{PDOC00557}
{PS00647; THYMID_PHOSPHORYLASE}
{BEGIN}
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* Thymidine and pyrimidine-nucleoside phosphorylases signature *
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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.

-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.
-Last update: April 2006 / Pattern revised.

[ 1] Walter M.R., Cook W.J., Cole L.B., Short S.A., Koszalka G.W.,
     Krenitsky T.A., Ealick S.E.
     "Three-dimensional structure of thymidine phosphorylase from
     Escherichia coli at 2.8 A resolution."
     J. Biol. Chem. 265:14016-14022(1990).
     PubMed=2199449
[ 2] Furukawa T., Yoshimura A., Sumizawa T., Haraguchi M., Akiyama S.-I.,
     Fukui K., Ishizawa M., Yamada Y.
     "Angiogenic factor."
     Nature 356:668-668(1992).
     PubMed=1570012; DOI=10.1038/356668a0
[ 3] Saxild H.H., Andersen L.N., Hammer K.
     "Dra-nupC-pdp operon of Bacillus subtilis: nucleotide sequence,
     induction by deoxyribonucleosides, and transcriptional regulation by
     the deoR-encoded DeoR repressor protein."
     J. Bacteriol. 178:424-434(1996).
     PubMed=8550462

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