ID Q18B84_CLOD6 Unreviewed; 446 AA. AC Q18B84; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 25-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00014680}; DE EC=2.4.2.2 {ECO:0000256|ARBA:ARBA00011889}; GN Name=pdp {ECO:0000313|EMBL:CAJ68079.1}; GN OrderedLocusNames=CD630_12250 {ECO:0000313|EMBL:CAJ68079.1}; OS Clostridioides difficile (strain 630) (Peptoclostridium difficile). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae; OC Clostridioides. OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ68079.1, ECO:0000313|Proteomes:UP000001978}; RN [1] {ECO:0000313|EMBL:CAJ68079.1, ECO:0000313|Proteomes:UP000001978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=630 {ECO:0000313|EMBL:CAJ68079.1, RC ECO:0000313|Proteomes:UP000001978}; RX PubMed=16804543; DOI=10.1038/ng1830; RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A., RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K., RA Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L., RA Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.; RT "The multidrug-resistant human pathogen Clostridium difficile has a highly RT mobile, mosaic genome."; RL Nat. Genet. 38:779-786(2006). CC -!- FUNCTION: Catalyzes phosphorolysis of the pyrimidine nucleosides CC uridine, thymidine and 2'-deoxyuridine with the formation of the CC corresponding pyrimidine base and ribose-1-phosphate. CC {ECO:0000256|ARBA:ARBA00003877}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2'-deoxyuridine + phosphate = 2-deoxy-alpha-D-ribose 1- CC phosphate + uracil; Xref=Rhea:RHEA:22824, ChEBI:CHEBI:16450, CC ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2; CC Evidence={ECO:0000256|ARBA:ARBA00001066}; 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=2.4.2.2; CC Evidence={ECO:0000256|ARBA:ARBA00000722}; CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil; CC Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.2; CC Evidence={ECO:0000256|ARBA:ARBA00001004}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside CC phosphorylase family. {ECO:0000256|ARBA:ARBA00006915}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AM180355; CAJ68079.1; -; Genomic_DNA. DR RefSeq; YP_001087718.1; NC_009089.1. DR AlphaFoldDB; Q18B84; -. DR STRING; 272563.CD630_12250; -. DR EnsemblBacteria; CAJ68079; CAJ68079; CD630_12250. DR KEGG; cdf:CD630_12250; -. DR PATRIC; fig|272563.8.peg.1284; -. DR eggNOG; COG0213; Bacteria. DR OrthoDB; 9763887at2; -. DR PhylomeDB; Q18B84; -. DR BioCyc; PDIF272563:G12WB-1356-MONOMER; -. DR Proteomes; UP000001978; Chromosome. DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro. DR GO; GO:0047847; F:deoxyuridine phosphorylase activity; IEA:RHEA. DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009032; F:thymidine phosphorylase activity; IEA:RHEA. DR GO; GO:0004850; F:uridine phosphorylase activity; IEA:RHEA. 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; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1. DR Gene3D; 3.90.1170.30; Pyrimidine nucleoside phosphorylase-like, C-terminal domain; 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; IPR018090; Pyrmidine_PPas_bac/euk. DR InterPro; IPR017872; Pyrmidine_PPase_CS. DR InterPro; IPR000053; Thymidine/pyrmidine_PPase. DR NCBIfam; TIGR02644; Y_phosphoryl; 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 PIRSF; PIRSF000478; TP_PyNP; 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 {ECO:0000256|ARBA:ARBA00022676, KW ECO:0000313|EMBL:CAJ68079.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001978}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAJ68079.1}. FT DOMAIN 350..424 FT /note="Pyrimidine nucleoside phosphorylase C-terminal" FT /evidence="ECO:0000259|SMART:SM00941" SQ SEQUENCE 446 AA; 48738 MW; 286324FA5E6E1A2B CRC64; MEISIMRMYD IIKKKRDNLE LSKKEINYFI ENYSKGDIPD YQASALLMSI YLNKMNKQET VHLTEAMMNS GDMINLSEID GIKVDKHSTG GVGDKTTIAL IPLVASCGAP VAKMSGRGLG HTGGTIDKLE SIPGFSTEME ISKFIDSVNK SKIAVCGQSA KVAIADKKIY ALRDVTATVD NISLISSSVM SKKLASGADA IVLDVKTGDG AFMKTLEESF ELAKSMVDIG TGMNRDTIGI VTDMDEPLGF AVGNSLEVIE AIETLKGNGP KDLVELCEVL GAYMLVLSKV AHDFEDGVEK IRESIKSGTA IQKLKEFIEN QGGNKDVVDD YSLFKKSKYK YPVKSTKSGY ISKIKAEDVG VSAMILGAGR ETKDDILDLS AGIILEKKVG DYVNEGEVLA YMYYNDEQKL SLAKGRFIDS YSIVDSKIEK NKLIYGIVTK EEIKKF //