ID   TYPH_KLEP7              Reviewed;         440 AA.
AC   A6THZ7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=KPN78578_47570; ORFNames=KPN_04838;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000647; ABR80181.1; -; Genomic_DNA.
DR   RefSeq; WP_002887787.1; NC_009648.1.
DR   AlphaFoldDB; A6THZ7; -.
DR   SMR; A6THZ7; -.
DR   STRING; 272620.KPN_04838; -.
DR   jPOST; A6THZ7; -.
DR   EnsemblBacteria; ABR80181; ABR80181; KPN_04838.
DR   KEGG; kpn:KPN_04838; -.
DR   HOGENOM; CLU_025040_0_1_6; -.
DR   OMA; DVWRRMI; -.
DR   UniPathway; UPA00578; UER00638.
DR   Proteomes; UP000000265; Chromosome.
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; IEA:UniProtKB-UniRule.
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; -; 1.
DR   Gene3D; 3.90.1170.30; -; 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   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   PIRSF; PIRSF000478; TP_PyNP; 1.
DR   SMART; SM00941; PYNP_C; 1.
DR   SUPFAM; SSF47648; SSF47648; 1.
DR   SUPFAM; SSF52418; SSF52418; 1.
DR   SUPFAM; SSF54680; SSF54680; 1.
DR   TIGRFAMs; TIGR02643; T_phosphoryl; 1.
DR   TIGRFAMs; TIGR02644; Y_phosphoryl; 1.
DR   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..440
FT                   /note="Thymidine phosphorylase"
FT                   /id="PRO_1000069663"
SQ   SEQUENCE   440 AA;  47045 MW;  3FA3DBB57876B640 CRC64;
     MFLAQEIIRK KRDGQALSDE EIRFFINGIR DNTISEGQIA ALAMTIFFHD MSMPERVSLT
     MAMRDSGTVL DWKSLNLNGP IVDKHSTGGV GDVTSLMLGP MVAACGGYVP MISGRGLGHT
     GGTLDKLEAI PGFDIFPDDN RFREIIKDVG VAIIGQTSSL APADKRFYAT RDITATVDSI
     PLITASILAK KLAEGLDALV MDVKVGSGAF MPTYELSAAL AEAIVGVANG AGVRTTALLT
     DMNQVLASSA GNAVEVREAV QFLTGEYRNP RLFDVTMALC VEMLISGKLA ADDAEARAKL
     QAVLDNGKAA EVFGRMVAAQ KGPSDFVENY ANYLPTAMLS KAVYADTEGF ISAMDTRALG
     MAVVSMGGGR RQASDTIDYS VGFTEMARLG DRVDGQRPLA VIHAKDENSW QEAAKAVKAA
     IKLDDKAPEI TPTVYRRITE