TYPH_RHOP5
ID TYPH_RHOP5 Reviewed; 513 AA.
AC Q07J10;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, 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=RPE_4149;
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53;
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., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-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; CP000463; ABJ08074.1; -; Genomic_DNA.
DR RefSeq; WP_011665534.1; NC_008435.1.
DR AlphaFoldDB; Q07J10; -.
DR SMR; Q07J10; -.
DR STRING; 316055.RPE_4149; -.
DR PRIDE; Q07J10; -.
DR EnsemblBacteria; ABJ08074; ABJ08074; RPE_4149.
DR KEGG; rpe:RPE_4149; -.
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_0000314714"
SQ SEQUENCE 513 AA; 54877 MW; 01A9C95320EF54B3 CRC64;
MSPVDAARPQ LKIRQIHLDT GRENVAVISR HSKALRPEVF SGFSRVEIRR GNQSMLATLL
ITDDNAMVGP DDLGLAEPAF RRFGEAAGSL VSVTPASPPA SLDAVRGKIQ GRTLTAPEIE
AIVNDLARYR YSDMEIAAFL IGAARFMTSD ELLALVSAMA SVGTQLRWDR PVVVDKHCIG
GIPGNRTSMV LVPIVAAHGL TIPKTSSRAI TSPAGTADTM EVLARVDVGV PEMKEIVAAC
NGCLIWGGHV NLSPADDILI SVERPLCLDT REQMVASIMS KKLAAGSTHL LVDLPLGPSA
KVISPIDAMR LRKLFEFVGD HFGIAVETIT TDGRQPIGNG IGPVLEAQDV MAVLGNDPKA
PADLREKSLR LAGHLLEYDP NLRGGSGYAR ARELLESGAA LKQMQKIIDN QGPTNCRKDL
GTLTTDIVAP RDGVVTGIDN LQLNRLARTA GAPIDKGAGI KLFKKVGDRV EQGEPLYRIY
AFDPSEQELA VSAAEESSGY TVDGVHAFRE QVL