Sequence of TYPH_ECOLI
EC Number:2.4.2.4
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate
Other sequences found for EC No. 2.4.2.4
General information:
Sequence
0 MFLAQEIIRK KRDGHALSDE EIRFFINGIR DNTISEGQIA ALAMTIFFHD MTMPERVSLT
60 MAMRDSGTVL DWKSLHLNGP IVDKHSTGGV GDVTSLMLGP MVAACGGYIP MISGRGLGHT
120 GGTLDKLESI PGFDIFPDDN RFREIIKDVG VAIIGQTSSL APADKRFYAT RDITATVDSI
180 PLITASILAK KLAEGLDALV MDVKVGSGAF MPTYELSEAL AEAIVGVANG AGVRTTALLT
240 DMNQVLASSA GNAVEVREAV QFLTGEYRNP RLFDVTMALC VEMLISGKLA KDDAEARAKL
300 QAVLDNGKAA EVFGRMVAAQ KGPTDFVENY AKYLPTAMLT KAVYADTEGF VSEMDTRALG
360 MAVVAMGGGR RQASDTIDYS VGFTDMARLG DQVDGQRPLA VIHAKDENNW QEAAKAVKAA
420 IKLADKAPES TPTVYRRISE
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
496872
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
496873
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.
Science
277
1453-1462
1997
496874
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
0-0
2006
496875
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
496876
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
496877
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
496878
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
