TYPH_RHOPS
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 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=RPD_1443;
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; 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 EnsemblBacteria; ABE38680; ABE38680; RPD_1443.
DR KEGG; rpd:RPD_1443; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_6_0_5; -.
DR OMA; QMVASIM; -.
DR OrthoDB; 1724909at2; -.
DR BioCyc; RPAL316057:RPD_RS07290-MON; -.
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; 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_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