPTA
     KVASALDAMR LRKLFEFVGD HFGIAVETIT TDGRQPIGNG IGPVLEAQDV MAVLGNDPKA
     PADLREKSLR LAAHLLEYDP HLRGGAGYAR ARELLESGAA LKQMQKIIDN QGPSTCHKDL
     GTLTAEVTAE RDGVVSAIDC LQLNRLARTA GAPIDKGAGI RLFKKVGDRV EAGEPLYRIY
     AFDPAERELA VAAAKLACGY TVDDAQTFRE QVM