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Sequence of AROG_YEAST

EC Number:2.5.1.54

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3-deoxy-7-phosphoheptulonate synthase
P32449
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
370
39749
Reaction
phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Other sequences found for EC No. 2.5.1.54

General information:

Sequence
show sequence in fasta format
  0 MSESPMFAAN GMPKVNQGAE EDVRILGYDP LASPALLQVQ IPATPTSLET AKRGRREAID
 60 IITGKDDRVL VIVGPCSIHD LEAAQEYALR LKKLSDELKG DLSIIMRAYL EKPRTTVGWK
120 GLINDPDVNN TFNINKGLQS ARQLFVNLTN IGLPIGSEML DTISPQYLAD LVSFGAIGAR
180 TTESQLHREL ASGLSFPVGF KNGTDGTLNV AVDACQAAAH SHHFMGVTKH GVAAITTTKG
240 NEHCFVILRG GKKGTNYDAK SVAEAKAQLP AGSNGLMIDY SHGNSNKDFR NQPKVNDVVC
300 EQIANGENAI TGVMIESNIN EGNQGIPAEG KAGLKYGVSI TDACIGWETT EDVLRKLAAA
360 VRQRREVNKK
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
133857
Kuenzler M.,Paravicini G.,Egli C.,Irniger S.,Braus G.H.
Cloning, primary structure and regulation of the ARO4 gene, encoding the tyrosine-inhibited 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Saccharomyces cerevisiae.
Gene
113
67-74
1992
133859
Doignon F.,Biteau N.,Aigle M.,Crouzet M.
The complete sequence of a 6794 bp segment located on the right arm of chromosome II of Saccharomyces cerevisiae. Finding of a putative dUTPase in a yeast.
Yeast
9
1131-1137
1993
133860
Feldmann H.,Aigle M.,Aljinovic G.,Andre B.,Baclet M.C.,Barthe C.,Baur A.,Becam A.-M.,Biteau N.,Boles E.,Brandt T.,Brendel M.,Brueckner M.,Bussereau F.,Christiansen C.,Contreras R.,Crouzet M.,Cziepluch C.,Demolis N.,Delaveau T.,Doignon F.,Domdey H.,Duesterhus S.,Dubois E.,Dujon B.,El Bakkoury M.,Entian K.-D.,Feuermann M.,Fiers W.,Fobo G.M.,Fritz C.,Gassenhuber J.,Glansdorff N.,Goffeau A.,Grivell L.A.,de Haan M.,Hein C.,Herbert C.J.,Hollenberg C.P.,Holmstroem K.,Jacq C.,Jacquet M.,Jauniaux J.-C.,Jonniaux J.-L.,Kallesoee T.,Kiesau P.,Kirchrath L.,Koetter P.,Korol S.,Liebl S.,Logghe M.,Lohan A.J.E.,Louis E.J.,Li Z.Y.,Maat M.J.,Mallet L.,Mannhaupt G.,Messenguy F.,Miosga T.,Molemans F.,Mueller S.,Nasr F.,Obermaier B.,Perea J.,Pierard A.,Piravandi E.,Pohl F.M.,Pohl T.M.,Potier S.,Proft M.,Purnelle B.,Ramezani Rad M.,Rieger M.,Rose M.,Schaaff-Gerstenschlaeger I.,Scherens B.,Schwarzlose C.,Skala J.,Slonimski P.P.,Smits P.H.M.,Souciet J.-L.,Steensma H.Y.,Stucka R.,Urrestarazu L.A.,van der Aart Q.J.M.,Van Dyck L.,Vassarotti A.,Vetter I.,Vierendeels F.,Vissers S.,Wagner G.,de Wergifosse P.,Wolfe K.H.,Zagulski M.,Zimmermann F.K.,Mewes H.-W.,Kleine K.
Complete DNA sequence of yeast chromosome II.
EMBO J.
13
5795-5809
1994
133861
Engel S.R.,Dietrich F.S.,Fisk D.G.,Binkley G.,Balakrishnan R.,Costanzo M.C.,Dwight S.S.,Hitz B.C.,Karra K.,Nash R.S.,Weng S.,Wong E.D.,Lloyd P.,Skrzypek M.S.,Miyasato S.R.,Simison M.,Cherry J.M.
The reference genome sequence of Saccharomyces cerevisiae: Then and now.
G3 (Bethesda)
4
389-398
2014
133862
Kuenzler M.,Balmelli T.,Egli C.M.,Paravicini G.,Braus G.H.
Cloning, primary structure, and regulation of the HIS7 gene encoding a bifunctional glutamine amidotransferase: cyclase from Saccharomyces cerevisiae.
J. Bacteriol.
175
5548-5558
1993
133863
Ghaemmaghami S.,Huh W.-K.,Bower K.,Howson R.W.,Belle A.,Dephoure N.,O'Shea E.K.,Weissman J.S.
Global analysis of protein expression in yeast.
Nature
425
737-741
2003
133864
Albuquerque C.P.,Smolka M.B.,Payne S.H.,Bafna V.,Eng J.,Zhou H.
A multidimensional chromatography technology for in-depth phosphoproteome analysis.
Mol. Cell. Proteomics
7
1389-1396
2008
133865
Van Damme P.,Lasa M.,Polevoda B.,Gazquez C.,Elosegui-Artola A.,Kim D.S.,De Juan-Pardo E.,Demeyer K.,Hole K.,Larrea E.,Timmerman E.,Prieto J.,Arnesen T.,Sherman F.,Gevaert K.,Aldabe R.
N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
Proc. Natl. Acad. Sci. U.S.A.
109
12449-12454
2012
133866
Hartmann M.,Schneider T.R.,Pfeil A.,Heinrich G.,Lipscomb W.N.,Braus G.H.
Evolution of feedback-inhibited beta/alpha barrel isoenzymes by gene duplication and a single mutation.
Proc. Natl. Acad. Sci. U.S.A.
100
862-867
2003