ID TYPH_VIBCH Reviewed; 448 AA. AC Q9KPL8; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 2. DT 13-SEP-2023, entry version 125. DE RecName: Full=Thymidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01628}; DE EC=2.4.2.4 {ECO:0000255|HAMAP-Rule:MF_01628}; DE AltName: Full=TdRPase {ECO:0000255|HAMAP-Rule:MF_01628}; GN Name=deoA {ECO:0000255|HAMAP-Rule:MF_01628}; GN OrderedLocusNames=VC_2349; OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=243277; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39315 / El Tor Inaba N16961; RX PubMed=10952301; DOI=10.1038/35020000; RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A., RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.; RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio RT cholerae."; RL Nature 406:477-483(2000). CC -!- FUNCTION: The enzymes which catalyze the reversible phosphorolysis of CC pyrimidine nucleosides are involved in the degradation of these CC compounds and in their utilization as carbon and energy sources, or in CC the rescue of pyrimidine bases for nucleotide synthesis. CC {ECO:0000255|HAMAP-Rule:MF_01628}. 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_01628}; CC -!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway; CC dTMP from thymine: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01628}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01628}. CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside CC phosphorylase family. {ECO:0000255|HAMAP-Rule:MF_01628}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF95492.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AE003852; AAF95492.1; ALT_INIT; Genomic_DNA. DR PIR; E82087; E82087. DR RefSeq; NP_231979.2; NC_002505.1. DR RefSeq; WP_000059246.1; NZ_LT906614.1. DR AlphaFoldDB; Q9KPL8; -. DR SMR; Q9KPL8; -. DR STRING; 243277.VC_2349; -. DR DNASU; 2613145; -. DR EnsemblBacteria; AAF95492; AAF95492; VC_2349. DR KEGG; vch:VC_2349; -. DR PATRIC; fig|243277.26.peg.2236; -. DR eggNOG; COG0213; Bacteria. DR HOGENOM; CLU_025040_0_1_6; -. DR OMA; DVWRRMI; -. DR UniPathway; UPA00578; UER00638. DR Proteomes; UP000000584; Chromosome 1. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro. DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:InterPro. DR GO; GO:0009032; F:thymidine phosphorylase activity; IBA:GO_Central. DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro. DR GO; GO:0046104; P:thymidine metabolic process; IEA:UniProtKB-UniRule. 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 HAMAP; MF_01628; Thymid_phosp; 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 InterPro; IPR013465; Thymidine_Pase. DR NCBIfam; TIGR02643; T_phosphoryl; 1. 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; Reference proteome; Transferase. FT CHAIN 1..448 FT /note="Thymidine phosphorylase" FT /id="PRO_0000059070" SQ SEQUENCE 448 AA; 47843 MW; 7955ABB95C401F62 CRC64; MSLSQAKYLP QEIIRRKRDG EVLTNDEINF FIQGVANNTV SEGQIAAFAM AIFFREMTMP ERIALTCAMR DSGMVIDWSH MNFDGPIVDK HSTGGVGDVT SLMLGPMVAA CGGYVPMISG RGLGHTGGTL DKLEAIPGYN ITPTNDVFGK VTKQAGVAII GQTGDLAPAD KRVYATRDIT ATVDNISLIT ASILSKKLAA GLESLVMDVK VGSGAFMPTY EASEELAKSI VAVANGAGTN TTAILTDMNQ VLASSAGNAV EVREAVRFLT GEYRNPRLLE VTMASCAEML VLGKLAKDTA QAREKLQAVL DNGQAADRFG KMVAGLGGPS DFVENYDKYL AKAEIIRPVY AQQSGVISAM DTRAIGMAVV GMGGGRRVAT DRIDYAVGFD QFIRLGEIAD SNKPLAMIHA RNEEQWQQAA NALQSAIKVG GDYLPTPDVY RQIRAQDV //