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P07650 (TYPH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thymidine phosphorylase

EC=2.4.2.4
Alternative name(s):
TdRPase
Gene names
Name:deoA
Synonyms:tpp, ttg
Ordered Locus Names:b4382, JW4345
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. 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.

Sequence similarities

Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ygjKP425921EBI-909674,EBI-1121018

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440Thymidine phosphorylase HAMAP-Rule MF_01628
PRO_0000059054

Secondary structure

.................................................................... 440
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07650 [UniParc].

Last modified February 1, 1995. Version 3.
Checksum: 1DB3083C9275D2ED

FASTA44047,207
        10         20         30         40         50         60 
MFLAQEIIRK KRDGHALSDE EIRFFINGIR DNTISEGQIA ALAMTIFFHD MTMPERVSLT 

        70         80         90        100        110        120 
MAMRDSGTVL DWKSLHLNGP IVDKHSTGGV GDVTSLMLGP MVAACGGYIP MISGRGLGHT 

       130        140        150        160        170        180 
GGTLDKLESI PGFDIFPDDN RFREIIKDVG VAIIGQTSSL APADKRFYAT RDITATVDSI 

       190        200        210        220        230        240 
PLITASILAK KLAEGLDALV MDVKVGSGAF MPTYELSEAL AEAIVGVANG AGVRTTALLT 

       250        260        270        280        290        300 
DMNQVLASSA GNAVEVREAV QFLTGEYRNP RLFDVTMALC VEMLISGKLA KDDAEARAKL 

       310        320        330        340        350        360 
QAVLDNGKAA EVFGRMVAAQ KGPTDFVENY AKYLPTAMLT KAVYADTEGF VSEMDTRALG 

       370        380        390        400        410        420 
MAVVAMGGGR RQASDTIDYS VGFTDMARLG DQVDGQRPLA VIHAKDENNW QEAAKAVKAA 

       430        440 
IKLADKAPES TPTVYRRISE 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, 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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The internal regulated promoter of the deo operon of Escherichia coli K-12."
Valentin-Hansen P., Hammer K., Larsen J.E.L., Svendsen I.
Nucleic Acids Res. 12:5211-5224(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-440.
Strain: K12.
[5]"Structure and function of the intercistronic regulatory deoC-deoA element of Escherichia coli K-12."
Valentin-Hansen P., Hammer-Jespersen K., Boetius F., Svendsen I.
EMBO J. 3:179-183(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
[6]"Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8-A resolution."
Walter M.R., Cook W.J., Cole L.B., Short S.A., Koszalka G.W., Krenitsky T.A., Ealick S.E.
J. Biol. Chem. 265:14016-14022(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[7]"Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase."
Pugmire M.J., Cook W.J., Jasanoff A., Walter M.R., Ealick S.E.
J. Mol. Biol. 281:285-299(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14003 Genomic DNA. Translation: AAA97278.1.
U00096 Genomic DNA. Translation: AAC77335.1.
AP009048 Genomic DNA. Translation: BAE78371.1.
X00742 Genomic DNA. Translation: CAA25324.1.
X03224 Genomic DNA. Translation: CAA26975.1.
PIRS56606.
RefSeqNP_418799.1. NC_000913.3.
YP_492512.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZYX-ray3.00A/B2-440[»]
1OTPX-ray2.80A2-440[»]
1TPTX-ray2.80A2-440[»]
2TPTX-ray2.60A2-440[»]
4EADX-ray1.50A2-440[»]
4EAFX-ray1.55A2-440[»]
4LHMX-ray1.52A2-440[»]
ProteinModelPortalP07650.
SMRP07650. Positions 1-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9426N.
IntActP07650. 2 interactions.
STRING511145.b4382.

Chemistry

BindingDBP07650.
ChEMBLCHEMBL3726.

Proteomic databases

PaxDbP07650.
PRIDEP07650.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77335; AAC77335; b4382.
BAE78371; BAE78371; BAE78371.
GeneID12933785.
948901.
KEGGecj:Y75_p4266.
eco:b4382.
PATRIC32124380. VBIEscCol129921_4530.

Organism-specific databases

EchoBASEEB0215.
EcoGeneEG10219. deoA.

Phylogenomic databases

eggNOGCOG0213.
HOGENOMHOG000047313.
KOK00758.
OMAFINGVRD.
OrthoDBEOG61ZTGG.
PhylomeDBP07650.

Enzyme and pathway databases

BioCycEcoCyc:DEOA-MONOMER.
ECOL316407:JW4345-MONOMER.
MetaCyc:DEOA-MONOMER.
UniPathwayUPA00578; UER00638.

Gene expression databases

GenevestigatorP07650.

Family and domain databases

Gene3D3.40.1030.10. 1 hit.
3.90.1170.30. 1 hit.
HAMAPMF_01628. Thymid_phosp.
InterProIPR000312. 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]
PANTHERPTHR10515. PTHR10515. 1 hit.
PfamPF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
PF07831. PYNP_C. 1 hit.
[Graphical view]
PIRSFPIRSF000478. TP_PyNP. 1 hit.
SMARTSM00941. PYNP_C. 1 hit.
[Graphical view]
SUPFAMSSF47648. SSF47648. 1 hit.
SSF52418. SSF52418. 1 hit.
SSF54680. SSF54680. 1 hit.
TIGRFAMsTIGR02643. T_phosphoryl. 1 hit.
TIGR02644. Y_phosphoryl. 1 hit.
PROSITEPS00647. THYMID_PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07650.
PROP07650.

Entry information

Entry nameTYPH_ECOLI
AccessionPrimary (citable) accession number: P07650
Secondary accession number(s): Q2M5T5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene