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P19663 - TYPH_LACRH
- Names & Taxonomy
- Subcellular locationSubcell. location
- Pathology & BiotechPathol./Biotech
- PTM / Processing
- Family & Domains
- Entry information
- BLAST>sp|P19663|TYPH_LACRH Thymidine phosphorylase (Fragment) OS=Lactobacillus rhamnosus GN=deoA PE=1 SV=1 MVKIGINEFGRIGRLAFRRIYEL
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Select a section on the left to see content.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.Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate.
Recommended name:Thymidine phosphorylase (EC:184.108.40.206)Alternative name(s):TdRPaseName:deoA
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Source: InterPro
- thymidine phosphorylase activity Source: UniProtKB-EC
Lactobacillus rhamnosus 47715 [NCBI] cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus
Feature key Position(s) Length Description Graphical view Feature identifier Actions 1 – ›23 ›23 Thymidine phosphorylase PRO_0000059077 Add
<p>Provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureiHomodimer.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniBelongs to the thymidine/pyrimidine-nucleoside phosphorylase family.Curated
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families<br/><a href='/database/29'>More..</a>Gene3Di 220.127.116.110. 1 hit. IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
Pfam protein domain database<br/><a href='/database/73'>More..</a>Pfami PF00044. Gp_dh_N. 1 hit.
<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusi: Fragment.Length:23Mass (Da):2,752Last modified:February 1, 1991 - v1<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8705C9C4D82C1AD7
Feature key Position(s) Length Description Graphical view Feature identifier Actions <p>Is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.</p><p><a href='../manual/non_ter' target='_top'>More...</a></p>Non-terminal residuei 23 – 23 1
Protein sequence database of the Protein Information Resource<br/><a href='/database/78'>More..</a>PIRi S11384.
Protein sequence database of the Protein Information Resource<br/><a href='/database/78'>More..</a> PIRi S11384.
3D structure databases
Database of comparative protein structure models<br/><a href='/database/63'>More..</a> ModBasei Search... Search...
Protocols and materials databases
Structural Biology Knowledgebase Search...
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families<br/><a href='/database/29'>More..</a> Gene3Di 18.104.22.1680. 1 hit. IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
[Graphical view ]
Pfam protein domain database<br/><a href='/database/73'>More..</a> Pfami PF00044. Gp_dh_N. 1 hit.
[Graphical view ]
- "Purification and characterization of uridine and thymidine phosphorylase from Lactobacillus casei."
Avraham Y., Grossowicz N., Yashphe J.
Biochim. Biophys. Acta 1040:287-293(1990) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, SUBUNIT.Strain: ATCC 7469 / DSM 20021 / NCDO 243 / NCIB 6375.
TYPH_LACRH P19663Primary (citable) accession number: P19663 Integrated into UniProtKB/Swiss-Prot: February 1, 1991 Last sequence update: February 1, 1991 Last modified: October 1, 2014 This is version 72 of the entry and version 1 of the sequence. [Complete history] Reviewed (UniProtKB/Swiss-Prot) Annotation program Prokaryotic Protein Annotation Program
- SIMILARITY commentsIndex of protein domains and families
External DataDasty 3