Sequence of T23O_XANCP
EC Number:1.13.11.11
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
tryptophan 2,3-dioxygenase
Q8PDA8
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
298
34617
Reaction
L-tryptophan + O2 = N-formyl-L-kynurenine
Other sequences found for EC No. 1.13.11.11
General information:
Sequence
0 MPVDKNLRDL EPGIHTDLEG RLTYGGYLRL DQLLSAQQPL SEPAHHDEML FIIQHQTSEL
60 WLKLLAHELR AAIVHLQRDE VWQCRKVLAR SKQVLRQLTE QWSVLETLTP SEYMGFRDVL
120 GPSSGFQSLQ YRYIEFLLGN KNPQMLQVFA YDPAGQARLR EVLEAPSLYE EFLRYLARFG
180 HAIPQQYQAR DWTAAHVADD TLRPVFERIY ENTDRYWREY SLCEDLVDVE TQFQLWRFRH
240 MRTVMRVIGF KRGTGGSSGV GFLQQALALT FFPELFDVRT SVGVDNRPPQ GSADAGKR
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
238458
da Silva A.C.R.,Ferro J.A.,Reinach F.C.,Farah C.S.,Furlan L.R.,Quaggio R.B.,Monteiro-Vitorello C.B.,Van Sluys M.A.,Almeida N.F. Jr.,Alves L.M.C.,do Amaral A.M.,Bertolini M.C.,Camargo L.E.A.,Camarotte G.,Cannavan F.,Cardozo J.,Chambergo F.,Ciapina L.P.,Cicarelli R.M.B.,Coutinho L.L.,Cursino-Santos J.R.,El-Dorry H.,Faria J.B.,Ferreira A.J.S.,Ferreira R.C.C.,Ferro M.I.T.,Formighieri E.F.,Franco M.C.,Greggio C.C.,Gruber A.,Katsuyama A.M.,Kishi L.T.,Leite R.P.,Lemos E.G.M.,Lemos M.V.F.,Locali E.C.,Machado M.A.,Madeira A.M.B.N.,Martinez-Rossi N.M.,Martins E.C.,Meidanis J.,Menck C.F.M.,Miyaki C.Y.,Moon D.H.,Moreira L.M.,Novo M.T.M.,Okura V.K.,Oliveira M.C.,Oliveira V.R.,Pereira H.A.,Rossi A.,Sena J.A.D.,Silva C.,de Souza R.F.,Spinola L.A.F.,Takita M.A.,Tamura R.E.,Teixeira E.C.,Tezza R.I.D.,Trindade dos Santos M.,Truffi D.,Tsai S.M.,White F.F.,Setubal J.C.,Kitajima J.P.
Comparison of the genomes of two Xanthomonas pathogens with differing host specificities.
Nature
417
459-463
2002
238459
Forouhar F.,Anderson J.L.R.,Mowat C.G.,Vorobiev S.M.,Hussain A.,Abashidze M.,Bruckmann C.,Thackray S.J.,Seetharaman J.,Tucker T.,Xiao R.,Ma L.-C.,Zhao L.,Acton T.B.,Montelione G.T.,Chapman S.K.,Tong L.
Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase.
Proc. Natl. Acad. Sci. U.S.A.
104
473-478
2007
238460
Thackray S.J.,Bruckmann C.,Anderson J.L.R.,Campbell L.P.,Xiao R.,Zhao L.,Mowat C.G.,Forouhar F.,Tong L.,Chapman S.K.
Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding.
Biochemistry
47
10677-10684
2008
