ID   TYPH_MYCGE              Reviewed;         421 AA.
AC   P47297; Q49312;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Thymidine phosphorylase;
DE            EC=2.4.2.4;
DE   AltName: Full=TdRPase;
GN   Name=deoA; OrderedLocusNames=MG051;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-421.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA   Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT   "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL   J. Bacteriol. 175:7918-7930(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; L43967; AAC71267.1; -; Genomic_DNA.
DR   EMBL; U02191; AAD12476.1; -; Genomic_DNA.
DR   PIR; F64205; F64205.
DR   RefSeq; WP_009885713.1; NZ_AAGX01000003.1.
DR   AlphaFoldDB; P47297; -.
DR   SMR; P47297; -.
DR   STRING; 243273.MG_051; -.
DR   KEGG; mge:MG_051; -.
DR   eggNOG; COG0213; Bacteria.
DR   HOGENOM; CLU_025040_0_1_14; -.
DR   InParanoid; P47297; -.
DR   OrthoDB; 9763887at2; -.
DR   BioCyc; MGEN243273:G1GJ2-52-MONOMER; -.
DR   Proteomes; UP000000807; Chromosome.
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: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; Reference proteome; Transferase.
FT   CHAIN           1..421
FT                   /note="Thymidine phosphorylase"
FT                   /id="PRO_0000059078"
FT   CONFLICT        392
FT                   /note="V -> I (in Ref. 2; AAD12476)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   421 AA;  46355 MW;  649CD517CD6E5E62 CRC64;
     MNIINLINKK QRGKALNLAE INWFVNAVLN KTIADYQITA FLMAIWFKGM NPNELFLLTK
     AMVDTGEIIK FNHHGKISVD KHSTGGIGDK VSLALVPILT SLGFSVAKLS GRGLGYTGGT
     IDKLEAVGVK TELTDQQAQA CLDKNDCFII GQSKDIAPVD KVLYGLRDIT GTVDSLPLIA
     SSIMSKKLAV MNEYIFIDLK YGKGAFCKTK KIANELAKLM QSIAKSFKRK LSVKLSDMNQ
     VLGKAVGNVI EVNEAVNFLK QDLDQVGQDF IDLMQTIVIN ILLETKQAKT KQKAIELYQD
     VLTSKKAWNR FLSFIESQGG NVELFTQKEG FFKPKYKASI KAEKSGILHF TDPIDLAKIG
     INLGAGRMKK TDQIDPMAGL FLMKKDNESV AVGDTVLNLY SSSPISNEYI SAAQKTIIIN
     K
//