TYPH_METHO
ID TYPH_METHO Reviewed; 272 AA.
AC P43050;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Thymidine phosphorylase;
DE EC=2.4.2.4;
DE AltName: Full=TdRPase;
DE Flags: Fragment;
GN Name=deoA;
OS Metamycoplasma hominis (Mycoplasma hominis).
OC Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC Metamycoplasma.
OX NCBI_TaxID=2098;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FBG;
RA Schuchart K.;
RL Thesis (1993), Heinrich-Heine University / Duesseldorf, Germany.
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; Z27121; CAA81645.1; -; Genomic_DNA.
DR AlphaFoldDB; P43050; -.
DR SMR; P43050; -.
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 Gene3D; 3.40.1030.10; -; 1.
DR Gene3D; 3.90.1170.30; -; 1.
DR InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR InterPro; IPR035902; Nuc_phospho_transferase.
DR InterPro; IPR036566; PYNP-like_C_sf.
DR InterPro; IPR013102; PYNP_C.
DR InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR PANTHER; PTHR10515; PTHR10515; 1.
DR Pfam; PF00591; Glycos_transf_3; 1.
DR Pfam; PF07831; PYNP_C; 1.
DR SMART; SM00941; PYNP_C; 1.
DR SUPFAM; SSF52418; SSF52418; 1.
DR SUPFAM; SSF54680; SSF54680; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Transferase.
FT CHAIN <1..272
FT /note="Thymidine phosphorylase"
FT /id="PRO_0000059079"
FT NON_TER 1
SQ SEQUENCE 272 AA; 30411 MW; B06BFB86FB6008EB CRC64;
DKKIYALRDV TGTVQSIPLI ASSIMSKKLA TGSNCILLDV KCGNGAFMKD INEAKKLGKL
MIEIGKKLNR KIAVEITNMQ QPLGKTIGNK IEVLEAIDTL NGHGPKDFTE IIYSSGSTLL
VLAQKAKDEV EARKMIDEVI NNKKAYNKFL EWISRQGGNI KVFEKDSKWF NPQYKQEIIA
SQSGYLKIKS RIDFGLVAMK LGAGRSKKED SIDYEAGIYL NKSSNEYVNK GDVLFTMYSS
KPINPELQKE LLSAIEFSES KHDIQTVFAK LM