ID   Q6MGR7_BDEBA            Unreviewed;       439 AA.
AC   Q6MGR7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   18-JUN-2025, entry version 108.
DE   RecName: Full=thymidine phosphorylase {ECO:0000256|ARBA:ARBA00011892};
DE            EC=2.4.2.4 {ECO:0000256|ARBA:ARBA00011892};
GN   Name=pdp {ECO:0000313|EMBL:CAE81212.1};
GN   OrderedLocusNames=Bd3855 {ECO:0000313|EMBL:CAE81212.1};
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia;
OC   Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462 {ECO:0000313|EMBL:CAE81212.1, ECO:0000313|Proteomes:UP000008080};
RN   [1] {ECO:0000313|EMBL:CAE81212.1, ECO:0000313|Proteomes:UP000008080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100
RC   {ECO:0000313|Proteomes:UP000008080};
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX842656; CAE81212.1; -; Genomic_DNA.
DR   RefSeq; WP_011166155.1; NC_005363.1.
DR   AlphaFoldDB; Q6MGR7; -.
DR   STRING; 264462.Bd3855; -.
DR   GeneID; 93014624; -.
DR   KEGG; bba:Bd3855; -.
DR   eggNOG; COG0213; Bacteria.
DR   HOGENOM; CLU_025040_0_1_7; -.
DR   Proteomes; UP000008080; 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:CAE81212.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008080};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAE81212.1}.
FT   DOMAIN          350..424
FT                   /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00941"
SQ   SEQUENCE   439 AA;  47286 MW;  A67E5CEE98809401 CRC64;
     MAFLPAEIIK IKRNGGELKY EEISEFILGY ARGQIPDYQM SALLMAIFFR GMNTEETLSL
     TKAMLHSGEV VDFSSVKEFK VDKHSTGGVG DKTSLILGPI VAAAGIPVPM ISGRGLGHTG
     GTLDKLESIP GFNTQKSLPE FIELVHKHKI CFIGQTKEIC PADKKIYALR DVTATVESLP
     LICASIMSKK MAEGIDGLVL DVKFGSGAFM KTPVLAEELA VNLMAIAKGY GKKVTALLTN
     MDQPLGRYAG NSVEVEECVA IMKNEKFMGP AGYDLYEDTR ELSLRLSAHM LLLAGVGKNE
     EESYKIAEDI LVSGKAMAKF EELCSIHGGN LKALPKPKHS IEVKSDKAGW VGGFHTESIG
     VAGILIKAGR AQTTDIIAPT AGIEFHVKVG DEVNVGDTVF TLHGDDKDLL QSALPMLRSA
     MTISLQKTSK PSLILKTLS
//