ID   Q98PS3_MYCPU            Unreviewed;       430 AA.
AC   Q98PS3;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   18-JUN-2025, entry version 114.
DE   SubName: Full=THYMIDINE PHOSPHORYLASE (TDRPASE) {ECO:0000313|EMBL:CAC13819.1};
DE            EC=2.4.2.4 {ECO:0000313|EMBL:CAC13819.1};
GN   OrderedLocusNames=MYPU_6460 {ECO:0000313|EMBL:CAC13819.1};
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales;
OC   Metamycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635 {ECO:0000313|Proteomes:UP000000528};
RN   [1] {ECO:0000313|EMBL:CAC13819.1, ECO:0000313|Proteomes:UP000000528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP {ECO:0000313|EMBL:CAC13819.1,
RC   ECO:0000313|Proteomes:UP000000528};
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
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:0000256|ARBA:ARBA00056338}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=thymidine + phosphate = 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:0000256|ARBA:ARBA00048550};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. {ECO:0000256|ARBA:ARBA00006915}.
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DR   EMBL; AL445565; CAC13819.1; -; Genomic_DNA.
DR   PIR; F90592; F90592.
DR   RefSeq; WP_010925447.1; NC_002771.1.
DR   AlphaFoldDB; Q98PS3; -.
DR   STRING; 272635.gene:17577253; -.
DR   KEGG; mpu:MYPU_6460; -.
DR   eggNOG; COG0213; Bacteria.
DR   HOGENOM; CLU_025040_0_1_14; -.
DR   BioCyc; MPUL272635:G1GT6-654-MONOMER; -.
DR   Proteomes; UP000000528; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR   GO; GO:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR   GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
DR   FunFam; 3.40.1030.10:FF:000003; Pyrimidine-nucleoside phosphorylase; 1.
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   Gene3D; 1.20.970.10; Transferase, Pyrimidine Nucleoside Phosphorylase, Chain C; 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; NF004490; PRK05820.1; 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 {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:CAC13819.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000528};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAC13819.1}.
FT   DOMAIN          344..417
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   430 AA;  47821 MW;  E328F7255898F996 CRC64;
     MRIVDLINKK MTGKALTKEE IDFLLDSYLN ESMPDYQMAA FLMAVVFKSM EKEELAHFSL
     KMLQSGKIID LSSIKQIKVD KHSTGGIGDK TTLVIAPIIA ALDLPVAKMS GRGLGHTGGT
     LDKLESIPGF RINLSEEEFI NQVKKINISV ISQSQSLVPL DKKLYALRDV TATVESIPLI
     ASSIMSKKLA TGSDAILLDV KCGNGAFMKD IDRARELAKH MVDIGKVLNK DVVVEITNMD
     RPLGKEIGNK NEVIEAIEAL KDKWSWDFKE LIYSSCINIL LMTKKASTNQ EAKTMIDSVI
     KSGKALEKFY EFVQAQGGDV EILKSKSFWN PKFKLEIKAN SNGYLNIYDA LTFGIVAMKL
     GAGRQTKEEK IDFEAGISLN KKTNDLVKKG DVIFSLYSSK PIDPSLIDEL KNSWKISESK
     VDFKMILDKF
//