Entry Information
Protein Name DeoA
Accession No P07650
Protein description Thymidine phosphorylase
pI/Mw (Da)
Theoretical Experimental
5.21/47207.12 5.15/46004
Protein function and expression Thymidine phosphorylase is part of the pyrimidine salvage pathway.
Reference(s) Champion, K. M., J. C. Nishihara, J. C. Joly, and D. Arnott. 2001. Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes. Proteomics 1:1133-1148. (NCBI)

2D gels information
Map ID38
Reference(s)Champion, K. M., J. C. Nishihara, J. C. Joly, and D. Arnott. 2001. Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes. Proteomics 1:1133-1148. (NCBI)
Protein function and expression(s)Map: A A
pI/Mw: 5.15/46004

A
2-DE profile of E. coli proteins at the end of anti-CD18 blank run fermentation.
Swiss-Prot Database Reference

Entry information
Entry Name TYPH_ECOLI
Primary accession number P07650
Secondary accession numbers Q2M5T5 
Integrated into Swiss-Prot on 1988-04-01
Sequence was last modified on 1995-02-01 (Sequence version 3)
Annotations were last modified on 2006-06-13 (Entry version 68)
Name and origin of the protein
Protein name Thymidine phosphorylase
Synonyms EC 2.4.2.4 Thymidine phosphorylase
TdRPase
Gene name Name : deoA
OrderedLocusName : b4382
SynonymName : tpp
SynonymName : ttg
From Escherichia coli [TaxID:562] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia;
References
[1] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / MG1655 / ATCC 47076
PubMed=7610040[NCBI, ExPASy, EBI, Israel, Japan]
Burland V.D. , Plunkett G. III , Sofia H.J. , Daniels D.L. , Blattner F.R. ,
"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Nucleic Acids Res.23:2105-2119(1995) 
[2] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / MG1655 / ATCC 47076
DOI=10.1126/science.277.5331.1453;PubMed=9278503[NCBI, ExPASy, EBI, Israel, Japan]
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. ,
"The complete genome sequence of Escherichia coli K-12."
Science277:1453-1474(1997) 
[3] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
DOI=10.1038/msb4100049;
Hayashi K. , Morooka N. , Yamamoto Y. , Fujita K. , Isono K. , Choi S. , Ohtsubo E. , Baba T. , Wanner B.L. , Mori H. , Horiuchi T. ,
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Mol. Syst. Biol.2:E1-E5(2006) 
[4] NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-440.
strain = K12
PubMed=6087276[NCBI, ExPASy, EBI, Israel, Japan]
Valentin-Hansen P. , Hammer K. , Larsen J.E.L. , Svendsen I. ,
"The internal regulated promoter of the deo operon of Escherichia coli K-12."
Nucleic Acids Res.12:5211-5224(1984) 
[5] NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.PubMed=6323164[NCBI, ExPASy, EBI, Israel, Japan]
Valentin-Hansen P. , Hammer-Jespersen K. , Boetius F. , Svendsen I. ,
"Structure and function of the intercistronic regulatory deoC-deoA element of Escherichia coli K-12."
EMBO J.3:179-183(1984) 
[6] X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).PubMed=2199449[NCBI, ExPASy, EBI, Israel, Japan]
Walter M.R. , Cook W.J. , Cole L.B. , Short S.A. , Koszalka G.W. , Krenitsky T.A. , Ealick S.E. ,
"Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8-A resolution."
J. Biol. Chem.265:14016-14022(1990) 
[7] X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).DOI=10.1006/jmbi.1998.1941;PubMed=9698549[NCBI, ExPASy, EBI, Israel, Japan]
Pugmire M.J. , Cook W.J. , Jasanoff A. , Walter M.R. , Ealick S.E. ,
"Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase."
J. Mol. Biol.281:285-299(1998) 
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
  • CATALYTIC ACTIVITY : Thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate
  • PATHWAY : Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (II): step 1
  • SUBUNIT : Homodimer
  • SIMILARITY : Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family
  • Copyright
    Copyrighted by the UniProt Consortium, see http://www.uniprot.org/. Distributed under the Creative Commons Attribution-NoDerivs License.
    Cross-reference
    Sequence databases
    EMBL U14003;AAA97278.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U00096;AAC77335.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    AP009048;BAE78371.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    X00742;CAA25324.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    X03224;CAA26975.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    PIR S56606;S56606.
    3D structure databases
    PDB 1AZY;X-ray;A/B=2-440[ExPASy/RCSB/EBI].
    1OTP;X-ray;@=2-440[ExPASy/RCSB/EBI].
    1TPT;X-ray;@=2-440[ExPASy/RCSB/EBI].
    2TPT;X-ray;@=2-440[ExPASy/RCSB/EBI].
    Detailed list of linked structures
    ModBase P07650
    Protein-protein interaction databases
    DIP P07650
    Enzyme and pathway databases
    BioCyc EcoCyc:DEOA-MONOMER;-.
    2D gel databases
    SWISS-2DPAGE Get region on 2D PAGE
    Organism-specific gene databases
    EchoBASE EB0215;-.
    EcoGene EG10219;deoA.
    HOGENOM [Family / Alignment / Tree]
    Family and domain databases
    HAMAP MF_01628-;1.
    PBIL [Family/Alignment/Tree]
    InterPro IPR000312;Glyco_trans_3.
    IPR013102;PYNP_C.
    IPR000053;Pyrmidine_PPase.
    IPR013465;Thymidine_Pase.
    Graphical view of domain structure
    Pfam PF02885;Glycos_trans_3N;1.
    PF00591;Glycos_transf_3;1.
    PF07831;PYNP_C;1.
    Pfam graphical view of domain structure
    PIRSF PIRSF000478;TP_PyNP;1.
    ProDom PD001864;Glyco_trans_3;1.
    [Domain structure / List of seq. sharing at least 1 domain]
    TIGRFAMs TIGR02643;T_phosphoryl;1.
    TIGR02644;Y_phosphoryl;1.
    BLOCKS P07650
    PROSITE PS00647;THYMID_PHOSPHORYLASE;1.
    Genome annotation databases
    GenomeReviews U00096_GR;b4382.
    Other
    LinkHub P07650;-.
    ProtoNet P07650
    UniRef View cluster of proteins with at least 50% / 90% / 100% identity
    Keyword
    3D-structure; Complete proteome; Glycosyltransferase; Transferase;
    Features
    Feature table viewer Feature aligner
    Key  From   To Length  Description  FTId
    CHAIN    1   440    440  Thymidine phosphorylase  PRO_0000059054
    HELIX    4    12      9    
    TURN   13    14      2    
    HELIX   19    30     12    
    TURN   31    32      2    
    STRAND   34    34      1    
    HELIX   36    49     14    
    HELIX   53    65     13    
    TURN   66    66      1    
    STRAND   67    68      2    
    TURN   73    76      4    
    STRAND   78    79      2    
    STRAND   81    86      6    
    STRAND   90    91      2    
    HELIX   94   104     11    
    TURN  105   106      2    
    STRAND  108   113      6    
    TURN  118   119      2    
    STRAND  120   120      1    
    HELIX  123   127      5    
    TURN  128   129      2    
    STRAND  130   130      1    
    TURN  131   132      2    
    STRAND  135   135      1    
    HELIX  139   148     10    
    TURN  149   149      1    
    STRAND  150   155      6    
    TURN  158   159      2    
    STRAND  160   161      2    
    HELIX  162   173     12    
    TURN  174   175      2    
    HELIX  180   192     13    
    TURN  193   194      2    
    STRAND  197   206     10    
    TURN  207   208      2    
    STRAND  209   213      5    
    HELIX  214   230     17    
    TURN  231   232      2    
    STRAND  234   241      8    
    STRAND  243   244      2    
    STRAND  246   248      3    
    STRAND  250   252      3    
    HELIX  253   263     11    
    TURN  264   265      2    
    STRAND  266   266      1    
    HELIX  270   286     17    
    TURN  287   288      2    
    STRAND  289   289      1    
    STRAND  291   292      2    
    HELIX  293   305     13    
    TURN  306   306      1    
    STRAND  307   307      1    
    HELIX  308   319     12    
    TURN  320   321      2    
    TURN  324   325      2    
    HELIX  326   333      8    
    STRAND  334   334      1    
    STRAND  338   343      6    
    STRAND  346   347      2    
    STRAND  349   354      6    
    HELIX  356   366     11    
    TURN  367   368      2    
    STRAND  369   369      1    
    STRAND  371   372      2    
    TURN  373   374      2    
    STRAND  379   380      2    
    STRAND  382   385      4    
    TURN  389   390      2    
    STRAND  392   394      3    
    TURN  395   396      2    
    STRAND  397   397      1    
    STRAND  399   406      8    
    HELIX  407   420     14    
    STRAND  421   426      6    
    STRAND  433   438      6    
    Sequence information
    Length: 440AA [This is the length of the unprocessed precursor] Molecular weight: 47207Da [This is the MW of the unprocessed precursor] CRC64: 1DB3083C9275D2ED[This is a checksum on the sequence]
            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 
    P07650 in FASTA format