Q8XB35 (TYPH_ECO57) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 74.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Thymidine phosphorylase EC=2.4.2.4 Alternative name(s): TdRPase | ||||
| Gene names |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 440 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| 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 By similarity. HAMAP-Rule MF_01628 |
| Catalytic activity | Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate. HAMAP-Rule MF_01628 |
| Pathway | Pyrimidine metabolism; dTMP biosynthesis via salvage pathway; dTMP from thymine: step 1/2. HAMAP-Rule MF_01628 |
| Subunit structure | Homodimer By similarity. HAMAP-Rule MF_01628 |
| Sequence similarities | Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Glycosyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | pyrimidine nucleobase metabolic process Inferred from electronic annotation. Source: InterPro thymidine metabolic processInferred from electronic annotation. Source: HAMAP |
| Molecular_function | phosphorylase activity Inferred from electronic annotation. Source: InterPro pyrimidine-nucleoside phosphorylase activityInferred from electronic annotation. Source: InterPro thymidine phosphorylase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 440 | 440 | Thymidine phosphorylase HAMAP-Rule MF_01628 | PRO_0000059055 | |||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG59563.1. BA000007 Genomic DNA. Translation: BAB38764.1. |
| PIR | E91296. G86137. |
| RefSeq | NP_290996.1. NC_002655.2. NP_313368.1. NC_002695.1. |
3D structure databases | |
| ProteinModelPortal | Q8XB35. |
| SMR | Q8XB35. Positions 1-440. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 155864.Z5984. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAG59563; AAG59563; Z5984. BAB38764; BAB38764; BAB38764. |
| GeneID | 913506. 959672. |
| KEGG | ece:Z5984. ecs:ECs5341. |
| PATRIC | 18360340. VBIEscCol44059_5300. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0213. |
| HOGENOM | HOG000047313. |
| KO | K00758. |
| OMA | LMAIYFR. |
| ProtClustDB | PRK05820. |
Enzyme and pathway databases | |
| BioCyc | ECOL386585:GJFA-5353-MONOMER. |
| UniPathway | UPA00578; UER00638. |
Family and domain databases | |
| Gene3D | 3.40.1030.10. 1 hit. 3.90.1170.30. 1 hit. |
| HAMAP | MF_01628. Thymid_phosp. |
| InterPro | IPR000312. Glycosyl_Trfase_fam3. IPR017459. Glycosyl_Trfase_fam3_N_dom. IPR013102. PYNP_C. IPR018090. Pyrmidine_PPas_bac/euk. IPR000053. Pyrmidine_PPase. IPR017872. Pyrmidine_PPase_CS. IPR013465. Thymidine_Pase. [Graphical view] |
| PANTHER | PTHR10515. PTHR10515. 1 hit. |
| Pfam | PF02885. Glycos_trans_3N. 1 hit. PF00591. Glycos_transf_3. 1 hit. PF07831. PYNP_C. 1 hit. [Graphical view] |
| PIRSF | PIRSF000478. TP_PyNP. 1 hit. |
| SMART | SM00941. PYNP_C. 1 hit. [Graphical view] |
| SUPFAM | SSF47648. Glyco_trans_3. 1 hit. SSF52418. Glyco_trans_3. 1 hit. SSF54680. PYNP_C. 1 hit. |
| TIGRFAMs | TIGR02643. T_phosphoryl. 1 hit. TIGR02644. Y_phosphoryl. 1 hit. |
| PROSITE | PS00647. THYMID_PHOSPHORYLASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TYPH_ECO57 | ||||||||
| Accession | Primary (citable) accession number: Q8XB35 Secondary accession number(s): Q8X2H2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
