Sequence of XDH1_ARATH
EC Number:1.17.1.4
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
xanthine + NAD+ + H2O = urate + NADH + H+
Other sequences found for EC No. 1.17.1.4
General information:
Sequence
0 MGSLKKDGEI GDEFTEALLY VNGVRRVLPD GLAHMTLLEY LRDLGLTGTK LGCGEGGCGA
60 CTVMVSSYDR KSKTSVHYAV NACLAPLYSV EGMHVISIEG LGHRKLGLHP VQESLASSHG
120 SQCGFCTPGF IMSMYSLLRS SKNSPSEEEI EECLAGNLCR CTGYRPIVDA FRVFAKSDDA
180 LYCGVSSLSL QDGSTICPST GKPCSCGSKT TNEVASCNED RFQSISYSDI DGAKYTDKEL
240 IFPPELLLRK LTPLKLRGNG GITWYRPVCL QNLLELKANY PDAKLLVGNT EVGIEMRLKR
300 LQYQVLISVA QVPELNALNV NDNGIEVGSA LRLSELLRLF RKIVKERPAH ETSACKAFIE
360 QLKWFAGTQI RNVACIGGNI CTASPISDLN PLWMASRAEF RITNCNGDVR SIPAKDFFLG
420 YRKVDMGSNE ILLSVFLPWT RPLEYVKEFK QAHRRDDDIA IVNGGMRVFL EDKGQQLFVS
480 DASIAYGGVA PLSLCARKTE EFLIGKNWNK DLLQDALKVI QSDVVIKEDA PGGMVEFRKS
540 LTLSFFFKFF LWVSHNVNNA NSAIETFPPS HMSAVQPVPR LSRIGKQDYE TVKQGTSVGS
600 SEVHLSARMQ VTGEAEYTDD TPVPPNTLHA AFVLSKVPHA RILSIDDSAA KSSSGFVGLF
660 LAKDIPGDNM IGPIVPDEEL FATDVVTCVG QVIGVVVADT HENAKTAAGK VDVRYEELPA
720 ILSIKEAINA KSFHPNTEKR LRKGDVELCF QSGQCDRVIE GEVQMGGQEH FYLEPNGSLV
780 WTVDGGSEVH MISSTQAPQK HQKYVSHVLG LPMSKVVCKT KRIGGGFGGK ETRSAFIAAA
840 ASVPSYLLNR PVKLILDRDV DMMITGHRHS FLGKYKVGFT NEGKILALDL EIYNNGGNSL
900 DLSLSVLERA MFHSDNVYEI PHVRIVGNVC FTNFPSNTAF RGFGGPQGML ITENWIQRIA
960 AELNKSPEEI KEMNFQVEGS VTHYCQTLQH CTLHQLWKEL KVSCNFLKAR READEFNSHN
1020 RWKKRGVAMV PTKFGISFTT KFMNQAGALV HVYTDGTVLV THGGVEMGQG LHTKVAQVAA
1080 SAFNIPLSSV FVSETSTDKV PNASPTAASA SSDMYGAAVL DACEQIIARM EPVASKHNFN
1140 TFTELVSACY FQRIDLSAHG FHIVPDLGFD WISGKGNAFR YYTYGAAFAE VEIDTLTGDF
1200 HTRAADIMLD LGYSLNPAID VGQIEGAFVQ GLGWVALEEL KWGDAAHKWI KPGSLLTCGP
1260 GNYKIPSIND MPFNLNVSLL KGNPNTKAIH SSKAVGEPPF FLASSVFFAI KEAIKAARTE
1320 VGLTDWFPLE SPATPERIRM ACFDEFSAPF VNSDFYPNLS V
Download this sequence
Download all sequences for 1.17.1.4
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
118540
Hesberg C.,Haensch R.,Mendel R.R.,Bittner F.
Tandem orientation of duplicated xanthine dehydrogenase genes from Arabidopsis thaliana: differential gene expression and enzyme activities.
J. Biol. Chem.
279
13547-13554
2004
118541
Mayer K.F.X.,Schueller C.,Wambutt R.,Murphy G.,Volckaert G.,Pohl T.,Duesterhoeft A.,Stiekema W.,Entian K.-D.,Terryn N.,Harris B.,Ansorge W.,Brandt P.,Grivell L.A.,Rieger M.,Weichselgartner M.,de Simone V.,Obermaier B.,Mache R.,Mueller M.,Kreis M.,Delseny M.,Puigdomenech P.,Watson M.,Schmidtheini T.,Reichert B.,Portetelle D.,Perez-Alonso M.,Boutry M.,Bancroft I.,Vos P.,Hoheisel J.,Zimmermann W.,Wedler H.,Ridley P.,Langham S.-A.,McCullagh B.,Bilham L.,Robben J.,van der Schueren J.,Grymonprez B.,Chuang Y.-J.,Vandenbussche F.,Braeken M.,Weltjens I.,Voet M.,Bastiaens I.,Aert R.,Defoor E.,Weitzenegger T.,Bothe G.,Ramsperger U.,Hilbert H.,Braun M.,Holzer E.,Brandt A.,Peters S.,van Staveren M.,Dirkse W.,Mooijman P.,Klein Lankhorst R.,Rose M.,Hauf J.,Koetter P.,Berneiser S.,Hempel S.,Feldpausch M.,Lamberth S.,Van den Daele H.,De Keyser A.,Buysshaert C.,Gielen J.,Villarroel R.,De Clercq R.,van Montagu M.,Rogers J.,Cronin A.,Quail M.A.,Bray-Allen S.,Clark L.,Doggett J.,Hall S.,Kay M.,Lennard N.,McLay K.,Mayes R.,Pettett A.,Rajandream M.A.,Lyne M.,Benes V.,Rechmann S.,Borkova D.,Bloecker H.,Scharfe M.,Grimm M.,Loehnert T.-H.,Dose S.,de Haan M.,Maarse A.C.,Schaefer M.,Mueller-Auer S.,Gabel C.,Fuchs M.,Fartmann B.,Granderath K.,Dauner D.,Herzl A.,Neumann S.,Argiriou A.,Vitale D.,Liguori R.,Piravandi E.,Massenet O.,Quigley F.,Clabauld G.,Muendlein A.,Felber R.,Schnabl S.,Hiller R.,Schmidt W.,Lecharny A.,Aubourg S.,Chefdor F.,Cooke R.,Berger C.,Monfort A.,Casacuberta E.,Gibbons T.,Weber N.,Vandenbol M.,Bargues M.,Terol J.,Torres A.,Perez-Perez A.,Purnelle B.,Bent E.,Johnson S.,Tacon D.,Jesse T.,Heijnen L.,Schwarz S.,Scholler P.,Heber S.,Francs P.,Bielke C.,Frishman D.,Haase D.,Lemcke K.,Mewes H.-W.,Stocker S.,Zaccaria P.,Bevan M.,Wilson R.K.,de la Bastide M.,Habermann K.,Parnell L.,Dedhia N.,Gnoj L.,Schutz K.,Huang E.,Spiegel L.,Sekhon M.,Murray J.,Sheet P.,Cordes M.,Abu-Threideh J.,Stoneking T.,Kalicki J.,Graves T.,Harmon G.,Edwards J.,Latreille P.,Courtney L.,Cloud J.,Abbott A.,Scott K.,Johnson D.,Minx P.,Bentley D.,Fulton B.,Miller N.,Greco T.,Kemp K.,Kramer J.,Fulton L.,Mardis E.,Dante M.,Pepin K.,Hillier L.W.,Nelson J.,Spieth J.,Ryan E.,Andrews S.,Geisel C.,Layman D.,Du H.,Ali J.,Berghoff A.,Jones K.,Drone K.,Cotton M.,Joshu C.,Antonoiu B.,Zidanic M.,Strong C.,Sun H.,Lamar B.,Yordan C.,Ma P.,Zhong J.,Preston R.,Vil D.,Shekher M.,Matero A.,Shah R.,Swaby I.K.,O'Shaughnessy A.,Rodriguez M.,Hoffman J.,Till S.,Granat S.,Shohdy N.,Hasegawa A.,Hameed A.,Lodhi M.,Johnson A.,Chen E.,Marra M.A.,Martienssen R.,McCombie W.R.
Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.
Nature
402
769-777
1999
118542
Cheng C.Y.,Krishnakumar V.,Chan A.P.,Thibaud-Nissen F.,Schobel S.,Town C.D.
Araport11: a complete reannotation of the Arabidopsis thaliana reference genome.
Plant J.
89
789-804
2017
118543
Yesbergenova Z.,Yang G.,Oron E.,Soffer D.,Fluhr R.,Sagi M.
The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have distinct reactive oxygen species signatures and are induced by drought and abscisic acid.
Plant J.
42
862-876
2005
118544
Nakagawa A.,Sakamoto S.,Takahashi M.,Morikawa H.,Sakamoto A.
The RNAi-mediated silencing of xanthine dehydrogenase impairs growth and fertility and accelerates leaf senescence in transgenic Arabidopsis plants.
Plant Cell Physiol.
48
1484-1495
2007
118545
Brychkova G.,Alikulov Z.,Fluhr R.,Sagi M.
A critical role for ureides in dark and senescence-induced purine remobilization is unmasked in the Atxdh1 Arabidopsis mutant.
Plant J.
54
496-509
2008
118546
Watanabe S.,Nakagawa A.,Izumi S.,Shimada H.,Sakamoto A.
RNA interference-mediated suppression of xanthine dehydrogenase reveals the role of purine metabolism in drought tolerance in Arabidopsis.
FEBS Lett.
584
1181-1186
2010
118547
Zarepour M.,Kaspari K.,Stagge S.,Rethmeier R.,Mendel R.R.,Bittner F.
Xanthine dehydrogenase AtXDH1 from Arabidopsis thaliana is a potent producer of superoxide anions via its NADH oxidase activity.
Plant Mol. Biol.
72
301-310
2010