ID   TYPH_MYCPI              Reviewed;         419 AA.
AC   P47717;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Thymidine phosphorylase;
DE            EC=2.4.2.4;
DE   AltName: Full=TdRPase;
GN   Name=deoA;
OS   Mycoplasmoides pirum (Mycoplasma pirum).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=2122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BER;
RX   PubMed=8349569; DOI=10.1128/jb.175.16.5281-5285.1993;
RA   Tham T.N., Ferris S., Kovacic R., Montagnier L., Blanchard A.;
RT   "Identification of Mycoplasma pirum genes involved in the salvage pathways
RT   for nucleosides.";
RL   J. Bacteriol. 175:5281-5285(1993).
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   -!- 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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. {ECO:0000305}.
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DR   EMBL; L13289; AAA25432.1; -; Genomic_DNA.
DR   PIR; C53312; C53312.
DR   AlphaFoldDB; P47717; -.
DR   SMR; P47717; -.
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; ISS:CAFA.
DR   GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR   GO; GO:0006213; P:pyrimidine nucleoside metabolic process; ISS:CAFA.
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; Transferase.
FT   CHAIN           1..419
FT                   /note="Thymidine phosphorylase"
FT                   /id="PRO_0000059080"
SQ   SEQUENCE   419 AA;  47279 MW;  C1620F2EF33929E3 CRC64;
     MNIIEIIELK KNKKKLSQDQ INFCISGLVN KSIPDYQISA LLMAIWFNGL DDNELYFLTK
     AMIDSGKIYK FHPEYKKILI DKHSTGGIGD KVSIALRPIL VSFDLGVAKL SGRGLGFTGG
     TIDKLESINV NTDIDLKNSK KILNIANMFI VGQTNDIVPA DKLLYALRDV TGTVDSLPLI
     AASILSKKFA LESDYIFIDI KYGQGAFCHD IETAKKISNI MKNLAKKFKR KVYFVLSDMN
     EVLGNTVGNA IEVKEAIDFL KNNSDVGTYF KKLMFDLVTL ILLKTKKCKT KKEAKEKINY
     VLENKIAFNN FCNWIELQNG NIAKIKNDTF FKPKYWTNIA AWKSGKISYK SIIELAEIGV
     DLGSGRRKKE DKIDFQAGIY LHAKSNEKIK IKDKILTLYS SKPIKQDLID KAKKIIKIS
//