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Thymidine phosphorylase (EC 2.4.2.4) catalyzes the reversible phosphorolysis of thymidine, deoxyuridine and their analogues to their respective bases and 2-deoxyribose 1-phosphate. This enzyme regulates the availability of thymidine and is therefore essential to nucleic acid metabolism.

In Escherichia coli (gene deoA), the enzyme is a dimer of identical subunits of about 48 Kd [1]. In humans it was first identified as platelet-derived endothelial cell growth factor (PD-ECGF) before being recognized [2] as thymidine phosphorylase.

Bacterial pyrimidine-nucleoside phosphorylase (EC 2.4.2.2) (gene pdp) [3] is an enzyme evolutionary and structurally related to thymidine phosphorylase.

As a signature pattern for these enzymes, we selected a well conserved region of 19 residues located in the N-terminal part of these proteins.

April 2006 / Pattern revised.

PROSITE method (with tools and information) covered by this documentation:

THYMID_PHOSPHORYLASE, PS00647; Thymidine and pyrimidine-nucleoside phosphorylases signature  (PATTERN)

Consensus pattern: [SA]-[GS]-R-[GA]-[LIV]-x(2)-[TAP]-[GAS]-G-T-x-D-x-[LIVMF]-[EDS] Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00647 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00647 • Scan Swiss-Prot/TrEMBL entries against PS00647 • view ligand binding statistics

Matching PDB structures: 1AZY 1BRW 1OTP 1TPT ... [ALL]

1	Authors	Walter M.R., Cook W.J., Cole L.B., Short S.A., Koszalka G.W., Krenitsky T.A., Ealick S.E.
	Title	Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution.
	Source	J. Biol. Chem. 265:14016-14022(1990).
	PubMed ID	2199449

2	Authors	Furukawa T., Yoshimura A., Sumizawa T., Haraguchi M., Akiyama S.-I., Fukui K., Ishizawa M., Yamada Y.
	Title	Angiogenic factor.
	Source	Nature 356:668-668(1992).
	PubMed ID	1570012
	DOI	10.1038/356668a0

3	Authors	Saxild H.H., Andersen L.N., Hammer K.
	Title	Dra-nupC-pdp operon of Bacillus subtilis: nucleotide sequence, induction by deoxyribonucleosides, and transcriptional regulation by the deoR-encoded DeoR repressor protein.
	Source	J. Bacteriol. 178:424-434(1996).
	PubMed ID	8550462

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