thymidine phosphorylase catalyzes the reversible phosphorolysis of pyrimidine nucleosides and is involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis
thymidine phosphorylase; Thymidine phosphorylase (alternate name: pyrimidine phosphorylase), EC 2.4.2.4, is the designation for the enzyme of E. coli and other Proteobacteria involved in (deoxy)nucleotide degradation. It often occurs in an operon with a deoxyribose-phosphate aldolase, phosphopentomutase and a purine nucleoside phosphorylase. In many other lineages, the corresponding enzyme is designated pyrimidine-nucleoside phosphorylase (EC 2.4.2.2); the naming convention imposed by this model represents standard literature practice. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 131691 Cd Length: 437 Bit Score: 658.74 E-value: 0e+00
Glycosyl transferase family, a/b domain; This family includes anthranilate ...
79-310
2.70e-45
Glycosyl transferase family, a/b domain; This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate.
Pssm-ID: 459860 [Multi-domain] Cd Length: 253 Bit Score: 157.84 E-value: 2.70e-45
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal ...
350-424
6.22e-21
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal end of the large alpha/beta domain making up various pyrimidine nucleoside phosphorylases. It has slightly different conformations in different members of this family. For example, in pyrimidine nucleoside phosphorylase (PYNP) there is an added three-stranded anti-parallel beta sheet as compared to other members of the family, such as E. coli thymidine phosphorylase (TP). The domain contains an alpha/ beta hammerhead fold and residues in this domain seem to be important in formation of the homodimer.
Pssm-ID: 214925 [Multi-domain] Cd Length: 75 Bit Score: 86.05 E-value: 6.22e-21
thymidine phosphorylase; Thymidine phosphorylase (alternate name: pyrimidine phosphorylase), EC 2.4.2.4, is the designation for the enzyme of E. coli and other Proteobacteria involved in (deoxy)nucleotide degradation. It often occurs in an operon with a deoxyribose-phosphate aldolase, phosphopentomutase and a purine nucleoside phosphorylase. In many other lineages, the corresponding enzyme is designated pyrimidine-nucleoside phosphorylase (EC 2.4.2.2); the naming convention imposed by this model represents standard literature practice. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 131691 Cd Length: 437 Bit Score: 658.74 E-value: 0e+00
pyrimidine-nucleoside phosphorylase; In general, members of this protein family are designated ...
4-412
0e+00
pyrimidine-nucleoside phosphorylase; In general, members of this protein family are designated pyrimidine-nucleoside phosphorylase, enzyme family EC 2.4.2.2, as in Bacillus subtilis, and more narrowly as the enzyme family EC 2.4.2.4, thymidine phosphorylase (alternate name: pyrimidine phosphorylase), as in Escherichia coli. The set of proteins encompassed by this model is designated subfamily rather than equivalog for this reason; the protein name from this model should be used when TIGR02643 does not score above trusted cutoff. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 274244 [Multi-domain] Cd Length: 405 Bit Score: 538.74 E-value: 0e+00
Glycosyl transferase family, a/b domain; This family includes anthranilate ...
79-310
2.70e-45
Glycosyl transferase family, a/b domain; This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate.
Pssm-ID: 459860 [Multi-domain] Cd Length: 253 Bit Score: 157.84 E-value: 2.70e-45
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal ...
350-424
6.22e-21
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal end of the large alpha/beta domain making up various pyrimidine nucleoside phosphorylases. It has slightly different conformations in different members of this family. For example, in pyrimidine nucleoside phosphorylase (PYNP) there is an added three-stranded anti-parallel beta sheet as compared to other members of the family, such as E. coli thymidine phosphorylase (TP). The domain contains an alpha/ beta hammerhead fold and residues in this domain seem to be important in formation of the homodimer.
Pssm-ID: 214925 [Multi-domain] Cd Length: 75 Bit Score: 86.05 E-value: 6.22e-21
Glycosyl transferase family, helical bundle domain; This family includes anthranilate ...
5-67
5.07e-18
Glycosyl transferase family, helical bundle domain; This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate.
Pssm-ID: 460737 [Multi-domain] Cd Length: 63 Bit Score: 77.80 E-value: 5.07e-18
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal ...
350-421
5.58e-18
Pyrimidine nucleoside phosphorylase C-terminal domain; This domain is found at the C-terminal end of the large alpha/beta domain making up various pyrimidine nucleoside phosphorylases. It has slightly different conformations in different members of this family. For example, in pyrimidine nucleoside phosphorylase (PYNP) there is an added three-stranded anti-parallel beta sheet as compared to other members of the family, such as E. coli thymidine phosphorylase (TP). The domain contains an alpha/ beta hammerhead fold and residues in this domain seem to be important in formation of the homodimer.
Pssm-ID: 429685 [Multi-domain] Cd Length: 74 Bit Score: 78.00 E-value: 5.58e-18
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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