Thymidine phosphorylase (P07650)

Identification
Name:Thymidine phosphorylase
Synonyms:
  • TdRPase
Gene Name:deoA
Enzyme Class:
Biological Properties
General Function:Involved in transferase activity, transferring glycosyl groups
Specific Function:The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are 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
Cellular Location:Not Available
SMPDB Pathways:
  • Pyrimidine metabolism PW000942
  • pyrimidine deoxyribonucleosides degradation PW002063
  • salvage pathways of pyrimidine deoxyribonucleotides PW002061
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Deoxyuridine + 1.0Phosphate ↔ 1.0Deoxyribose 1-phosphate + 1.0Uracil
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Phosphate + 1.0Thymidine ↔ 1.0Deoxyribose 1-phosphate + 1.0Thymine
ReactionCard
1.05'-Deoxy-5-fluorouridine+1.0Thumb ↔ 1.05-FU+1.05-Deoxyribose-1-phosphate
1.05'-Deoxy-5-fluorouridine + 1.0Phosphate ↔ 1.05-FU + 1.05-Deoxyribose-1-phosphate
ReactionCard
1.05-FU+1.0Thumb ↔ 1.05-Fluorodeoxyuridine+1.0Thumb
1.05-FU + 1.0Deoxyribose 1-phosphate ↔ 1.05-Fluorodeoxyuridine + 1.0Phosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Deoxyuridine + 1.0Phosphate → 1.0Uracil + 1.0Deoxyribose 1-phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Deoxyribose 1-phosphate + 1.0Thymine → 1.0Phosphate + 1.0Thymidine
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01351Deoxyribose 1-phosphateMetaboCard
ECMDB00012DeoxyuridineMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00273ThymidineMetaboCard
ECMDB00262ThymineMetaboCard
ECMDB00300UracilMetaboCard
GO Classification:
Function
catalytic activity
pyrimidine-nucleoside phosphorylase activity
thymidine phosphorylase activity
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups
Process
cellular aromatic compound metabolic process
cellular metabolic process
cellular nitrogen compound metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside metabolic process
pyrimidine base metabolic process
pyrimidine nucleoside metabolic process
Gene Properties
Blattner:b4382
Gene OrientationClockwise
Centisome Percentage:99.50
Left Sequence End4616252
Right Sequence End4617574
Gene Sequence:
>1323 bp
ATGAGTGAATTTTCCCAGACAGTCCCCGAACTGGTTGCCTGGGCCAGAAAAAATGACTTC
TCCATCTCGCTGCCGGTAGACCGACTCTCTTTTCTGCTGGCGGTTGCCACGCTGAACGGC
GAGCGTCTGGATGGTGAGATGAGTGAAGGCGAGCTGGTGGATGCATTCCGCCATGTGAGT
GATGCGTTTGAGCAAACCAGCGAAACCATCGGCGTGCGCGCCAATAACGCGATCAACGAC
ATGGTGCGTCAACGTCTGCTGAACCGCTTTACCAGCGAGCAGGCGGAAGGGAACGCAATT
TACCGTCTGACGCCGCTCGGCATCGGCATTACTGACTACTACATCCGTCAGCGCGAGTTT
TCTACGCTGCGTCTTTCTATGCAGTTGTCGATTGTGGCGGGTGAGCTCAAACGCGCAGCA
GATGCCGCCGAAGAGGGCGGTGATGAATTTCACTGGCACCGTAATGTCTATGCGCCACTG
AAATATTCGGTAGCAGAAATTTTCGACAGTATCGACCTGACGCAACGTCTGATGGACGAA
CAGCAGCAGCAGGTGAAGGACGATATCGCCCAGTTGCTGAACAAAGACTGGCGGGCGGCG
ATTTCCAGCTGTGAATTGTTGCTTTCGGAAACTTCCGGAACGCTGCGTGAATTGCAGGAT
ACGCTGGAAGCGGCAGGCGACAAATTGCAGGCTAATCTGTTGCGCATTCAGGATGCGACG
ATGACCCATGACGATCTGCATTTCGTCGATCGTCTGGTGTTCGATCTGCAGAGCAAACTC
GATCGTATTATCAGTTGGGGCCAGCAATCCATCGACTTGTGGATTGGCTACGACCGCCAC
GTACACAAATTTATTCGTACCGCGATCGATATGGATAAAAACCGCGTCTTTGCTCAGCGG
TTACGTCAGTCGGTACAAACCTATTTTGATGAGCCGTGGGCGCTAACTTATGCCAATGCC
GATCGTCTGCTGGATATGCGTGACGAAGAGATGGCACTGCGCGATGAAGAAGTGACTGGG
GAACTTCCTGAGGATCTGGAATACGAAGAGTTTAACGAGATCCGCGAACAGCTGGCGGCG
ATCATCGAAGAACAACTTGCCGTGTACAAAACCAGACAAGTGCCGCTGGATCTTGGTCTG
GTGGTACGCGAATATCTGTCACAGTATCCGCGTGCACGTCACTTTGACGTTGCGCGTATT
GTTATTGATCAGGCGGTACGTCTTGGCGTAGCGCAAGCAGATTTCACCGGACTGCCAGCG
AAATGGCAGCCGATTAATGATTACGGAGCCAAGGTACAGGCGCATGTCATCGACAAATAT
TGA
Protein Properties
Pfam Domain Function:
Protein Residues:440
Protein Molecular Weight:47207
Protein Theoretical pI:5
PDB File:2TPT
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Thymidine phosphorylase
MFLAQEIIRKKRDGHALSDEEIRFFINGIRDNTISEGQIAALAMTIFFHDMTMPERVSLT
MAMRDSGTVLDWKSLHLNGPIVDKHSTGGVGDVTSLMLGPMVAACGGYIPMISGRGLGHT
GGTLDKLESIPGFDIFPDDNRFREIIKDVGVAIIGQTSSLAPADKRFYATRDITATVDSI
PLITASILAKKLAEGLDALVMDVKVGSGAFMPTYELSEALAEAIVGVANGAGVRTTALLT
DMNQVLASSAGNAVEVREAVQFLTGEYRNPRLFDVTMALCVEMLISGKLAKDDAEARAKL
QAVLDNGKAAEVFGRMVAAQKGPTDFVENYAKYLPTAMLTKAVYADTEGFVSEMDTRALG
MAVVAMGGGRRQASDTIDYSVGFTDMARLGDQVDGQRPLAVIHAKDENNWQEAAKAVKAA
IKLADKAPESTPTVYRRISE
References
External Links:
ResourceLink
Uniprot ID:P07650
Uniprot Name:TYPH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651446
PDB ID:2TPT
Ecogene ID:EG10219
Ecocyc:EG10219
ColiBase:b4382
Kegg Gene:b4382
EchoBASE ID:EB0215
CCDB:TYPH_ECOLI
BacMap:16132199
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Pugmire, M. J., Cook, W. J., Jasanoff, A., Walter, M. R., Ealick, S. E. (1998). "Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase." J Mol Biol 281:285-299. Pubmed: 9698549
  • Valentin-Hansen, P., Hammer, K., Love Larsen, J. E., Svendsen, I. (1984). "The internal regulated promoter of the deo operon of Escherichia coli K-12." Nucleic Acids Res 12:5211-5224. Pubmed: 6087276
  • Valentin-Hansen, P., Hammer-Jespersen, K., Boetius, F., Svendsen, I. (1984). "Structure and function of the intercistronic regulatory deoC-deoA element of Escherichia coli K-12." EMBO J 3:179-183. Pubmed: 6323164
  • Walter, M. R., Cook, W. J., Cole, L. B., Short, S. A., Koszalka, G. W., Krenitsky, T. A., Ealick, S. E. (1990). "Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution." J Biol Chem 265:14016-14022. Pubmed: 2199449